Search: 1000 results found for "Transgelin"

Description:

Transgelin Human Recombinant

SM22, SMCC, TAGLN1, WS3-10, Transgelin, Smooth muscle protein 22-alpha, SM22-alpha, TAGLN, DKFZp686B01212, DKFZp686P11128.

Product # :

PRO-851

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Description

TAGLN Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 221 amino acids (1-201 a.a.) and having a molecular mass of 24.8 kDa. The TAGLN is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TAGLN Human solution containing 20mM Tris-HCl pH-7.5, 1mM DTT & 20% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
TAGLN is a transformation and form-change responsive actin cross-linking/gelling protein that is part of the calponin family. TAGLN is expressed abundantly in fibroblasts and smooth muscle. TAGLN participates in calcium interactions and contractile properties of the cell that contribute to replicative senescence. Throughout embryogenesis, TAGLN is expressed in smooth, cardiac and skeletal muscle, but is limited during late fetal growth and adulthood to all vascular and visceral smooth muscle cells and low levels of expression in heart. TAGLN is downregulated in several transformed cell lines, showing that a decrease of TAGLN expression is an premature indicator of the onset of transformation.
Synonyms
SM22, SMCC, TAGLN1, WS3-10, Transgelin, Smooth muscle protein 22-alpha, SM22-alpha, TAGLN, DKFZp686B01212, DKFZp686P11128.
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 MANKGPSYGM SREVQSKIEK KYDEELEERL VEWIIVQCGP DVGRPDRGRL GFQVWLKNGV ILSKLVNSLY PDGSKPVKVP ENPPSMVFKQ MEQVAQFLKA AEDYGVIKTD MFQTVDLFEG KDMAAVQRTL MALGSLAVTK NDGHYRGDPN WFMKKAQEHK REFTESQLQE GKHVIGLQMG SNRGASQAGM TGYGRPRQII S.

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.

Description:

Transgelin-3 Human Recombinant

Transgelin 3, NP22, NP25, Neuronal protein 22, Neuronal protein NP25.

Product # :

PRO-946

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Description

TAGLN3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 219 amino acids (1-199) and having a molecular mass of 24.6 kDa.The TAGLN3 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The TAGLN3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
TAGLN3 holds a putative Actin-binding domain, two potential phosphorylation sites, two EF-hand motifs and a calponin-homology (CH) domain. TAGLN3 is homologic to transgelin and calponin, two cytoskeleton-interacting proteins. TAGLN3 is a member of the calponin family, and is co-localized with Actin and tubulin, which indicates that TAGLN3 has a part in neuronal plasticity or as a signaling protein. As a result of a wide-ranging expression pattern, TAGLN3 is able to take different roles in the developing and adult brain.
Synonyms
Transgelin 3, NP22, NP25, Neuronal protein 22, Neuronal protein NP25.
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 MANRGPSYGL SREVQEKIEQ KYDADLENKL VDWIILQCAE DIEHPPPGRA HFQKWLMDGT VLCKLINSLY PPGQEPIPKI SESKMAFKQM EQISQFLKAA ETYGVRTTDI FQTVDLWEGK DMAAVQRTLM ALGSVAVTKD DGCYRGEPSW FHRKAQQNRR GFSEEQLRQG QNVIGLQMGS NKGASQAGMT GYGMPRQIM

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.

Description:

Transgelin-2 Human Recombinant

Transgelin-2, SM22-alpha homolog, TAGLN2, KIAA0120, HA1756.

