Hydrolase Protein | ABHD | ACY1 | ENTPD3 | BLMH

Hydrolase

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Name :
HAGH Human

Description:

Hydroxyacylglutathione Hydrolase Human Recombinant

GLX2, Glyoxalase II, GLO2, Hydroxyacyl Glutathione Hydrolase, HAGH1, GLXII, Hydroxyacylglutathione Hydrolase, hydroxyacylglutathione hydroxylase.

Product # :
ENZ-034

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Description

HAGH produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (1-260a.a.) and having a molecular mass of 31.4kDa.HAGH is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The HAGH protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl Buffer (pH 8.5) and 10% Glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
HAGH is a part of the glyoxalase family and a thiolesterase which hydrolyses S-lactoyl-glutathione to reduced glutathione and D-lactate. HAGH protein is a detoxifying enzyme of glycolysis byproduct methylglyoxal and a target of p63 and p73 and serves as a pro-survival factor of the p53 family. HAGH appears only as a monomer and binds two zinc ions per subunit.

Synonyms
GLX2, Glyoxalase II, GLO2, Hydroxyacyl Glutathione Hydrolase, HAGH1, GLXII, Hydroxyacylglutathione Hydrolase, hydroxyacylglutathione hydroxylase.

Physical Appearance
Sterile Filtered clear solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.

Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMKVEVL PALTDNYMYL VIDDETKEAA IVDPVQPQKV VDAARKHGVK LTTVLTTHHH WDHAGGNEKL VKLESGLKVY GGDDRIGALT HKITHLSTLQ VGSLNVKCLA TPCHTSGHIC YFVSKPGGSE PPAVFTGDTL FVAGCGKFYE GTADEMCKAL LEVLGRLPPD TRVYCGHEYT INNLKFARHV EPGNAAIREK LAWAKEKYSI GEPTVPSTLA EEFTYNPFMR VREKTVQQHA GETDPVTTMR AVRREKDQFK MPRD.

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Name :
PTRHD1 Human

Description:

Peptidyl-TRNA Hydrolase Domain Containing 1 Human Recombinant

C2orf79, Putative peptidyl-tRNA hydrolase PTRHD1, Peptidyl-tRNA hydrolase domain-containing protein 1, PTRHD1.

Product # :
ENZ-826

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PTRHD1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (1-140 a.a) and having a molecular mass of 18.2kDa.PTRHD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PTRHD1 protein solution (1mg/ml) containing Phosphate buffer saline (pH 7.4), 30% glycerol and 1mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Putative peptidyl-tRNA hydrolase PTRHD1 (PTRHD1) is a 140 amino acid protein, which is encoded by a gene located on human chromosome 2p23.3. Chromosome 2 is the second largest human chromosome; it consists of 237 million bases, encodes over 1,400 genes and makes up approximately 8% of the human genome. Several genetic diseases are linked to genes on chromosome 2.

Synonyms
C2orf79, Putative peptidyl-tRNA hydrolase PTRHD1, Peptidyl-tRNA hydrolase domain-containing protein 1, PTRHD1.

Physical Appearance
Sterile Filtered colorless solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMHRGVGP AFRVVRKMAA SGAEPQVLVQ YLVLRKDLSQ APFSWPAGAL VAQACHAATA ALHTHRDHPH TAAYLQELGR MRKVVLEAPD ETTLKELAET LQQKNIDHML WLEQPENIAT CIALRPYPKE EVGQYLKKFR LFK.

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Name :
PTRH2 Human

Description:

Peptidyl-tRNA Hydrolase 2 Human Recombinant

Peptidyl-tRNA hydrolase 2, mitochondrial, PTH 2, Bcl-2 inhibitor of transcription 1, PTRH2, BIT1, PTH2, CGI-147, FLJ32471, PTRH2.

Product # :
ENZ-045

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PTRH2 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 137 amino acids (64-179 a.a.) and having a molecular mass of 14.9kDa. The PTRH2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PTRH2 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Peptidyl-tRNA hydrolase 2 (PTRH2) is a mitochondrial protein. PTRH2 is released during apoptosis from the mitochondria to the cytoplasm. When in the cytoplasm, PTRH2 regulates the function of 2 transcriptional regulators, TLE5 and TLE1, thus promoting caspase-independent cell death. Natural substrates for PTRH2 may be petidyl-tRNAs which drop off the ribosome during protein synthesis.

Synonyms
Peptidyl-tRNA hydrolase 2, mitochondrial, PTH 2, Bcl-2 inhibitor of transcription 1, PTRH2, BIT1, PTH2, CGI-147, FLJ32471, PTRH2.

Physical Appearance
Sterile Filtered colorless solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEYKMILVVR NDLKMGKGKV AAQCSHAAVS AYKQIQRRNP EMLKQWEYCG QPKVVVKAPD EETLIALLAH AKMLGLTVSL IQDAGRTQIA PGSQTVLGIG PGPADLIDKV TGHLKLY.

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Name :
LTA4H Human

Description:

Leukotriene A4 Hydrolase Human Recombinant

Leukotriene A-4 hydrolase isoform1, LTA-4 hydrolase, Leukotriene A(4) hydrolase, LTA4.

Product # :
ENZ-869

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LTA4H Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 634 amino acids (1-611 a.a) and having a molecular mass of 71.7kDa.LTA4H is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

LTA4H protein solution (0.25mg/ml) in Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Leukotriene A-4 hydrolase (LTA4H) is a bifunctional enzyme that converts leukotriene A4 to leukotriene B4 and functions as an aminopeptidase. The LTA4H enzyme is a member of the family of hydrolases, specifically those acting on ether bonds (ether hydrolases). LTA4H participates in arachidonic acid metabolism.

Synonyms
Leukotriene A-4 hydrolase isoform1, LTA-4 hydrolase, Leukotriene A(4) hydrolase, LTA4.

Physical Appearance
Sterile Filtered colorless solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPEIVDT CSLASPASVC RTKHLHLRCS VDFTRRTLTG TAALTVQSQE DNLRSLVLDT KDLTIEKVVI NGQEVKYALG ERQSYKGSPM EISLPIALSK NQEIVIEISF ETSPKSSALQ WLTPEQTSGK EHPYLFSQCQ AIHCRAILPC QDTPSVKLTY TAEVSVPKEL VALMSAIRDG ETPDPEDPSR KIYKFIQKVP IPCYLIALVV GALESRQIGP RTLVWSEKEQ VEKSAYEFSE TESMLKIAED LGGPYVWGQY DLLVLPPSFP YGGMENPCLT FVTPTLLAGD KSLSNVIAHE ISHSWTGNLV TNKTWDHFWL NEGHTVYLER HICGRLFGEK FRHFNALGGW GELQNSVKTF GETHPFTKLV VDLTDIDPDV AYSSVPYEKG FALLFYLEQL LGGPEIFLGF LKAYVEKFSY KSITTDDWKD FLYSYFKDKV DVLNQVDWNA WLYSPGLPPI KPNYDMTLTN ACIALSQRWI TAKEDDLNSF NATDLKDLSS HQLNEFLAQT LQRAPLPLGH IKRMQEVYNF NAINNSEIRF RWLRLCIQSK WEDAIPLALK MATEQGRMKF TRPLFKDLAA FDKSHDQAVR TYQEHKASMH PVTAMLVGKD LKVD.

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Name :
GGH Human

Description:

Gamma-Glutamyl Hydrolase Human Recombinant

Gamma-glutamyl hydrolase (conjugase, folylpolygammaglutamyl hydrolase), Gamma-Glu-X carboxypeptidase, gamma-glutamyl hydrolase, Conjugase, GH, EC 3.4.19.9.

Product # :
ENZ-242

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GGH Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (25-318) and having a molecular mass of 35.9kDa.GGH is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The GGH solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
GGH is a homodimeric protein which catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates. GGH is a vital enzyme in folyl and antifolyl poly-gamma-glutamate metabolism and it has a significant part in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of antifolates and pteroylpolyglutamates.

Synonyms
Gamma-glutamyl hydrolase (conjugase, folylpolygammaglutamyl hydrolase), Gamma-Glu-X carboxypeptidase, gamma-glutamyl hydrolase, Conjugase, GH, EC 3.4.19.9.

Physical Appearance
Sterile Filtered colorless solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MRPHGDTAKK PIIGILMQKC RNKVMKNYGR YYIAASYVKY LESAGARVVP VRLDLTEKDY EILFKSINGI LFPGGSVDLR RSDYAKVAKI FYNLSIQSFD DGDYFPVWGT CLGFEELSLL ISGECLLTAT DTVDVAMPLN FTGGQLHSRM FQNFPTELLL SLAVEPLTAN FHKWSLSVKN FTMNEKLKKF FNVLTTNTDG KIEFISTMEG YKYPVYGVQW HPEKAPYEWK NLDGISHAPN AVKTAFYLAE FFVNEARKNN HHFKSESEEE KALIYQFSPI YTGNISSFQQ CYIFD

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Name :
FUCA2 Human

Description:

Fucosidase Alpha-L- 2 Plasma Human Recombinant

Fucosidase, alpha-L- 2, plasma, dJ20N2.5, RP1-20N2.5, Plasma alpha-L-fucosidase, Alpha-L-fucoside fucohydrolase 2, Alpha-L-fucosidase 2, PSEC0151, UNQ227/PRO260.

