Hydroxylase

Hydroxylase

Hydroxylase

Name

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  • View Data Sheet

    Name :

    TH Mouse

    Description:

    Tyrosine Hydroxylase Mouse Recombinant

    Tyrosine 3-monooxygenase, Tyrosine 3-hydroxylase, TH.

    Product # :

    ENZ-988

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    Description

    TH Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 507 amino acids (1-498a.a.) and having a molecular mass of 57.0kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). TH is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TH protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Tyrosine 3-monooxygenase (Th), is a rate-limiting enzyme in catecholamine synthesis. Th utilizes tetrahydrobiopterin as well as molecular oxygen to convert tyrosine to DOPA. Th regulates dopamine (DA) neurotransmission at the biosynthesis and reuptake steps. Th takes a vital part in the physiology of adrenergic neurons. Furthermore, Th effects overexpression in lymphocytes on the differentiation as well as function of T helper cells.

    • Synonyms

      Tyrosine 3-monooxygenase, Tyrosine 3-hydroxylase, TH.

    • 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

      ADPMPTPSAS SPQPKGFRRA VSEQDTKQAE AVTSPRFIGR RQSLIEDARK EREAAAAAAA AAVASAEPGN PLEAVVFEER DGNAVLNLLF SLRGTKPSSL SRALKVFETF EAKIHHLETR PAQRPLAGSP HLEYFVRFEV PSGDLAALLS SVRRVSDDVR SAREDKVPWF PRKVSELDKC HHLVTKFDPD LDLDHPGFSD QAYRQRRKLI AEIAFQYKQG EPIPHVEYTK EEIATWKEVY ATLKGLYATH ACREHLEAFQ LLERYCGYRE DSIPQLEDVS HFLKERTGFQ LRPVAGLLSA RDFLASLAFR VFQCTQYIRH ASSPMHSPEP DCCHELLGHV PMLADRTFAQ FSQDIGLASL GASDEEIEKL STVYWFTVEF GLCKQNGELK AYGAGLLSSY GELLHSLSEE PEVRAFDPDT AAVQPYQDQT YQPVYFVSES FSDAKDKLRN YASRIQRPFS VKFDPYTLAI DVLDSPHTIR RSLEGVQDEL HTLTQALSAI SHHHHHH.

    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.

    Th Mouse
  • View Data Sheet

    Description:

    Prolyl 4-Hydroxylase Beta Mouse Recombinant

    Protein disulfide-isomerase, PDI, Cellular thyroid hormone-binding protein, Endoplasmic reticulum resident protein 59, ER protein 59, ERp59, Prolyl 4-hydroxylase subunit beta, p55.

    Product # :

    ENZ-935

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    Description

    P4HB produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 498 amino acids (20-509a.a.) and having a molecular mass of 56.1kDa. P4HB is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    P4HB protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      P4HB is a multifunctional and highly abundant enzyme that is part of the protein disulfide isomerase family. When present as a tetramer consisting of two alpha and two beta subunits, P4HB has a role in hydroxylation of prolyl residues in preprocollagen. P4HB is a disulfide isomerase containing two thioredoxin domains that catalyze the formation, breakage and rearrangement of disulfide bonds.

    • Synonyms

      Protein disulfide-isomerase, PDI, Cellular thyroid hormone-binding protein, Endoplasmic reticulum resident protein 59, ER protein 59, ERp59, Prolyl 4-hydroxylase subunit beta, p55.

    • 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

      DALEEEDNVL VLKKSNFEEA LAAHKYLLVE FYAPWCGHCK ALAPEYAKAA AKLKAEGSEI RLAKVDATEE SDLAQQYGVR GYPTIKFFKN GDTASPKEYT AGREADDIVN WLKKRTGPAA TTLSDTAAAE SLVDSSEVTV IGFFKDVESD SAKQFLLAAE AIDDIPFGIT SNSGVFSKYQ LDKDGVVLFK KFDEGRNNFE GEITKEKLLD FIKHNQLPLV IEFTEQTAPK IFGGEIKTHI LLFLPKSVSD YDGKLSSFKR AAEGFKGKIL FIFIDSDHTD NQRILEFFGL KKEECPAVRL ITLEEEMTKY KPESDELTAE KITEFCHRFL EGKIKPHLMS QEVPEDWDKQ PVKVLVGANF EEVAFDEKKN VFVEFYAPWC GHCKQLAPIW DKLGETYKDH ENIIIAKMDS TANEVEAVKV HSFPTLKFFP ASADRTVIDY NGERTLDGFK KFLESGGQDG AGDDEDLDLE EALEPDMEED DDQKAVKDEL LEHHHHHH.

    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.

    P4Hb Mouse
  • View Data Sheet

    Description:

    Prolyl 4-Hydroxylase Beta Human Recombinant, Active

    P4Hbeta, PDI, PDIA1, PHD, PO4DB, PO4HB, ERBA2L.