Product # :

PRO-124

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Description

TAGLN2 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 208 amino acids (13-199 a.a.) and having a molecular mass of 23.4kDa. The TAGLN2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TAGLN2 solution (1 mg/ml), 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Transgelin 2 (TAGLN2) is one of the earliest markers of differentiated smooth muscle. TAGLN2 contains a calponin like repeat and a calponin-homology (CH) domain. TAGLN2 is downregulated in some transformed cell lines, indicating that a reduction of transgelin expression may be an early indicator of the onset of transformation. TAGLN2 also binds actin, causing actin fibers to gel within minutes of binding. The binding of transgelin to actin occurs at a ratio of 1:6 actin monomers.
Synonyms
Transgelin-2, SM22-alpha homolog, TAGLN2, KIAA0120, HA1756.
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 MEVQQKIEKQ YDADLEQILI QWITTQCRKD VGRPQPGREN FQNWLKDGTV LCELINALYP EGQAPVKKIQ ASTMAFKQME QISQFLQAAE RYGINTTDIF QTVDLWEGKN MACVQRTLMN LGGLAVARDD GLFSGDPNWF PKKSKENPRN FSDNQLQEGK NVIGLQMGTN RGASQAGMTG YGMPRQIL.

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.

Description:

Pregnant Mare Serum Gonadotropin

Product # :

HOR-272

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Description

PMSG is a complex glycoprotein obtained from the serum of pregnant mares. This 43-63 kda protein is capable of supplementing and being substituted for the follicle stimulating and interstitial cell-stimulating hormone of the anterior pituitary gland in both the male and female. Thus PMSG-Intervet stimulates development of the ovarian follicle in the female.

Source

Serum of pregnant mares.

Formulation

The PMSG was lyophilized with no additives.

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Introduction
PMSG Hormone is a well know used hormone together with progestogen to increase ovulation just before to artificial insemination. PMSG hormone is a placental glycoprotein produced from the serum of pregnant mares. PMSG comprises of an alfa subunit and a beta subunit. PMSG hormone is secreted from endometrial cups within the pregnant mare uterus aging from 40 to 130 days into their maturation, and once extracted, it can been used to promote artificially estrus in female animals. These assemblies produce PMSG hormone to induce mare's ovarian and repsouctive structures. PMSG can induce the growth of follicles by ovaries and results in ovulatation. PMSG hormone has an about a 4 day half-life of bioactivity in species other than horses. The extended biological activity can cause ovarian stimulation and ovulation. However, PMSG use alone often causes cystic ovarian disease because of the unrestrained ovarian stimulation and due to the sugar molecules which decrease clearance of the hormone. PMSG is more likely to be used than other pituitary hormones due to the extended circulatory half-life. PMSG solely exhibits luteinizing hormone like activity, however in other animal classes it has FSH & LH like activity.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PMSG although stable at room temperature for 3 weeks, should be stored between 2-8°C.
Solubility
It is recommended to reconstitute the lyophilized PMSG in sterile 18M-cm H2O at a concentration of 1000 IU/ml, which can then be further diluted to other aqueous solutions.
Background
What is the molecular weight/Mw of PMSG Protein?
PMSG Protein has a total Mw of 43-63 kDa.

What is the source or expression system of PMSG Protein?
Serum of pregnant mares.

What is the Biological Activity of PMSG Protein?
The biological functionality of PMSG Protein will be determined in the future.

What applications can PMSG Protein be used in?
PMSG Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for PMSG Protein?
The endotoxin level is minimal, PMSG Protein was purified using conventional chromatography techniques.

Who supplies PMSG that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of PMSG?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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.

Description:

Triptorelin Acetate

Product # :

HOR-238

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Description

Triptorelin C64H82N18O13, Pyr-His-Trp-Ser-Tyr-D-Trp-Leu-Arg-Pro-Gly-NH2 is a synthetic analogue of gonadorelin (GnRH). As a result of the substitution of the 6th amino acid residue in the native molecule, the agonistic effect is more pronounced and the plasma half-life prolonged.

Formulation

The protein (1 mg/ml) was lyophilized with no additives.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Trp although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Trp should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Trp in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Background
What is the Purity of TRIPTORELIN Protein?
TRIPTORELIN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of TRIPTORELIN Protein?
The biological functionality of TRIPTORELIN Protein will be determined in the future.