Product # :
ENZ-840

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FUCA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 462 amino acids (29-467 a.a) and having a molecular mass of 53.3kDa.FUCA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FUCA2 protein solution (1mg/ml) containing 20mM phosphate (pH8.0) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Fucosidase Alpha-L- 2 Plasma (FUCA2) is a plasma alpha-L-fucosidase, which represents 10-20% of the total cellular fucosidase activity. FUCA2 protein belongs to the glycosyl hydrolase 29 family, and catalyzes the hydrolysis of the alpha-1,6-linked fucose fused to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. FUCA2 is crucial for Helicobacter pylori adhesion to human gastric cancer cells.

Synonyms
Fucosidase, alpha-L- 2, plasma, dJ20N2.5, RP1-20N2.5, Plasma alpha-L-fucosidase, Alpha-L-fucoside fucohydrolase 2, Alpha-L-fucosidase 2, PSEC0151, UNQ227/PRO260.

Physical Appearance
Sterile Filtered colorless solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHSATRFD PTWESLDARQ LPAWFDQAKF GIFIHWGVFS VPSFGSEWFW WYWQKEKIPK YVEFMKDNYP PSFKYEDFGP LFTAKFFNAN QWADIFQASG AKYIVLTSKH HEGFTLWGSE YSWNWNAIDE GPKRDIVKEL EVAIRNRTDL RFGLYYSLFE WFHPLFLEDE SSSFHKRQFP VSKTLPELYE LVNNYQPEVL WSDGDGGAPD QYWNSTGFLA WLYNESPVRG TVVTNDRWGA GSICKHGGFY TCSDRYNPGH LLPHKWENCM TIDKLSWGYR REAGISDYLT IEELVKQLVE TVSCGGNLLM NIGPTLDGTI SVVFEERLRQ MGSWLKVNGE AIYETHTWRS QNDTVTPDVW YTSKPKEKLV YAIFLKWPTS GQLFLGHPKA ILGATEVKLL GHGQPLNWIS LEQNGIMVEL PQLTIHQMPC KWGWALALTN VI.

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Name :
FUCA1 Human

Description:

Fucosidase Alpha-L- 1 Plasma Human Recombinant

Fucosidase, Alpha-L- 1, Tissue, Alpha-L-Fucoside Fucohydrolase 1, Alpha-L-Fucosidase 1, Alpha-L-Fucosidase I, EC 3.2.1.51, Tissue Alpha-L-Fucosidase, EC 3.2.1, FUCA, Tissue alpha-L-fucosidase.

Product # :
ENZ-921

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FUCA1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 445 amino acids (28-466a.a.) and having a molecular mass of 51.7kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). FUCA1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

FUCA1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Fucosidase Alpha-L- 1 Plasma, also known as FUCA1 is a member of the glycosyl hydrolase 29 family which is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Fucosidosis is an autosomal recessive lysosomal storage disease caused by the absence of alpha-L-fucosidase activity.

Synonyms
Fucosidase, Alpha-L- 1, Tissue, Alpha-L-Fucoside Fucohydrolase 1, Alpha-L-Fucosidase 1, Alpha-L-Fucosidase I, EC 3.2.1.51, Tissue Alpha-L-Fucosidase, EC 3.2.1, FUCA, Tissue alpha-L-fucosidase.

Physical Appearance
Sterile Filtered colorless solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
VRRAQPPRRY TPDWPSLDSR PLPAWFDEAK FGVFIHWGVF SVPAWGSEWF WWHWQGEGRP QYQRFMRDNY PPGFSYADFG PQFTARFFHP EEWADLFQAA GAKYVVLTTK HHEGFTNWPS PVSWNWNSKD VGPHRDLVGE LGTALRKRNI RYGLYHSLLE WFHPLYLLDK KNGFKTQHFV SAKTMPELYD LVNSYKPDLI WSDGEWECPD TYWNSTNFLS WLYNDSPVKD EVVVNDRWGQ NCSCHHGGYY NCEDKFKPQS LPDHKWEMCT SIDKFSWGYR RDMALSDVTE ESEIISELVQ TVSLGGNYLL NIGPTKDGLI VPIFQERLLA VGKWLSINGE AIYASKPWRV QWEKNTTSVW YTSKGSAVYA IFLHWPENGV LNLESPITTS TTKITMLGIQ GDLKWSTDPD KGLFISLPQL PPSAVPAEFA WTIKLTGVKH HHHHH.

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Name :
FOLH1 Mouse

Description:

Folate Hydrolase 1 Mouse Recombinant

Folh1, GCP2, mopsm, Glutamate carboxypeptidase 2, Folate hydrolase 1, Folylpoly-gamma-glutamate carboxypeptidase, FGCP, Glutamate carboxypeptidase II, GCPII, Naalad1.

Product # :
ENZ-957

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FOLH1 Mouse Recombinant produced in in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 717 amino acids (45-752a.a) and having a molecular mass of 80.5kDa (Migrates at 70-100kDa on SDS-PAGE under reducing conditions). FOLH1 is fused to a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The FOLH1 solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Folate Hydrolase 1 (Folh1) is a single pass type 2 membrane protein which is expressed mainly in prostate epithelium. Folh1 which is a part of the peptidase M28 family and M28B subfamily has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase activity. Folh1 can be found in urinary bladder, kidney, testis, ovary, stomach, small intestine colon, and the capillary endothelium of various tumors. Therefore, Folh1 plays a role in directed imaging and therapy of recurrent of metastatic disease.

Synonyms
Folh1, GCP2, mopsm, Glutamate carboxypeptidase 2, Folate hydrolase 1, Folylpoly-gamma-glutamate carboxypeptidase, FGCP, Glutamate carboxypeptidase II, GCPII, Naalad1.

Physical Appearance
Sterile Filtered colorless solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
ADPKPSNEAT GNVSHSGMKK EFLHELKAEN IKKFLYNFTR TPHLAGTQNN FELAKQIHDQ WKEFGLDLVE LSHYDVLLSY PNKTHPNYIS IINEDGNEIF KTSLSEQPPP GYENISDVVP PYSAFSPQGT PEGDLVYVNY ARTEDFFKLE REMKISCSGK IVIARYGKVF RGNMVKNAQL AGAKGMILYS DPADYFVPAV KSYPDGWNLP GGGVQRGNVL NLNGAGDPLT PGYPANEHAY RHELTNAVGL PSIPVHPIGY DDAQKLLEHM GGPAPPDSSW KGGLKVPYNV GPGFAGNFST QKVKMHIHSY TKVTRIYNVI GTLKGALEPD RYVILGGHRD AWVFGGIDPQ SGAAVVHEIV RSFGTLKKKG RRPRRTILFA SWDAEEFGLL GSTEWAEEHS RLLQERGVAY INADSSIEGN YTLRVDCTPL MYSLVYNLTK ELQSPDEGFE GKSLYDSWKE KSPSPEFIGM PRISKLGSGN DFEVFFQRLG IASGRARYTK NWKTNKVSSY PLYHSVYETY ELVVKFYDPT FKYHLTVAQV RGAMVFELAN SIVLPFDCQS YAVALKKYAD TIYNISMKHP QEMKAYMISF DSLFSAVNNF TDVASKFNQR LQELDKSNPI LLRIMNDQLM YLERAFIDPL GLPGRPFYRH IIYAPSSHNK YAGESFPGIY DALFDISSKV NASKAWNEVK RQISIATFTV QAAAETLREV AHHHHHH.

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Name :
FOLH1 Human

Description:

Folate Hydrolase 1 Human Recombinant

Glutamate carboxypeptidase 2 isoform 1,Cell growth-inhibiting gene 27 protein, Folate hydrolase 1, Folylpolygamma-glutamate carboxypeptidase, Glutamate carboxypeptidase II, Membrane glutamate carboxypeptidase, Nacetylated-alpha-linked acidic dipeptidase I, Prostate-specific membrane antigen, Pteroylpoly-gamma glutamate carboxypeptidase, Folh1, FGCP, FOLH, GCP2, GCPII, mGCP, NAALAD1, NAALAdase, PSM, PSMA

Product # :
ENZ-1170

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Description

FOLH1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 717 amino acids (44-750 a.a) and having a molecular mass of 80.7kDa.FOLH1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

FOLH1 protein solution (0.25mg/ml) contains Phosphate buffered saline (pH 7.4) and 20% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
FOLH1, also known as glutamate carboxypeptidase 2 (GCPII), is a single pass type 2 membrane protein which belongs to the peptidase M28 family. FOLH1 is highly produced in prostate epithelium. FOLH1 is also found in ovary, live, stomach, small intestine colon, urinary bladder, kidney, testis, and the capillary endothelium of a variety of tumours. Therefore, it plays a role in directed imaging and therapy of recurrent of metastatic disease. FOLH1 is a zinc metalloenzyme that resides in membranes and catalyses the hydrolysis of N-acetylaspartylglutamate to glutamate and N-acetylaspartate.