    Product # :

    ENZ-991

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    Description

    P4HB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 521 amino acids (18-508 a.a.) and having a molecular mass of 57.5kDa. The P4HB is fused to a 21 amino acid His Tag and purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

    The P4HB 1mg/ml protein solution contains 20mM Tris-HCl pH-8, and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity > 100 A650/cm/min/mg. Enzymatic activity was confirmed by measuring the aggregation of insulin in the presence of DTT.

    More Info

    • Introduction

      P4HB is a multifunctional and highly abundant enzyme that is part of the protein disulfide isomerase family. When present as a tetramer consisting of two alpha and two beta subunits, P4HB has a role in hydroxylation of prolyl residues in preprocollagen. P4HB is a disulfide isomerase containing two thioredoxin domains that catalyze the formation, breakage and rearrangement of disulfide bonds.

    • Synonyms

      P4Hbeta, PDI, PDIA1, PHD, PO4DB, PO4HB, ERBA2L.

    • 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 MDAPEEEDHV LVLRKSNFAE ALAAHKYLLV EFYAPWCGHC KALAPEYAKA AGKLKAEGSE IRLAKVDATE ESDLAQQYGV RGYPTIKFFR NGDTASPKEY TAGREADDIV NWLKKRTGPA ATTLPDGAAA ESLVESSEVA VIGFFKDVES DSAKQFLQAA EAIDDIPFGI TSNSDVFSKY QLDKDGVVLF KKFDEGRNNF EGEVTKENLL DFIKHNQLPL VIEFTEQTAP KIFGGEIKTH ILLFLPKSVS DYDGKLSNFK TAAESFKGKI LFIFIDSDHT DNQRILEFFG LKKEECPAVR LITLEEEMTK YKPESEELTA ERITEFCHRF LEGKIKPHLM SQELPEDWDK QPVKVLVGKN FEDVAFDEKK NVFVEFYAPW CGHCKQLAPI WDKLGETYKD HENIVIAKMD STANEVEAVK VHSFPTLKFF PASADRTVID YNGERTLDGF KKFLESGGQD GAGDDDDLED LEEAEEPDME EDDDQKAVKD EL.

    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.

    P4Hb Human Active
  • View Data Sheet

    Description:

    Prolyl 4-Hydroxylase Beta Human Recombinant

    P4Hbeta, PDI, PDIA1, PHD, PO4DB, PO4HB, ERBA2L.

    Product # :

    ENZ-252

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    Description

    P4HB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 512 amino acids (18-508 a.a.) and having a molecular mass of 57.5 kDa. The P4HB is fused to a 21 amino acid His Tag and purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

    The P4HB 1mg/ml protein solution contains 20mM Tris-HCl pH-8, and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      P4HB is a multifunctional and highly abundant enzyme that is part of the protein disulfide isomerase family. When present as a tetramer consisting of two alpha and two beta subunits, P4HB has a role in hydroxylation of prolyl residues in preprocollagen. P4HB is a disulfide isomerase containing two thioredoxin domains that catalyze the formation, breakage and rearrangement of disulfide bonds.

    • Synonyms

      P4Hbeta, PDI, PDIA1, PHD, PO4DB, PO4HB, ERBA2L.

    • 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 MDAPEEEDHV LVLRKSNFAE ALAAHKYLLV EFYAPWCGHC KALAPEYAKA AGKLKAEGSE IRLAKVDATE ESDLAQQYGV RGYPTIKFFR NGDTASPKEY TAGREADDIV NWLKKRTGPA ATTLPDGAAA ESLVESSEVA VIGFFKDVES DSAKQFLQAA
      EAIDDIPFGI TSNSDVFSKY QLDKDGVVLF KKFDEGRNNF EGEVTKENLL DFIKHNQLPL VIEFTEQTAP KIFGGEIKTH ILLFLPKSVS DYDGKLSNFK TAAESFKGKI LFIFIDSDHT DNQRILEFFG LKKEECPAVR LITLEEEMTK YKPESEELTA ERITEFCHRF LEGKIKPHLM
      SQELPEDWDK QPVKVLVGKN FEDVAFDEKK NVFVEFYAPW CGHCKQLAPI WDKLGETYKD HENIVIAKMD STANEVEAVK VHSFPTLKFF PASADRTVID YNGERTLDGF KKFLESGGQD GAGDDDDLED LEEAEEPDME EDDDQKAVKD EL.

    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.

    P4Hb Human
  • View Data Sheet

    Description:

    Aspartate Beta-Hydroxylase Human Recombinant

    AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH.

    Product # :

    ENZ-488

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    Description

    ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids (75-270 a.a.) and having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag and purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

    The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters and goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms (a and f) include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, and X, and the complement factors C1R and C1S. Further isoforms diverge mainly in the C-terminal sequence and lack the hydroxylase domain, and some have been localized to the endoplasmic and sarcoplasmic reticulum.

    • Synonyms

      AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH.