What applications can TRIPTORELIN Protein be used in?
TRIPTORELIN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for TRIPTORELIN Protein?
The endotoxin level is minimal, TRIPTORELIN Protein was purified using conventional chromatography techniques.

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.

Description:

Prealbumin Human Recombinant

TTHY, TTR, ATTR, TBPA, Transthyretin, Prealbumin, PALB, HsT2651.

Product # :

PRO-771

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Description

Transthyertin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (21-147 a.a.) and having a molecular weight of 13.8kDa. The Transthyertin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Transthyertin protein solution contains 1x PBS, pH-7.4, and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Prealbumin is a thyroid hormone-binding protein that transports thyroxine from the bloodstream to the brain. Prealbumin is a carrier protein which transports thyroid hormones in the plasma and cerebrospinal fluid, and also transports retinol (vitamin A) in the plasma. Transthyretin consists of a tetramer of identical subunits and is dominantly produced in the liver. Mutations in Prealbumin are related to amyloid deposition, affecting predominantly peripheral nerve and/or the heart. The diseases caused by mutations include amyloidotic polyneuropathy, euthyroid hyperthyroxinaemia, amyloidotic vitreous opacities, cardiomyopathy, oculoleptomeningeal amyloidosis, meningocerebrovascular amyloidosis, and carpal tunnel syndrome. Prealbumin is an indicator of protein-energy malnutrition since it has a circulating half life of 2 days and reacts swiftly to changes in nutritional status.
Synonyms
TTHY, TTR, ATTR, TBPA, Transthyretin, Prealbumin, PALB, HsT2651.
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
MGPTGTGESK CPLMVKVLDA VRGSPAINVA VHVFRKAADD TWEPFASGKT SESGELHGLT TEEEFVEGIY KVEIDTKSYW KALGISPFHE HAEVVFTAND SGPRRYTIAA LLSPYSYSTT AVVTNPKE.

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.

Description:

Human Endothelin-3

EDN3, EDN-3, ET-3, ET3, WS4B, HSCR4, MGC15067, MGC61498, Endothelin-3, Preproendothelin-3, PPET3.

Product # :

HOR-309

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Description

EDN3 contains 21 amino acids having a molecular mass of 2643.08 Dalton, and the molecular formula is: C121H168N26O33S4. Disulfide bonds between cys-1 and cys-15 + cys-3 and cys-11.

Formulation

The protein (1mg/ml) was lyophilized with no additives.

Purity

Greater than 97.0% as determined by RP-HPLC.

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Introduction
EDN3 interacts with endothelin receptor B, on the surface of cells. Throughout embryonic development, EDN3 takes part in neural crest cells that migrate from the developing spinal cord to specific regions in the embryo, where they give rise to many different types of cells. EDN3 and EDN3R are necessary for the formation of nerves in the large intestine (enteric nerves) and melanocytes (produce melanin). Mutations in the EDN3 gene is linked with Waardenburg syndrome, type IV that is characterized by changes in skin, hair, and eye coloring. Mutations in the EDN3 gene is linked with Hirschsprung disease that causes severe constipation or intestinal blockage.
Synonyms
EDN3, EDN-3, ET-3, ET3, WS4B, HSCR4, MGC15067, MGC61498, Endothelin-3, Preproendothelin-3, PPET3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized EDN3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EDN3 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized EDN3 in sterile Acetic Acid not less than 0.5mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
H-Cys-Thr-Cys-Phe-Thr-Tyr-Lys-Asp-Lys-Glu-Cys-Val-Tyr-Tyr-Cys-His-Leu-Asp-Ile-Ile-Trp-OH.
Peptide Content
88%.

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.

Description:

Semenogelin I Human Recombinant

CT103, dJ172H20.2, SEMG, SGI, Semenogelin-1, Semenogelin I, SEMG1.