Synonyms
Glutamate carboxypeptidase 2 isoform 1,Cell growth-inhibiting gene 27 protein, Folate hydrolase 1, Folylpolygamma-glutamate carboxypeptidase, Glutamate carboxypeptidase II, Membrane glutamate carboxypeptidase, Nacetylated-alpha-linked acidic dipeptidase I, Prostate-specific membrane antigen, Pteroylpoly-gamma glutamate carboxypeptidase, Folh1, FGCP, FOLH, GCP2, GCPII, mGCP, NAALAD1, NAALAdase, PSM, PSMA

Physical Appearance
Sterile Filtered colorless solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
ADPMKSSNEA TNITPKHNMK AFLDELKAEN IKKFLYNFTQ IPHLAGTEQN FQLAKQIQSQ WKEFGLDSVE LAHYDVLLSY PNKTHPNYIS IINEDGNEIF NTSLFEPPPP GYENVSDIVP PFSAFSPQGM PEGDLVYVNY ARTEDFFKLE RDMKINCSGK IVIARYGKVF RGNKVKNAQL AGAKGVILYS DPADYFAPGV KSYPDGWNLP GGGVQRGNIL NLNGAGDPLT PGYPANEYAY RRGIAEAVGL PSIPVHPIGY YDAQKLLEKM GGSAPPDSSW RGSLKVPYNV GPGFTGNFST QKVKMHIHST NEVTRIYNVI GTLRGAVEPD RYVILGGHRD SWVFGGIDPQ SGAAVVHEIV RSFGTLKKEG WRPRRTILFA SWDAEEFGLL GSTEWAEENS RLLQERGVAY INADSSIEGN YTLRVDCTPL MYSLVHNLTK ELKSPDEGFE GKSLYESWTK KSPSPEFSGM PRISKLGSGN DFEVFFQRLG IASGRARYTK NWETNKFSGY PLYHSVYETY ELVEKFYDPM FKYHLTVAQV RGGMVFELAN SIVLPFDCRD YAVVLRKYAD KIYSISMKHP QEMKTYSVSF DSLFSAVKNF TEIASKFSER LQDFDKSNPI VLRMMNDQLM FLERAFIDPL GLPDRPFYRH VIYAPSSHNK YAGESFPGIY DALFDIESKV DPSKAWGEVK RQIYVAAFTV QAAAETLSEV AHHHHHH

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Name :
FAHD1 Human

Description:

Fumarylacetoacetate Hydrolase Domain Containing 1 Human Recombinant

Fumarylacetoacetate hydrolase domain-containing protein 1, YisK-like protein, FAHD1, C16orf36, YISKL, MGC74876, DKFZp566J2046.

Product # :
ENZ-067

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FAHD1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 244 amino acids (1-224 a.a.) and having a molecular mass of 27kDa. The FAHD1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The FAHD1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Fumarylacetoacetate hydrolase domain-containing protein 1 (FAHD1) is a member of the FAH family. FAHD1 is considered to have hydrolase activity and it uses Magnesium and Calcium as cofactors. It seems quite likely that the metal binding sites are involved in an enzymatic activity connected to the catabolism of aromatic amino acids.

Synonyms
Fumarylacetoacetate hydrolase domain-containing protein 1, YisK-like protein, FAHD1, C16orf36, YISKL, MGC74876, DKFZp566J2046.

Physical Appearance
Sterile Filtered colorless solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGIMAASRPL SRFWEWGKNI VCVGRNYADH VREMRSAVLS EPVLFLKPST AYAPEGSPIL MPAYTRNLHH ELELGVVMGK RCRAVPEAAA MDYVGGYALC LDMTARDVQD ECKKKGLPWT LAKSFTASCP VSAFVPKEKI PDPHKLKLWL KVNGELRQEG ETSSMIFSIP YIISYVSKII TLEEGDIILT GTPKGVGPVK ENDEIEAGIH GLVSMTFKVE KPEY.

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Name :
FAAH2 Human

Description:

Fatty Acid Amide Hydrolase 2 Human Recombinant

Fatty acid amide hydrolase 2, AMDD, Amidase domain-containing protein, Anandamide amidohydrolase 2, Oleamide hydrolase 2, FAAH2.

Product # :
ENZ-777

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Description

FAAH2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 524 amino acids (32-532a.a) and having a molecular mass of 57.4kDa. FAAH2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The FAAH2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 80% as determined by SDS-PAGE.

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Introduction
Fatty Acid Amide Hydrolase 2 (FAAH2) shares a conserved protein motif with the amidase signature family of enzymes. FAAH2 catalyzes the hydrolysis of a broad range of bioactive lipids, including those from the 3 main classes of fatty acid amides; N-acylethanolamines, fatty acid primary amides and N-acyl amino acids. FAAH2 is also degrades bioactive fatty acid amides to their corresponding acids, thus helping to end the signaling functions of these molecules. FAAH2 prefers monounsaturated acyl chains as a substrate.

Synonyms
Fatty acid amide hydrolase 2, AMDD, Amidase domain-containing protein, Anandamide amidohydrolase 2, Oleamide hydrolase 2, FAAH2.

Physical Appearance
Sterile Filtered clear solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSGGPKFAS KTPRPVTEPL LLLSGMQLAK LIRQRKVKCI DVVQAYINRI KDVNPMINGI VKYRFEEAMK EAHAVDQKLA EKQEDEATLE NKWPFLGVPL TVKEAFQLQG MPNSSGLMNR RDAIAKTDAT VVALLKGAGA IPLGITNCSE LCMWYESSNK IYGRSNNPYD LQHIVGGSSG GEGCTLAAAC SVIGVGSDIG GSIRMPAFFN GIFGHKPSPG VVPNKGQFPL AVGAQELFLC TGPMCRYAED LAPMLKVMAG PGIKRLKLDT KVHLKDLKFY WMEHDGGSFL MSKVDQDLIM TQKKVVVHLE TILGASVQHV KLKKMKYSFQ LWIAMMSAKG HDGKEPVKFV DLLGDHGKHV SPLWELIKWC LGLSVYTIPS IGLALLEEKL RYSNEKYQKF KAVEESLRKE LVDMLGDDGV FLYPSHPTVA PKHHVPLTRP FNFAYTGVFS ALGLPVTQCP LGLNAKGLPL GIQVVAGPFN DHLTLAVAQY LEKTFGGWVC PGKF.

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Name :
BPHL Human

Description:

Biphenyl Hydrolase-Like Human Recombinant

Biphenyl Hydrolase-Like (serine hydrolase), Bph-rp, Breast Epithelial Mucin-Associated Antigen, MCNAA, VACVASE, MGC41865, MGC125930.

Product # :
ENZ-055

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Description

BPHL produced in E.Coli is a single, non-glycosylated polypeptide chain containing 275 amino acids (38-291a.a.) and having a molecular mass of 31.1kDa.BPHL is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The BPHL protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
1mM DTT, 50mM NaCl and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
BPHL is a Serine hydrolase that is a part of the AB hydrolase superfamily which catalyzes the hydrolytic activation of amino acid ester prodrugs of nucleoside analogs. BPHL is expressed large quantities in liver and kidney and in minor quantities in heart, intestine and skeletal muscle. BPHL takes part in detoxification processes and is a specific alpha-amino acid ester hydrolase which favors small, hydrophobic, and aromatic side chains and does not have a strict necessity for the leaving group except for favoring a primary alcohol.

Synonyms
Biphenyl Hydrolase-Like (serine hydrolase), Bph-rp, Breast Epithelial Mucin-Associated Antigen, MCNAA, VACVASE, MGC41865, MGC125930.

Physical Appearance
Sterile Filtered clear solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.

Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSVTSAKVAV NGVQLHYQQT GEGDHAVLLL PGMLGSGETD FGPQLKNLNK KLFTVVAWDP RGYGHSRPPD RDFPADFFER DAKDAVDLMK ALKFKKVSLL GWSDGGITAL IAAAKYPSYI HKMVIWGANA YVTDEDSMIY EGIRDVSKWS ERTRKPLEAL YGYDYFARTC EKWVDGIRQF KHLPDGNICR HLLPRVQCPA LIVHGEKDPL VPRFHADFIH KHVKGSRLHL MPEGKHNLHL RFADEFNKLA EDFLQ

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Name :
PAFAH2 Human

Description:

Platelet-Activating Factor Acetylhydrolase 2 Human Recombinant

HSD-PLA2, Platelet-activating factor acetylhydrolase 2, cytoplasmic, Serine-dependent phospholipase A2, SD-PLA2, hSD-PLA2.