    • 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 MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT.

    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.

    Asph Human
  • View Data Sheet

    Description:

    DBH Human Recombinant

    EC 1.14.17.1, DBM, DBH.

    Product # :

    ENZ-891

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    Description

    DBH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 599 amino acids (40-617 a.a) and having a molecular mass of 67.2kDa.DBH is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DBH protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DBH catalyzes the chemical reaction. DBH is an oxidoreductase which belongs to the copper type II, ascorbate-dependent monooxygenase family, in particular those performing on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated can not be derived from O2 with reduced ascorbate as one donor, as well as incorporation of one ato of oxygen into the other donor.

    • Synonyms

      EC 1.14.17.1, DBM, DBH.

    • 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 MSAPRESPLP YHIPLDPEGS LELSWNVSYT QEAIHFQLLV RRLKAGVLFG MSDRGELENA DLVVLWTDGD TAYFADAWSD QKGQIHLDPQ QDYQLLQVQR TPEGLTLLFK RPFGTCDPKD YLIEDGTVHL VYGILEEPFR SLEAINGSGL QMGLQRVQLL KPNIPEPELP SDACTMEVQA PNIQIPSQET TYWCYIKELP KGFSRHHIIK YEPIVTKGNE ALVHHMEVFQ CAPEMDSVPH FSGPCDSKMK PDRLNYCRHV LAAWALGAKA FYYPEEAGLA FGGPGSSRYL RLEVHYHNPL VIEGRNDSSG IRLYYTAKLR RFNAGIMELG LVYTPVMAIP PRETAFILTG YCTDKCTQLA LPPSGIHIFA SQLHTHLTGR KVVTVLVRDG REWEIVNQDN HYSPHFQEIR MLKKVVSVHP GDVLITSCTY NTEDRELATV GGFGILEEMC VNYVHYYPQT QLELCKSAVD AGFLQKYFHL INRFNNEDVC TCPQASVSQQ FTSVPWNSFN RDVLKALYSF APISMHCNKS SAVRFQGEWN LQPLPKVIST LEEPTPQCPT SQGRSPAGPT VVSIGGGKG

    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.

    Dbh Human

About Hydroxylase:

Hydroxylases are enzymes which add a hydroxyl group to a different type of organic compounds. The addition of this group is the first stage of aerobic oxidative degradation. Essentially, every time an organic compound begins the process of oxidative degradation in air, hydroxylases are at work on the process known as hydroxylation. This process is at work in the human body all the time and is a vital part of kidney function and the overall detoxification process of the human body. Hydroxylation facilitates the conversion of lipophilic compounds into hydrophilic, water-soluble products. These products can then be more readily removed by the kidneys, liver or skin and excreted.
Hydroxylases are also key components in the activation (or deactivation) of certain drugs such as steroids.

Hydroxylase Mechanism
Hydroxylases have a range of biological functions. All of which revolve around the insertion of oxygen into C-H bonds usually derived from atmospheric oxygen. Because oxygen itself is a slow and unselective hydroxylating agent, catalysts are required to speed up the process and introduce selectivity.

Hydroxylases Interactions and functions
Hydroxylases are perhaps best known for their interactions with proteins.
The residue most frequently hydroxylated in human proteins is proline owing to the abundance of collagen in the human body. Indeed, collagen makes up about 25–35% of the protein in the human body and contains a hydroxyproline at almost every 3rd residue in its amino acid sequence.
The process of hydroxylation occurs at the γ-C atom, and hydroxyproline is formed. Due to the highly electronegative effects of oxygen, this stabilizes the secondary structure of collagen. Proline hydroxylation is also a key component of hypoxia response by way of numerous hypoxia inducible factors. In some cases, proline may instead be hydroxylated instead on its β-C atom instead of the γ-C atom. Lysine may also be hydroxylated on its δ-C atom, to form hydroxylysine (Hyl).
These three reactions are catalyzed by significant multi-subunit enzymes. These are prolyl 4-hydroxylase, prolyl 3-hydroxylase and lysyl 5-hydroxylas respectively. Iron is required for these reactions as is α-ketoglutarate and, of course, molecular oxygen to carry out the oxidation. Ascorbic acid (vitamin C) is also used to return the iron to its reduced state. Deprivation of ascorbate leads to deficiencies in proline hydroxylation, undermining the stability of collagen.
Historically, this has led to the disease scurvy which has famously been mitigated by the use of fruits that are high vitamin C. Of course, the hydroxylation of proline is by far the only example of hydroxylase interaction in the human body.
Other key examples include Phenylalanine hydroxylase (PAH) which is found in the liver and catalyzes the hydroxylation of phenylalanine to tyrosine. Likewise, Tyrosine hydroxylase (TH) is found in the brain and in the adrenal gland where it catalyzes the conversion of tyrosine to 3,4-dihydroxyphenylalanine (DOPA) which is the initial step in the biosynthesis of dopamine, norepinephrine and epinephrine.