Product # :

PRO-1732

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Description

SEMG1 Human Recombinant produced in E. coli is a single polypeptide chain containing 462 amino acids (24-462) and having a molecular mass of 52kDa. SEMG1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The SEMG1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.5M NaCl, 10% glycerol, 250mM Imidazole, 0.1mM PMSF and 1mM DTT.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
SEMG1 is the predominant protein in semen. The secreted protein takes part in the formation of a gel matrix which encases ejaculated spermatozoa. The prostate-specific antigen (PSA) protease processes SEMG1 into smaller peptides, with each possibly having a separate function. The proteolysis process breaks down the gel matrix and allows the spermatozoa to shift more freely. 2 transcript variants encoding different isoforms have been found for SEMG1.
Synonyms
CT103, dJ172H20.2, SEMG, SGI, Semenogelin-1, Semenogelin I, SEMG1.
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 MGSQKGGSKG RLPSEFSQFP HGQKGQHYSG QKGKQQTESK GSFSIQYTYH VDANDHDQSR KSQQYDLNAL HKTTKSQRHL GGSQQLLHNK QEGRDHDKSK GHFHRVVIHH KGGKAHRGTQ NPSQDQGNSP SGKGISSQYS NTEERLWVHG LSKEQTSVSG AQKGRKQGGS QSSYVLQTEE LVANKQQRET KNSHQNKGHY QNVVEVREEH SSKVQTSLCP AHQDKLQHGS KDIFSTQDEL LVYNKNQHQT KNLNQDQQHG RKANKISYQS SSTEERRLHY GENGVQKDVS QSSIYSQTEE KAQGKSQKQI TIPSQEQEHS QKANKISYQS SSTEERRLHY GENGVQKDVS QRSIYSQTEK LVAGKSQIQA PNPKQEPWHG ENAKGESGQS TNREQDLLSH EQKGRHQHGS HGGLDIVIIE QEDDSDRHLA QHLNNDRNPL FT.

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.

Description:

Translin Human Recombinant

Translin, TRSLN, BCLF-1, REHF-1, RCHF1, TBRBP, Recombination Hotspot-binding Protein, Recombination Hotspot Associated factor.

Product # :

PRO-271

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Description

TSN produced in E.Coli is a single, non-glycosylated polypeptide chain containing 228 amino acids (1-228a.a.) and having a molecular mass of 26.1kDa. TSN is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TSN protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 100mM NaCl, and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Translin is a DNA and RNA binding protein that identifies specifically preserved target sequences at the breakpoint junction of chromosomal translocations. TSN forms a ring-shaped configuration, that is in charge of DNA binding, and in addition has a leucine zipper motif, which is believed to assist TSN to form dimers. TSN exports specific mRNAs out of the nucleus, reinforced by its localization in both the nuclei and cytoplasm of neurons, and regulates their translation.
Synonyms
Translin, TRSLN, BCLF-1, REHF-1, RCHF1, TBRBP, Recombination Hotspot-binding Protein, Recombination Hotspot Associated factor.
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
MSVSEIFVEL QGFLAAEQDI REEIRKVVQS LEQTAREILT LLQGVHQGAG FQDIPKRCLK AREHFGTVKT HLTSLKTKFP AEQYYRFHEH WRFVLQRLVF LAAFVVYLET ETLVTREAVT EILGIEPDRE KGFHLDVEDY LSGVLILASE LSRLSVNSVT AGDYSRPLHI STFINELDSG FRLLNLKNDS LRKRYDGLKY DVKKVEEVVY DLSIRGFNKE TAAACVEK.

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.

Description:

Transforming Growth Factor-Beta 1 Human Recombinant, HEK

Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, LAP, TGFB1.

Product # :

CYT-1260

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Description

TGFB1 Human Recombinant produced in 293 cells is a glycosylated homodimer polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.0kDa. The TGFB1 is purified by proprietary chromatographic techniques.