Product # :
ENZ-899

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Description

PAFAH2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 415 amino acids (1-392 a.a) and having a molecular mass of 46.4kDa.PAFAH2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PAFAH2 protein solution (1mg/ml) in Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Platelet-activating factor acetylhydrolase 2 cytoplasmic (PAFAH2) has a marked selectivity for phospholipids with short acyl chains at the sn-2 position. PAFAH2 may share a mutual physiologic function with the plasma-type enzyme.

Synonyms
HSD-PLA2, Platelet-activating factor acetylhydrolase 2, cytoplasmic, Serine-dependent phospholipase A2, SD-PLA2, hSD-PLA2.

Physical Appearance
Sterile Filtered colorless solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMGVNQSV GFPPVTGPHL VGCGDVMEGQ NLQGSFFRLF YPCQKAEETM EQPLWIPRYE YCTGLAEYLQ FNKRCGGLLF NLAVGSCRLP VSWNGPFKTK DSGYPLIIFS HGLGAFRTLY SAFCMELASR GFVVAVPEHR DRSAATTYFC KQAPEENQPT NESLQEEWIP FRRVEEGEKE FHVRNPQVHQ RVSECLRVLK ILQEVTAGQT VFNILPGGLD LMTLKGNIDM SRVAVMGHSF GGATAILALA KETQFRCAVA LDAWMFPLER DFYPKARGPV FFINTEKFQT MESVNLMKKI CAQHEQSRII TVLGSVHRSQ TDFAFVTGNL IGKFFSTETR GSLDPYEGQE VMVRAMLAFL QKHLDLKEDY NQWNNLIEGI GPSLTPGAPH HLSSL.

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Name :
PAFAH1B3 Human

Description:

Platelet-activating Factor Acetylhydrolase 1b, Catalytic Subunit 3 Human Recombinant

Platelet-activating factor acetylhydrolase 1b catalytic subunit 3 (29kDa), PAF acetylhydrolase 29 kDa subunit, platelet-activating factor acetylhydrolase, isoform Ib gamma subunit (29kD), PAF-AH1b alpha 1 subunit, PAF-AH 29 kDa subunit, PAFAHG, PAFAH subunit gamma, EC 3.1.1.47.

Product # :
ENZ-641

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PAFAH1B3 Human Recombinant produced in E. coli is a single polypeptide chain containing 254 amino acids (1-231) and having a molecular mass of 28.2 kDa.PAFAH1B3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The PAFAH1B3 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Platelet-activating Factor Acetylhydrolase 1b Catalytic Subunit 3 (PAFAH1B3) is a member of the 'GDSL' lipolytic enzyme family. Acetylhydrolase catalyzes the elimination of an acetyl group from the glycerol backbone of platelet-activating factor. PAFAH1B3, which is a subunit of the platelet-activating factor cetylhydrolase isoform 1B complex, is comprised of the catalytic beta and gamma subunits and the regulatory alpha subunit. The PAFAH1B3 complex has an imperative role during the development of brain.

Synonyms
Platelet-activating factor acetylhydrolase 1b catalytic subunit 3 (29kDa), PAF acetylhydrolase 29 kDa subunit, platelet-activating factor acetylhydrolase, isoform Ib gamma subunit (29kD), PAF-AH1b alpha 1 subunit, PAF-AH 29 kDa subunit, PAFAHG, PAFAH subunit gamma, EC 3.1.1.47.

Physical Appearance
Sterile Filtered colorless solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSGEENP ASKPTPVQDV QGDGRWMSLH HRFVADSKDK EPEVVFIGDS LVQLMHQCEI WRELFSPLHA LNFGIGGDGT QHVLWRLENG ELEHIRPKIV VVWVGTNNHG HTAEQVTGGI KAIVQLVNER QPQARVVVLG LLPRGQHPNP LREKNRQVNE LVRAALAGHP RAHFLDADPG FVHSDGTISH HDMYDYLHLS RLGYTPVCRA LHSLLLRLLA QDQGQGAPLL EPAP

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Name :
EPHX1 Human, Sf9

Description:

Epoxide Hydrolase 1 Microsomal Human Recombinant, sf9

Epoxide hydrolase 1, Epoxide hydratase, Microsomal epoxide hydrolase, Meh, EPHX1, EPHX, EPOX, Epoxide Hydrolase 1 Microsomal, Microsomal Epoxide Hydrolase, EC 3.3.2.9, HYL1

Product # :
ENZ-1076

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EPHX1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 442 amino acids (21-455 a.a.) and having a molecular mass of 51.5kDaEPHX1 is expressed with an 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

EPHX1 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) 50% glycerol,1mM DTT and 0.1M NaCl.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Epoxide Hydrolase 1 Microsomal (EPHX1) is a vital biotransformation enzyme which transfers epoxides from the degradation of aromatic compounds to trans-dihydrodiols that can be conjugated and excreted from the body. Epoxide hydrolase plays a role in both activation and detoxification of epoxides. Mutations in EPHX1 trigger preeclampsia, epoxide hydrolase deficiency or increased epoxide hydrolase activity.

Synonyms
Epoxide hydrolase 1, Epoxide hydratase, Microsomal epoxide hydrolase, Meh, EPHX1, EPHX, EPOX, Epoxide Hydrolase 1 Microsomal, Microsomal Epoxide Hydrolase,
EC 3.3.2.9, HYL1

Physical Appearance
Sterile Filtered colorless solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
MRDKEETLPL EDGWWGPGTR SAAREDDSIR PFKVETSDEE IHDLHQRIDK FRFTPPLEDS CFHYGFNSNY LKKVISYWRN EFDWKKQVEI LNRYPHFKTK IEGLDIHFIH VKPPQLPAGH TPKPLLMVHG WPGSFYEFYK IIPLLTDPKN HGLSDEHVFE VICPSIPGYG FSEASSKKGF NSVATARIFY KLMLRLGFQE FYIQGGDWGS LICTNMAQLV PSHVKGLHLN MALVLSNFST LTLLLGQRFG RFLGLTERDV ELLYPVKEKV FYSLMRESGY MHIQCTKPDT VGSALNDSPV GLAAYILEKF STWTNTEFRY LEDGGLERKF SLDDLLTNVM LYWTTGTIIS SQRFYKENLG QGWMTQKHER MKVYVPTGFS AFPFELLHTP EKWVRFKYPK LISYSYMVRG GHFAAFEEPE LLAQDIRKFL SVLERQHHHH HH.

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Name :
EPHX1 Human

Description:

Epoxide Hydrolase 1 Microsomal Human Recombinant

Epoxide hydrolase 1, microsomal (xenobiotic), MEH, EPHX, EPOX, Epoxide hydratase, Microsomal epoxide hydrolase.

Product # :
ENZ-773

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EPHX1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 451 amino acids (21-455a.a) and having a molecular mass of 52.2kDa. EPHX1 is fused to a 16 amino acid T7-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The EPHX1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
Epoxide Hydrolase 1 Microsomal (EPHX1) is a vital biotransformation enzyme which transfers epoxides from the degradation of aromatic compounds to trans-dihydrodiols that can be conjugated and excreted from the body. Epoxide hydrolase plays a role in both activation and detoxification of epoxides. Mutations in EPHX1 trigger preeclampsia, epoxide hydrolase deficiency or increased epoxide hydrolase activity.

Synonyms
Epoxide hydrolase 1, microsomal (xenobiotic), MEH, EPHX, EPOX, Epoxide hydratase, Microsomal epoxide hydrolase.

Physical Appearance
Sterile Filtered colorless solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
MASMTGGQQM GRGSHMRDKE ETLPLEDGWW GPGTRSAARE DDSIRPFKVE TSDEEIHDLH QRIDKFRFTP PLEDSCFHYG FNSNYLKKVI SYWRNEFDWK KQVEILNRYP HFKTKIEGLD IHFIHVKPPQ LPAGHTPKPL LMVHGWPGSF YEFYKIIPLL TDPKNHGLSD EHVFEVICPS IPGYGFSEAS SKKGFNSVAT ARIFYKLMLR LGFQEFYIQG GDWGSLICTN MAQLVPSHVK GLHLNMALVL SNFSTLTLLL GQRFGRFLGL TERDVELLYP VKEKVFYSLM RESGYMHIQC TKPDTVGSAL NDSPVGLAAY ILEKFSTWTN TEFRYLEDGG LERKFSLDDL LTNVMLYWTT GTIISSQRFY KENLGQGWMT QKHERMKVYV PTGFSAFPFE LLHTPEKWVR FKYPKLISYS YMVRGGHFAA FEEPELLAQD IRKFLSVLER Q.

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Name :
BLMH Mouse

Description:

Bleomycin Hydrolase Mouse Recombinant

BMH, BH, BLM hydrolase, Bleomycin Hydrolase.