Source

HEK 293 cells.

Formulation

Lyophilized from a sterile filtered solution containing TFA (0.1%).

Purity

Greater than 98.0% as determined by: (a) Analysis by HPLC. (b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependent inhibition of IL-4-induced proliferation of HT-2 cells is ≤ 0.05 ng/ml, corresponding to a specific activity of ≥ 2 x 10⁷ units/mg.

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Synonyms
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, LAP, TGFB1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGFB1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB1 Human should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized TGFB1 in sterile in 18MΩ-cm H2O at a concentration of 0.1 mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ALDTNYCFSS TEKNCCVRQL YIDFRKDLGW KWIHEPKGYH ANFCLGPCPY IWSLDTQYSK VLALYNQHNP GASAAPCCVP QALEPLPIVY YVGRKPKVEQ LSNMIVRSCK CS.
Background
Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. 3 TGF Betas have been identified in mammals: TGF Beta 1, TGF Beta 2 and TGF Beta 3. each are synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.

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.

Description:

Transferrin Human Recombinant

Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.

Product # :

PRO-747

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Description

Recombinant Human Transferrin produced in Plant is a non-glycosylated, polypeptide chain containing 679 amino acids and having a molecular mass of 76 kDa. The Recombinant Human Transferrin is purified by proprietary chromatographic techniques.

Source

Oryza sativa (rice).

Formulation

The protein (1mg/ml) was lyophilized with no additives.

Purity

Purity as determined by SDS-PAGE is 97%.

Biological Activity

One mg of Recombinant Human Transferrin will bind to approximately 2 micrograms of Fe.

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Introduction
Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
Physical Appearance
Sterile Filtered lyophilized (freeze-dried) powder.
Stability
Lyophilized Transferrin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Transferrin Human Recombinant should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
Stock solutions can be prepared by dissolving gently into PBS for several minutes. Recommended stock concentrations are 5mg/ml to 20 mg/ml in PBS, though others can be used as well. Please try to avoid the formation of bubbles when dissolving the protein. Sterile filter through 0.2µm filter.

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.

Description:

Trefoil Factor-2 Human Recombinant

TFF-2, Spasmolytic polypeptide, Spasmolysin, SML1, Trefoil factor 2, SP, TFF2.

Product # :

CYT-612

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Description

TFF-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 106 amino acids (24-129) and having a total molecular mass of 12 kDa. TFF2 Human Recombinant includes a 40-amino acid trefoil motif containing three conserved intramolecular disulfide bonds and was purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TFF2 protein was lyophilized from 0.4μm filtered solution at a concentration of 1mg/mL containing 1x PBS pH-7.4.

Purity

Greater than 97.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Determined by its ability to chemoattract human MCF-7 cells using a concentration 1.0-10.0 ng/ml.

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Introduction
Proteins of the TFF family are characterized by obtaining a minimum of 1 copy of the trefoil motif, a 40-amino acid domain that contains 3 conserved disulfides. Trefoil Factors are stable secretory proteins expressed in gastrointestinal mucosa which protect the mucosa from insults, stabilize the mucus layer and affect healing of the epithelium.TFF2 inhibits gastric acid motility & secretion. TFF2 stabilizes glycoproteins in the mucus gel through interactions with carbohydrate side chains.
Synonyms
TFF-2, Spasmolytic polypeptide, Spasmolysin, SML1, Trefoil factor 2, SP, TFF2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TFF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF2 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized TFF2 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
EKPSPCQCSR LSPHNRTNCG FPGITSDQCF DNGCCFDSSV TGVPWCFHPL PKQESDQCVM EVSDRRNCGY PGISPEECAS RKCCFSNFIF EVPWCFFPKSVEDCHY.

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.

Description:

Tesamorelin

Product # :

HOR-062

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Quantity :

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Description

Tesamorelin is a synthetic single, non-glycosylated polypeptide chain containing 44 amino acids, having a molecular mass of 5135.78 Dalton and a Molecular formula of C221H366N72O67S.