Product # :
ENZ-1109

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BLMH Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 478 amino acids (1-455 aa) and having a molecular mass of 54.9 kDa.BLMH is fused to a 23 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The BLMH solution (0.25 mg/ml) contains 1mM DTT, 30% Glycerol, 20mM Tris-HCl(pH8.0) and 0.1M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 1,500 pmole/min/ug. Measured by hydrolysis of 1pmole of Met-AMC to Methionine and AMC per minute at pH7.5 at 37C˚.

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Introduction
BLMH is affiliate to the papain superfamily of the cysteine protease and the peptidase C1 family. BLMH is a cytoplasmic cysteinepeptidase usually found as a homohexamer. BLMH shields normal and malignant cells from the glycopeptide antitumor drug BLM. BLMH catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxyamide bond of its B-aminoalaninamide moiety and in addition demonstrates general aminopeptidase activity.

Synonyms
BMH, BH, BLM hydrolase, Bleomycin Hydrolase.

Physical Appearance
Sterile Filtered colorless solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMNNAGLN SEKVSALIQK LNSDPQFVLA QNVGTTHDLL
DICLRRATVQ GAQHVFQHVV PQEGKPVTNQ KSSGRCWIFS CLNVMRLPFM KKFNIEEFEF
SQSYLFFWDK VERCYFFLNA FVDTAQKKEP EDGRLVQYLL MNPTNDGGQW DMLVNIVEKY
GVVPKKCFPE SHTTEATRRM NDILNHKMRE FCIRLRNLVH SGATKGEISS TQDAMMEEIF
RVVCICLGNP PETFTWEYRD KDKNYHKIGP ITPLQFYKEH VKPLFNMEDK ICFVNDPRPQ
HKYNKLYTVD YLSNMVGGRK TLYNNQPIDF LKKMVAASIK DGEAVWFGCD VGKHFNGKLG
LSDMNVYDHE LVFGVSLKNM NKAERLAFGE SLMTHAMTFT AVSEKDNQEG TFVKWRVENS
WGEDHGHKGY LCMTDEWFSE YVYEVVVDKK HVPEEVLAVL EQEPIVLPAW DPMGALAE

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Name :
BLMH Human

Description:

BLM Hydrolase Human Recombinant

BMH, BH, BLM hydrolase.

Product # :
ENZ-018

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Description

BLMH produced in E.Coli is a single, non-glycosylated polypeptide chain containing 475 amino acids (1-455a.a.) and having a molecular mass of 54.7kDa.BLMH is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The BLMH protein solution (1mg/1ml) is formulated in 20mM Tris-HCl Buffer (pH 8.0) and 10% Glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

Biological Activity

Specific activity: > 1,000 pmole/min/ug. Measured by the hydrolysis of Met-AMC at pH 7.5, at 37C.

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Introduction
BLMH is affiliate to the papain superfamily of the cysteine protease and the peptidase C1 family. BLMH is a cytoplasmic cysteinepeptidase usually found as a homohexamer. The standard physiological role of BLMH has not been determined, but it shields normal and malignant cells from the glycopeptide antitumor drug BLM. BLMH catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxyamide bond of its B-aminoalaninamide moiety and in addition demonstrates general aminopeptidase activity.

Synonyms
BMH, BH, BLM hydrolase.

Physical Appearance
Sterile Filtered clear solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.

Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSSSGLNSEK VAALIQKLNS DPQFVLAQNV GTTHDLLDIC LKRATVQRAQ HVFQHAVPQE GKPITNQKSS GRCWIFSCLN VMRLPFMKKL NIEEFEFSQS YLFFWDKVER CYFFLSAFVD TAQRKEPEDG RLVQFLLMNP ANDGGQWDML VNIVEKYGVI PKKCFPESYT TEATRRMNDI LNHKMREFCI RLRNLVHSGA TKGEISATQD VMMEEIFRVV CICLGNPPET FTWEYRDKDK NYQKIGPITP LEFYREHVKP LFNMEDKICL VNDPRPQHKY NKLYTVEYLS NMVGGRKTLY NNQPIDFLKK MVAASIKDGE AVWFGCDVGK HFNSKLGLSD MNLYDHELVF GVSLKNMNKA ERLTFGESLM THAMTFTAVS EKDDQDGAFT KWRVENSWGE DHGHKGYLCM TDEWFSEYVY EVVVDRKHVP EEVLAVLEQE PIILPAWDPM GALAE

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Name :
ENTPD3 Human, sf9 Bioactive

Description:

Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant, sf9 Bioactive

Ectonucleoside Triphosphate Diphosphohydrolase 3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, CD39L3, HB6, NTPDase-3, EC 3.6.1, Ectonucleoside triphosphate diphosphohydrolase 3, NTPDase 3, CD39 antigen-like 3, Ecto-ATP diphosphohydrolase 3, Ecto-ATPDase 3, Ecto-ATPase 3, Ecto-apyrase 3, HB6.

Product # :
ENZ-1020

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Description

ENTPD3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 451 amino acids (44-485a.a.) and having a molecular mass of 50.7kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).ENTPD3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

ENTPD3 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 250,000 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze ATP per minute at pH 7.5 at 37C.

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Introduction
Ectonucleoside Triphosphate Diphosphohydrolase 3, also known as ENTPD3, which owns a threefold preference for the hydrolysis of ATP over ADP is similar to E-type nucleotidases (NTPases). ENTPD3 is a protein coding gene which contains four apyrase-conserved areas which is characteristic of NTPases.

Synonyms
Ectonucleoside Triphosphate Diphosphohydrolase 3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, CD39L3, HB6, NTPDase-3, EC 3.6.1, Ectonucleoside triphosphate diphosphohydrolase 3, NTPDase 3, CD39 antigen-like 3, Ecto-ATP diphosphohydrolase 3, Ecto-ATPDase 3, Ecto-ATPase 3, Ecto-apyrase 3, HB6.

Physical Appearance
Sterile Filtered colorless solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
ADLQIHKQEV LPPGLKYGIV LDAGSSRTTV YVYQWPAEKE NNTGVVSQTF KCSVKGSGIS SYGNNPQDVP RAFEECMQKV KGQVPSHLHG STPIHLGATA GMRLLRLQNE TAANEVLESI QSYFKSQPFD FRGAQIISGQ EEGVYGWITA NYLMGNFLEK NLWHMWVHPH GVETTGALDL GGASTQISFV AGEKMDLNTS DIMQVSLYGY VYTLYTHSFQ CYGRNEAEKK FLAMLLQNSP TKNHLTNPCY PRDYSISFTM GHVFDSLCTV DQRPESYNPN DVITFEGTGD PSLCKEKVAS IFDFKACHDQ ETCSFDGVYQ PKIKGPFVAF AGFYYTASAL NLSGSFSLDT FNSSTWNFCS QNWSQLPLLL PKFDEVYARS YCFSANYIYH LFVNGYKFTE ETWPQIHFEK EVGNSSIAWS LGYMLSLTNQ IPAESPLIRL PIEPPHHHHHH.

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View Data Sheet

Name :
ENTPD3 Human, sf9

Description:

Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant, sf9

Ectonucleoside Triphosphate Diphosphohydrolase 3, CD39L3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, HB6, NTPDase-3.

Product # :
ENZ-958

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Description

ENTPD3 Human Recombinant produced in in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 451 amino acids (44-485a.a) and having a molecular mass of 50.7kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions). ENTPD3 is fused to a 6 amino acids His-tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

ENTPD3 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Ectonucleoside Triphosphate Diphosphohydrolase 3, also known as ENTPD3, which owns a threefold preference for the hydrolysis of ATP over ADP is similar to E-type nucleotidases (NTPases). ENTPD3 is a protein coding gene which contains four apyrase-conserved areas which is characteristic of NTPases.

Synonyms
Ectonucleoside Triphosphate Diphosphohydrolase 3, CD39L3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, HB6, NTPDase-3.

Physical Appearance
Sterile Filtered colorless solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
ADLQIHKQEV LPPGLKYGIV LDAGSSRTTV YVYQWPAEKE NNTGVVSQTF KCSVKGSGIS SYGNNPQDVP RAFEECMQKV KGQVPSHLHG STPIHLGATA GMRLLRLQNE TAANEVLESI QSYFKSQPFD FRGAQIISGQ EEGVYGWITA NYLMGNFLEK NLWHMWVHPH GVETTGALDL GGASTQISFV AGEKMDLNTS DIMQVSLYGY VYTLYTHSFQ CYGRNEAEKK FLAMLLQNSP TKNHLTNPCY PRDYSISFTM GHVFDSLCTV DQRPESYNPN DVITFEGTGD PSLCKEKVAS IFDFKACHDQ ETCSFDGVYQ PKIKGPFVAF AGFYYTASAL NLSGSFSLDT FNSSTWNFCS QNWSQLPLLL PKFDEVYARS YCFSANYIYH LFVNGYKFTE ETWPQIHFEK EVGNSSIAWS LGYMLSLTNQ IPAESPLIRL PIEPPHHHHHH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
View Data Sheet

Name :
ENTPD3 Human

Description:

Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant

Ectonucleoside Triphosphate Diphosphohydrolase 3, CD39L3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, HB6, NTPDase-3.