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 97.0% as determined by analysis by RP-HPLC.

More Info

Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Tesamorelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Tesamorelin should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Tesamorelin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
trans-3-hexenoyl-Tyr-Ala-Asp-Ala-IlePhe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala-Arg-LysLeu-Leu-Gln-Asp-Ile-Met-Ser-Arg-Gln-Gln-Gly-Glu-Ser-Asn-Gln-GluArg-Gly-Ala-Arg-Ala-Arg-Leu-NH2.
Background
Tesamorelin is a growth hormone-releasing hormone (GHRH) analogue. Tesamorelin stimulates the pituitary gland to produce endogenous growth hormone, which targets visceral adipose tissue. Tesamorelin has evolved from a HIV treatment into an effective metabolic and regenerative therapy.

What is the molecular weight/Mw of TESAMORELIN Protein?
TESAMORELIN Protein has a total Mw of 5.135kDa.

What is the Purity of TESAMORELIN Protein?
TESAMORELIN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of TESAMORELIN Protein?
The biological functionality of TESAMORELIN Protein will be determined in the future.

What is the amino acid sequence of TESAMORELIN Protein?
trans-3-hexenoyl-Tyr-Ala-Asp-Ala-IlePhe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala-Arg-LysLeu-Leu-Gln-Asp-Ile-Met-Ser-Arg-Gln-Gln-Gly-Glu-Ser-Asn-Gln-GluArg-Gly-Ala-Arg-Ala-Arg-Leu-NH2.

What applications can TESAMORELIN Protein be used in?
TESAMORELIN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for TESAMORELIN Protein?
The endotoxin level is minimal, TESAMORELIN Protein was purified using conventional chromatography techniques.

Who supplies TESAMORELIN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of TESAMORELIN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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.

Description:

Transforming Growth Factor-Beta 1 Human Recombinant

Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, LAP, TGFB1.

Product # :

CYT-716

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Description

TGFB1 Human Recombinant produced in CHO cells is a glycosylated homodimeric polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.6kDa. The TGFB1 is purified by proprietary chromatographic techniques.

Source

CHO cells.

Formulation

Lyophilized from a sterile filtered solution containing 0.1 % trifluoroacetic acid (TFA) And trehalose (1:20 protein to Trehalose ratio).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependent inhibition of IL-4-induced proliferation of HT-2 cells is 0.142ng/ml, corresponding to a specific activity of 7.4x10⁶units/mg.

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Introduction
Transforming growth factor betas (TGFBetas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
Synonyms
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, LAP, TGFB1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGFB1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB1 Human should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized TGFB1 in sterile 10mM HCl at a concentration of 0.1 mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ALDTNYCFSS TEKNCCVRQL YIDFRKDLGW KWIHEPKGYH ANFCLGPCPY IWSLDTQYSK VLALYNQHNP GASAAPCCVP QALEPLPIVY YVGRKPKVEQ LSNMIVRSCK CS.
Background
Title: Transforming Growth Factor-Beta 1 Human Recombinant: A Promising Tool for Biomedical Research
Abstract:

Transforming Growth Factor-Beta 1 (TGF-β1) is a crucial cytokine involved in diverse cellular processes. This research paper provides an in-depth analysis of human recombinant TGF-β1, focusing on its production, purification, and applications in biomedical research. The paper discusses the significance of TGF-β1 in tissue engineering, regenerative medicine, and immunology. Furthermore, it elucidates the potential therapeutic implications of recombinant TGF-β1 in various diseases and highlights ongoing research in the field. The information presented in this paper aims to enhance the understanding of TGF-β1 and its utility as a research tool in biomedical sciences.
Introduction:

Transforming Growth Factor-Beta 1 (TGF-β1) is a multifunctional cytokine that regulates cellular processes such as cell growth, differentiation, and immune modulation. Human recombinant TGF-β1 is synthesized using genetic engineering techniques, enabling the production of large quantities of biologically active protein for research purposes.
Production and Purification:

Recombinant TGF-β1 is typically produced in expression systems such as bacteria, yeast, or mammalian cells. The protein is then purified using various chromatographic techniques to obtain a highly pure and active form. Quality control measures ensure the biological activity and integrity of the recombinant protein.
Biomedical Applications:

Human recombinant TGF-β1 has found broad applications in biomedical research. In tissue engineering and regenerative medicine, it plays a critical role in promoting cell proliferation, extracellular matrix production, and tissue repair. TGF-β1 is also involved in immune modulation, influencing immune cell differentiation and function. Recombinant TGF-β1 is a valuable tool for studying these processes and developing therapeutic interventions.
Therapeutic Implications:

The dysregulation of TGF-β1 signaling is associated with various diseases, including fibrosis, cancer, and autoimmune disorders. Recombinant TGF-β1 offers potential therapeutic applications through its ability to modulate cellular responses. Ongoing research aims to develop targeted therapies that specifically regulate TGF-β1 signaling for the treatment of these conditions.
Conclusion:

Human recombinant TGF-β1 holds immense potential as a research tool in biomedical sciences. Its production, purification, and applications in tissue engineering, regenerative medicine, and immunology contribute to advancing our understanding of cellular processes and disease mechanisms. With ongoing research, recombinant TGF-β1 may pave the way for novel therapeutic strategies in various medical fields.

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.

Description:

Trefoil Factor-2 Human Recombinant, His Tag

TFF-2, Spasmolytic polypeptide, Spasmolysin, SML1, Trefoil factor 2, SP, TFF2.

Product # :

CYT-611

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Description

TFF-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 116 amino acids (24-129) which includes a 10 amino acid His Tag fused at N-terminus and having a total molecular mass of 13.2 kDa. TFF2 Human Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TFF2 protein was lyophilized from 0.4μm filtered solution at a concentration of 0.5mg/ml containing 20mM Tris pH-7.5, and 20mM NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Proteins of the TFF family are characterized by obtaining a minimum of 1 copy of the trefoil motif, a 40-amino acid domain that contains 3 conserved disulfides. Trefoil Factors are stable secretory proteins expressed in gastrointestinal mucosa which protect the mucosa from insults, stabilize the mucus layer and affect healing of the epithelium.TFF2 inhibits gastric acid motility & secretion. TFF2 stabilizes glycoproteins in the mucus gel through interactions with carbohydrate side chains.
Synonyms
TFF-2, Spasmolytic polypeptide, Spasmolysin, SML1, Trefoil factor 2, SP, TFF2.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TFF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF2 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHAS EKPSPCQCSR LSPHNRTNCG FPGITSDQCF DNGCCFDSSV TGVPWCFHPL PKQESDQCVM EVSDRRNCGY PGISPEECAS RKCCFSNFIF EVPWCFFPKSVEDCHY.

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.

Description:

Tubulointerstitial Nephritis Antigen Like 1 Human Recombinant

Tubulointerstitial nephritis antigen-like isoform 1, TINAGL1, Tubulointerstitial nephritis antigen-like, Glucocorticoid-inducible protein 5, Oxidized LDL-responsive gene 2 protein, OLRG-2, Tubulointerstitial nephritis antigen-related protein, TIN Ag-related protein, TIN-Ag-RP, GIS5, LCN7, OLRG2, TINAGL, PP6614, PSEC0088, UNQ204/PRO230.