Product # :
ENZ-844

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Description

ENTPD3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 465 amino acids (44-485 a.a) and having a molecular mass of 52kDa. ENTPD3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ENTPD3 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

More Info

Introduction
Ectonucleoside Triphosphate Diphosphohydrolase 3, also known as ENTPD3, which owns a threefold preference for the hydrolysis of ATP over ADP is similar to E-type nucleotidases (NTPases). ENTPD3 is a protein coding gene which contains four apyrase-conserved areas which is characteristic of NTPases.

Synonyms
Ectonucleoside Triphosphate Diphosphohydrolase 3, CD39L3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, HB6, NTPDase-3.

Physical Appearance
Sterile Filtered clear solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSQIHKQEV LPPGLKYGIV LDAGSSRTTV YVYQWPAEKE NNTGVVSQTF KCSVKGSGIS SYGNNPQDVP RAFEECMQKV KGQVPSHLHG STPIHLGATA GMRLLRLQNE TAANEVLESI QSYFKSQPFD FRGAQIISGQ EEGVYGWITA NYLMGNFLEK NLWHMWVHPH GVETTGALDL GGASTQISFV AGEKMDLNTS DIMQVSLYGY VYTLYTHSFQ CYGRNEAEKK FLAMLLQNSP TKNHLTNPCY PRDYSISFTM GHVFDSLCTV DQRPESYNPN DVITFEGTGD PSLCKEKVAS IFDFKACHDQ ETCSFDGVYQ PKIKGPFVAF AGFYYTASAL NLSGSFSLDT FNSSTWNFCS QNWSQLPLLL PKFDEVYARS YCFSANYIYH LFVNGYKFTE ETWPQIHFEK EVGNSSIAWS LGYMLSLTNQ IPAESPLIRL PIEPP.

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View Data Sheet

Name :
DDAH1 Human

Description:

Dimethylarginine Dimethylaminohydrolase 1 Human Recombinant

DDAH, DDAH-1, Dimethylargininase-1, dimethylargininase-1, Dimethylarginine Dimethylaminohydrolase 1.

Product # :
ENZ-014

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Description

DDAH1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (1-285a.a.) and having a molecular mass of 33.5kDa.DDAH1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The DDAH1 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) 1mM DTT, 50mM NaCl and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Dimethylarginine dimethylaminohydrolase 1, is a part of the Dimethylarginine Dimethylaminohydrolase gene family. DDAH1 participates in nitric oxide generation by regulating cellular concentrations of methylarginines, that in turn inhibit nitric oxide synthase activity. Deficiency of DDAH1 results in ADMA (asymmetric dimethylarginine) increase and a decrease in cGMP generation.

Synonyms
DDAH, DDAH-1, Dimethylargininase-1, dimethylargininase-1, Dimethylarginine Dimethylaminohydrolase 1.

Physical Appearance
Sterile Filtered clear solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAGLGHP AAFGRATHAV VRALPESLGQ HALRSAKGEE VDVARAERQH QLYVGVLGSK LGLQVVELPA DESLPDCVFV EDVAVVCEET ALITRPGAPS RRKEVDMMKE ALEKLQLNIV EMKDENATLD GGDVLFTGRE FFVGLSKRTN QRGAEILADT FKDYAVSTVP VADGLHLKSF CSMAGPNLIA IGSSESAQKA LKIMQQMSDH RYDKLTVPDD IAANCIYLNI PNKGHVLLHR TPEEYPESAK VYEKLKDHML IPVSMSELEK VDGLLTCCSV LINKKVDS

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View Data Sheet

Name :
HIBCH Human

Description:

3-Hydroxyisobutyryl-CoA Hydrolase Human Recombinant

3-hydroxyisobutyryl-coenzyme A hydrolase mitochondrial, HIBYL-CoA-H, HIB-CoA hydrolase, EC 3.1.2.4

Product # :
ENZ-594

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Description

HIBCH Recombinant produced in E. coli is a single polypeptide chain containing 379 amino acids (33-386) and having a molecular mass of 42.1kDa.HIBCH is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The HIBCH solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
HIBCH enzyme is in charge of hydrolysis of both HIBYL-CoA and beta-hydroxypropionyl-CoA. Damages in the HIBCH gene linked to 3-hyroxyisobutyryl-CoA hydrolase deficiency. Multiple transcript variants exist as a result of alternative splicing.

Synonyms
3-hydroxyisobutyryl-coenzyme A hydrolase mitochondrial, HIBYL-CoA-H, HIB-CoA hydrolase, EC 3.1.2.4

Physical Appearance
Sterile Filtered colorless solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMDAAEE VLLEKKGCTG VITLNRPKFL NALTLNMIRQ IYPQLKKWEQ DPETFLIIIK GAGGKAFCAG GDIRVISEAE KAKQKIAPVF FREEYMLNNA VGSCQKPYVA LIHGITMGGG VGLSVHGQFR VATEKCLFAM PETAIGLFPD VGGGYFLPRL QGKLGYFLAL TGFRLKGRDV YRAGIATHFV DSEKLAMLEE DLLALKSPSK ENIASVLENY HTESKIDRDK SFILEEHMDK INSCFSANTV EEIIENLQQD GSSFALEQLK VINKMSPTSL KITLRQLMEG SSKTLQEVLT MEYRLSQACM RGHDFHEGVR AVLIDKDQSP KWKPADLKEV TEEDLNNHFK SLGSSDLKF.

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View Data Sheet

Name :
ADPRHL2 Human

Description:

ADP-Ribosylhydrolase Like 2 Human Recombinant

Poly(ADP-ribose) glycohydrolase ARH3, ADP-ribosylhydrolase 3, [Protein ADP-ribosylarginine] hydrolase-like protein 2, ADPRHL2, ARH3.

Product # :
ENZ-638

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Description

ADPRHL2 Human Recombinant produced in E. coli is a single polypeptide chain containing 387 amino acids (1-363) and having a molecular mass of 41.5kDa.ADPRHL2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The ADPRHL2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 30% glycerol and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
ADP-ribosylhydrolase like 2 (ADPRHL2) belongs to the ADP-ribosylglycohydrolase family. ADPRHL2 catalyzes the removal of ADP-ribose from ADP-ribosylated proteins. ADPRHL2, which is ubiquitously expressed, uses magnesium as a cofactor to catalyze the hydrolysis of poly (ADP-ribose) that is synthesized after DNA damage. Furthermore, ADPRHL2 has an essential role in the maintenance of normal neuronal cell function. The ADPRHL2 enzyme localizes to the mitochondria, in addition to the nucleus and cytoplasm.

Synonyms
Poly(ADP-ribose) glycohydrolase ARH3, ADP-ribosylhydrolase 3, [Protein ADP-ribosylarginine] hydrolase-like protein 2, ADPRHL2, ARH3.

Physical Appearance
Sterile Filtered colorless solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAAAAM AAAAGGGAGA ARSLSRFRGC LAGALLGDCV GSFYEAHDTV DLTSVLRHVQ SLEPDPGTPG SERTEALYYT DDTAMARALV QSLLAKEAFD EVDMAHRFAQ EYKKDPDRGY GAGVVTVFKK LLNPKCRDVF EPARAQFNGK GSYGNGGAMR VAGISLAYSS VQDVQKFARL SAQLTHASSL GYNGAILQAL AVHLALQGES SSEHFLKQLL GHMEDLEGDA QSVLDARELG MEERPYSSRL KKIGELLDQA SVTREEVVSE LGNGIAAFES VPTAIYCFLR CMEPDPEIPS AFNSLQRTLI YSISLGGDTD TIATMAGAIA GAYYGMDQVP ESWQQSCEGY EETDILAQSL HRVFQKS.

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View Data Sheet

Name :
ADPRH Human

Description:

ADP-Ribosylarginine Hydrolase Human Recombinant

[Protein ADP-ribosylarginine] hydrolase, ADP-ribosylarginine hydrolase, ADP-ribose-L-arginine cleaving enzyme, ADPRH, ARH1.

Product # :
ENZ-631

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Description

ADPRH Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 381 amino acids (1-357) and having a molecular mass of 42.1kDa.ADPRH is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The ADPRH solution (0.5mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 1mM DTT and 100mM NaCl.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
ADP-ribosylarginine hydrolase (ADPRH) is a member of the ADP-ribosylglycohydrolase family. ADPRH catalyzes the removal of mono-ADP-ribose from arginine residues of proteins in the ADP-ribosylation cycle. The human ADPRH enzyme is DTT-independent as opposed to the rat and mouse enzymes, which require DTT for maximal activity.

Synonyms
[Protein ADP-ribosylarginine] hydrolase, ADP-ribosylarginine hydrolase, ADP-ribose-L-arginine cleaving enzyme, ADPRH, ARH1.

Physical Appearance
Sterile Filtered colorless solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMEKYVA AMVLSAAGDA LGYYNGKWEF LQDGEKIHRQ LAQLGGLDAL DVGRWRVSDD TVMHLATAEA LVEAGKAPKL TQLYYLLAKH YQDCMEDMDG RAPGGASVHN AMQLKPGKPN GWRIPFNSHE GGCGAAMRAM CIGLRFPHHS QLDTLIQVSI ESGRMTHHHP TGYLGALASA LFTAYAVNSR PPLQWGKGLM ELLPEAKKYI VQSGYFVEEN LQHWSYFQTK WENYLKLRGI LDGESAPTFP ESFGVKERDQ FYTSLSYSGW GGSSGHDAPM IAYDAVLAAG DSWKELAHRA FFHGGDSDST AAIAGCWWGV MYGFKGVSPS NYEKLEYRNR
LEETARALYS LGSKEDTVIS L.

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View Data Sheet

Name :
HDHD3 Human

Description:

Haloacid Dehalogenase-Like Hydrolase Domain Containing 3 Human Recombinant

Haloacid dehalogenase-like hydrolase domain-containing protein 3, HDHD3, C9orf158, MGC12904, 2810435D12Rik.

Product # :
ENZ-089

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Description

HDHD3 Human Recombinant fused with a 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 287 amino acids (1-251 a.a.) and having a molecular mass of 32.2kDa. The HDHD3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The HDHD3 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Haloacid dehalogenase-like hydrolase domain-containing protein 3 (HDHD3) is a member of the HAD-like hydrolase superfamily. This family of hydrolase enzymes includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases.

Synonyms
Haloacid dehalogenase-like hydrolase domain-containing protein 3, HDHD3, C9orf158, MGC12904, 2810435D12Rik.

Physical Appearance
Sterile Filtered colorless solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMAHR LQIRLLTWDV KDTLLRLRHP LGEAYATKAR AHGLEVEPSA LEQGFRQAYR AQSHSFPNYG LSHGLTSRQW WLDVVLQTFH LAGVQDAQAV APIAEQLYKD FSHPCTWQVL DGAEDTLREC RTRGLRLAVI SNFDRRLEGI LEGLGLREHF DFVLTSEAAG WPKPDPRIFQ EALRLAHMEP VVAAHVGDNY LCDYQGPRAV GMHSFLVVGP QALDPVVRDS VPKEHILPSL AHLLPALDCL EGSTPGL.

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View Data Sheet

Name :
HDHD2 Human

Description:

Haloacid Dehalogenase-Like Hydrolase Domain Containing 2 Human Recombinant

Haloacid Dehalogenase-like Hydrolase Domain Containing 2, DKFZP564D1378, 3110052N05Rik, DKFZp564D1378.

Product # :
ENZ-038

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Description

HDHD2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 279 amino acids (1-259a.a.) and having a molecular mass of 30.6kDa.HDHD2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The HDHD2 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT, and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
HDHD2 is a member of the HAD-like hydrolase superfamily which includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. There are two active sites in HDHD2 - an L-2-haloacid dehalogenase and a carboxylate group. The L-2-haloacid dehalogenase active site catalyzes the hydrolytic dehalogenation of D- and L-2-haloalkanoic acids, producing L- and D-2-hydroxyalkanoic acids.

Synonyms
Haloacid Dehalogenase-like Hydrolase Domain Containing 2, DKFZP564D1378, 3110052N05Rik, DKFZp564D1378.

Physical Appearance
Sterile Filtered clear solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAACRALKAV LVDLSGTLHI EDAAVPGAQE ALKRLRGASV IIRFVTNTTK ESKQDLLERL RKLEFDISED EIFTSLTAAR SLLERKQVRP MLLVDDRALP DFKGIQTSDP NAVVMGLAPE HFHYQILNQA FRLLLDGAPL IAIHKARYYK RKDGLALGPG PFVTALEYAT DTKATVVGKP EKTFFLEALR GTGCEPEEAV MIGDDCRDDV GGAQDVGMLG ILVKTGKYRA SDEEKINPPP YLTCESFPHA VDHILQHLL

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View Data Sheet

Name :
HDHD1 Human

Description:

Haloacid Dehalogenase-Like Hydrolase Domain Containing 1 Human Recombinant

Pseudouridine-5'-monophosphatase, 5'-PsiMPase, Haloacid dehalogenase-like hydrolase domain-containing protein 1, Haloacid dehalogenase-like hydrolase domain-containing protein 1A, Protein GS1, HDHD1, DXF68S1E, FAM16AX, GS1, HDHD1A.

Product # :
ENZ-028

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Description

HDHD1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 248 amino acids (1-228 a.a.) and having a molecular mass of 27.4kDa. The HDHD1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The HDHD1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol,
0.1M NaCl and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Haloacid dehalogenase-like hydrolase domain-containing protein 1A (HDHD1A) is a member of the adiponutrin family. HDHD1A is interesting because it is an X-linked gene that escapes X-inactivation. HDHD1A is particularly important in the perception of human X chromosome structural organization as well as the mechanism of X-inactivation.

Synonyms
Pseudouridine-5'-monophosphatase, 5'-PsiMPase, Haloacid dehalogenase-like hydrolase domain-containing protein 1, Haloacid dehalogenase-like hydrolase domain-containing protein 1A, Protein GS1, HDHD1, DXF68S1E, FAM16AX, GS1, HDHD1A.

Physical Appearance
Sterile Filtered colorless solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAAPPQPVTH LIFDMDGLLL DTERLYSVVF QEICNRYDKK YSWDVKSLVM GKKALEAAQI IIDVLQLPMS KEELVEESQT KLKEVFPTAA LMPGAEKLII HLRKHGIPFA LATSSGSASF DMKTSRHKEF FSLFSHIVLG DDPEVQHGKP DPDIFLACAK RFSPPPAMEK CLVFEDAPNG VEAALAAGMQ VVMVPDGNLS RDLTTKATLV LNSLQDFQPE LFGLPSYE.

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View Data Sheet

Name :
HDDC3 Human

Description:

HD domain containing 3 Human Recombinant

Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase MESH1, HD domain-containing protein 3, Metazoan SpoT homolog 1, MESH1, Penta-phosphate guanosine-3'-pyrophosphohydrolase, (ppGpp)ase, HDDC3.

Product # :
ENZ-184

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Description

HDDC3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 160 amino acids (1-140) and having a molecular mass of 17.9kDa.HDDC3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The HDDC3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.15M NaCl and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Guanosine-3',5'-bis(diphosphate)-pyrophosphohydrolase MESH1 (HDDC3) contains an active site for ppGpp hydrolysis and a conserved His-Asp-box motif for Mn(2+) binding. In accordance with its structure, HDDC3 effectively catalyzes the hydrolysis of guanosine 3',5'-diphosphate (ppGpp) both in vitro and in vivo. In addition, HDDC3 suppresses SpoT-deficient lethality and RelA-induced delayed cell growth in bacteria.

Synonyms
Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase MESH1, HD domain-containing protein 3, Metazoan SpoT homolog 1, MESH1, Penta-phosphate guanosine-3'-pyrophosphohydrolase, (ppGpp)ase, HDDC3.

Physical Appearance
Sterile Filtered colorless solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSEAAQLLE AADFAARKHR QQRRKDPEGT PYINHPIGVA RILTHEAGIT DIVVLQAALL HDTVEDTDTT LDEVELHFGA QVRRLVEEVT DDKTLPKLER KRLQVEQAPH SSPGAKLVKL ADKLYNLRDL NRCTPEVKIQ.

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Name :
ACY1 Mouse

Description:

AminoAcylase-1 Mouse Recombinant

Aminoacylase-1, ACY-1, N-acyl-L-amino-acid amidohydrolase, Aminoacylase 1, Acy1.

Product # :
ENZ-905

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Description

ACY1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 433 amino acids (1-408 a.a) and having a molecular mass of 48.4kDa. ACY1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ACY1 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Acy1 or Aminoacylase1 is a cytosolic, homodimeric, zinc-binding enzyme which catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and acyl group, and has been suggested to operate in the catabolism and salvage of acylated amino acids. ACY1 is localized in chromosome 3p21.1, a region reduced to homozygosity in small-cell lung cancer (SCLC), and its expression has been observed to be reduced or undetectable in SCLC cell lines and tumors.

Synonyms
Aminoacylase-1, ACY-1, N-acyl-L-amino-acid amidohydrolase, Aminoacylase 1, Acy1.

Physical Appearance
Sterile Filtered colorless solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSEFMTTKD PESEHPSVTL FRQYLRICTV QPNPDYGGAI TFLEERARQL GLSCQKIEVV PGFVITVLTW PGTNPSLPSI LLNSHTDVVP VFKEHWHHDP FEAFKDSEGY IYARGSQDMK SVSIQYLEAV RRLKSEGHRF PRTIHMTFVP DEEVGGHKGM ELFVKRPEFQ ALRAGFALDE GLANPTDAFT VFYSERSPWW VRVTSTGKPG HASRFIEDTA AEKLHKVISS ILAFREKERQ RLQANPHLKE GAVTSVNLTK LEGGVAYNVV PATMSASFDF RVAPDVDMKA FEKQLQRWCQ EAGEGVTFEF AQKFTEPRMT PTDDSDPWWA AFSGACKAMN LTLEPEIFPA ATDSRYIRAV GIPALGFSPM NRTPVLLHDH NERLHEDIFL RGVDIYTGLL SALASVPTLP GES.

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Name :
ACY1 Human

Description:

Aminoacylase-1 Human Recombinant

N-acyl-L-amino-acid amidohydrolase, ACY-1, ACY1D, ACYLASE, ACY1,EC 3.5.1.143.

Product # :
ENZ-296

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ACY1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 428 amino acids (1-408 a.a.) and having a molecular mass of 48kDa. The ACY1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The ACY1 solution (0.5mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Aminoacylase-1 is a cytosolic, homodimeric, zinc-binding enzyme that catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and acyl group, and has been postulated to function in the catabolism and salvage of acylated amino acids. ACY1 has been assigned to chromosome 3p21.1, a region reduced to homozygosity in small-cell lung cancer (SCLC), and its expression has been reported to be reduced or undetectable in SCLC cell lines and tumors. The amino acid sequence of human aminoacylase-1 is highly homologous to the porcine counterpart, and ACY1 is the first member of a new family of zinc-binding enzymes.

Synonyms
N-acyl-L-amino-acid amidohydrolase, ACY-1, ACY1D, ACYLASE, ACY1,EC 3.5.1.143.

Physical Appearance
Sterile Filtered clear solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTSKGPEEEH PSVTLFRQYL RIRTVQPKPD YGAAVAFFEE TARQLGLGCQ KVEVAPGYVV TVLTWPGTNP TLSSILLNSH TDVVPVFKEH WSHDPFEAFK DSEGYIYARG AQDMKCVSIQ YLEAVRRLKV EGHRFPRTIH MTFVPDEEVG GHQGMELFVQ
RPEFHALRAG FALDEGIANP TDAFTVFYSE RSPWWVRVTS TGRPGHASRF MEDTAAEKLH KVVNSILAFR EKEWQRLQSN PHLKEGSVTS VNLTKLEGGV AYNVIPATMS ASFDFRVAPD VDFKAFEEQL QSWCQAAGEG VTLEFAQKWM HPQVTPTDDS NPWWAAFSRV CKDMNLTLEP EIMPAATDNR YIRAVGVPAL GFSPMNRTPV LLHDHDERLH EAVFLRGVDI YTRLLPALAS VPALPSDS.

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Name :
ABHD14B Human

Description:

Abhydrolase Domain Containing 14B Human Recombinant

Abhydrolase domain containing protein 14B, CIB, CCG1-interacting factor B, cell cycle gene 1-interacting factor B, EC 3.1.11.6, EC 3.1.21.4.

Product # :
ENZ-240

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ABHD14B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 234 amino acids (1-210) and having a molecular mass of 25.0kDa.ABHD14B is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The ABHD14B solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
ABHD14B is a member of the AB hydrolase superfamily. ABHD14B has an alpha/beta hydrolase fold - a catalytic domain found in a large number of enzymes. In molecular biology, the alpha/beta hydrolase fold is common to a number of hydrolytic enzymes of broad differing phylogenetic source and catalytic function. The Ab hydrolase domain containing gene subfamily includes 15 mostly uncharacterized members. ABHD14B has hydrolase activity with p-nitrophenyl butyrate (in vitro) and is able to activate transcription.

Synonyms
Abhydrolase domain containing protein 14B, CIB, CCG1-interacting factor B, cell cycle gene 1-interacting factor B, EC 3.1.11.6, EC 3.1.21.4.

Physical Appearance
Sterile Filtered colorless solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAASVE QREGTIQVQG QALFFREALP GSGQARFSVL LLHGIRFSSE TWQNLGTLHR LAQAGYRAVA IDLPGLGHSK EAAAPAPIGE LAPGSFLAAV VDALELGPPV VISPSLSGMY SLPFLTAPGS QLPGFVPVAP ICTDKINAAN YASVKTPALI VYGDQDPMGQ TSFEHLKQLP NHRVLIMKGA GHPCYLDKPE EWHTGLLDFL QGLQ

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Name :
ABHD10 Human

Description:

Abhydrolase Domain Containing 10 Human Recombinant

Abhydrolase domain containing 10 mitochondrial2, FLJ11342, EC 3.4.-.-.

Product # :
ENZ-612

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ABHD10 Human Recombinant produced in E. coli is a single polypeptide chain containing 279 amino acids (53-306) and having a molecular mass of 30.9kDa.ABHD10 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The ABHD10 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 100mM NaCl and 20% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Abhydrolase domain-containing protein 10 (ABHD10) is a member of the AB hydrolase superfamily.

Synonyms
Abhydrolase domain containing 10 mitochondrial2, FLJ11342, EC 3.4.-.-.

Physical Appearance
Sterile Filtered colorless solution.

Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMTSLSF LNRPDLPNLA YKKLKGKSPG IIFIPGYLSY MNGTKALAIE EFCKSLGHAC IRFDYSGVGS SDGNSEESTL GKWRKDVLSI IDDLADGPQI LVGSSLGGWL MLHAAIARPE KVVALIGVAT AADTLVTKFN QLPVELKKEV EMKGVWSMPS KYSEEGVYNV QYSFIKEAEH HCLLHSPIPV NCPIRLLHGM KDDIVPWHTS MQVADRVLST DVDVILRKHS DHRMREKADI QLLVYTIDDL IDKLSTIVN

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

About Hydrolases:

Hydrolases are a class of hydrolytic enzymes that divide larger molecules into smaller molecules using water to break the glycosidic bonds. They are present in a wide range of biological interactions in the human body and the natural world. One most obvious example is the presence of hydrolases secreted by Lactobacillus jensenii in the human gut. This stimulates the secretion of bile salts by the liver which aid in the digestion of food. A common examples of hydrolase enzymes might be esterases including phosphatases, glycosidases, lipases, peptidases, and nucleosidases. They are divided into a wide range of subclasses based upon the different bonds they act upon.

Hydrolase Mechanism
Enzymatic hydrolysis of the glycosidic bond takes place via general acid catalysis that requires. Two critical residues are required for this to occur, a nucleophile and a proton donor.
Two major mechanisms give rise to this hydrolysis. Either there is an overall retention, or an inversion of anomeric configuration. In both mechanisms, the position of the proton donor is identical, i.e. within hydrogen-bonding distance of the glycosidic oxygen.
In retaining enzymes, the nucleophilic catalytic base is in close proximity to the sugar anomeric carbon.

Hydrolase Interactions
Different subclasses of hydrolases have a wide range of different molecular interactions inside the body. Esterases, for example, cleave ester bonds in lipids while phosphatases cleave phosphate groups off molecules. Acetylcholine esterase is a prime example of a crucial esterase. It aids in transforming the neuron impulse into acetic acid. After the impulse, the hydrolase breaks the acetylcholine into choline and acetic acid.
This acetic acid is an important metabolite in the body and a critical intermediate for other bodily reactions like glycolysis. Glycosidases, on the other hand, cleave sugar molecules off carbohydrates and peptidases hydrolyze peptide bonds while lipases hydrolyze glycerides and nucleosidases hydrolyze the bonds of nucleotides.

Hydrolase Function
Hydrolase enzymes have a wide range of functions inside of the body. The degenerative properties of hydrolases, for example, are essential for the body. In lipids, lipases help to facilitate the breakdown of fats, lipoproteins and other larger molecules into smaller molecules like fatty acids and glycerol. These fatty acids and other small molecules are essential in the body’s storage and synthesis of energy.
Structures
Hydrolases have a range of structures which dictate their interactions and functions.
Crater / pocket structure topology is most optimal for the recognition of a saccharide non-reducing extremity. It is most commonly encountered in monosaccharides as well as exopolysaccharides such as glucoamylase and β-amylase.
Tunnel structures have only been found in cellobiohydrolases. Nonetheless, the resulting tunnel shapes structure enables a polysaccharide chain to be threaded through it. Thus, the structure allows enzymes to release the product while remaining firmly bound to the polysaccharide chain and create the conditions for processivity.
Groove / cleft structure are “open” structures allow for a random binding of multiple sugar units in polymeric substrates. It is usually found in endo-acting polysaccharidases. Some examples of which might include endocellulases, chitinases, lysozymes and xylanases among others.

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