Product # :

PRO-1675

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Description

800x600 TINAGL1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 469 amino acids (22-467) and having a molecular mass of 52.5 kDa.TINAGL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TINAGL1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Tubulointerstitial Nephritis Antigen Like 1 also known as TINAGL1 is similar in sequence to tubulointerstitial nephritis antigen, a secreted glycoprotein which is identified by antibodies in several types of immune-related tubulointerstitial nephritis. Three transcript variants encoding different isoforms are known for TINAGL1.
Synonyms
Tubulointerstitial nephritis antigen-like isoform 1, TINAGL1, Tubulointerstitial nephritis antigen-like, Glucocorticoid-inducible protein 5, Oxidized LDL-responsive gene 2 protein, OLRG-2, Tubulointerstitial nephritis antigen-related protein, TIN Ag-related protein, TIN-Ag-RP, GIS5, LCN7, OLRG2, TINAGL, PP6614, PSEC0088, UNQ204/PRO230.
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 MGSAQQGRGR RELAPGLHLR GIRDAGGRYC QEQDLCCRGR ADDCALPYLG AICYCDLFCN RTVSDCCPDF WDFCLGVPPP FPPIQGCMHG GRIYPVLGTY WDNCNRCTCQ ENRQWQCDQE PCLVDPDMIK AINQGNYGWQ AGNHSAFWGM TLDEGIRYRL GTIRPSSSVM NMHEIYTVLN PGEVLPTAFE ASEKWPNLIH EPLDQGNCAG SWAFSTAAVA SDRVSIHSLG HMTPVLSPQN LLSCDTHQQQ GCRGGRLDGA WWFLRRRGVV SDHCYPFSGR ERDEAGPAPP CMMHSRAMGR GKRQATAHCP NSYVNNNDIY QVTPVYRLGS NDKEIMKELM ENGPVQALME VHEDFFLYKG GIYSHTPVSL GRPERYRRHG THSVKITGWG EETLPDGRTL KYWTAANSWG PAWGERGHFR IVRGVNECDI ESFVLGVWGR VGMEDMGHH.

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.

Description:

Tissue Transglutaminase Human Recombinant

Protein gamma-glutamyltransferase 2, EC 2.3.2.13, Tissue transglutaminase, TGase C, TGC, TG(C), Transglutaminase-2, TGase-H, TG2, TGM2.

Product # :

ENZ-394

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Description

Tissue Transglutaminase Human Recombinant produced in E.coli is a non-glycosylated, polypeptide chain having a molecular mass of 78,018 Dalton. tTG is expressed with a -6xHis tag and purified by proprietary chromatographic techniques. By point mutation of the active center the catalytic transglutaminase activity has been eliminated, resulting in increased stability during storage and coating.

Source

Escherichia Coli.

Formulation

TGM2 is supplied in 16mM HEPES buffer pH-8.0, 400mM NaCl, and 20% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Celiac disease is an enteropathy that is characterized by intestinal lesions of variable severity. Tissue-type transglutaminase (tTG) is believed to be the predominant autoantigen for celiac disease and the corresponding autoantibodies show higher sensitivity and specificity than anti-gliadin antibodies. Highly pure recombinant human tTG is now available to replace the traditionally used tTG fraction from guinea pig.
Tissue-type transglutaminase antigens have been specifically modified for improved handling: exchange of an active site amino acid eliminates the protein cross-linking activity of the enzyme, while maintaining the native three-dimensional structure and the enzyme's secondary GTPase activity. This engineering assures reproducible properties of the antigen preparations through the absence of variable and ill-defined covalent aggregates of tTG antigen and host cell proteins.
Synonyms
Protein gamma-glutamyltransferase 2, EC 2.3.2.13, Tissue transglutaminase, TGase C, TGC, TG(C), Transglutaminase-2, TGase-H, TG2, TGM2.
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. Avoid multiple freeze-thaw cycles.

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.

Description:

Tissue Transglutaminase Human Recombinant, Sf9

Protein-glutamine gamma-glutamyltransferase 2, EC 2.3.2.13, Tissue transglutaminase, TGase C, TGC, TG(C), Transglutaminase-2, TGase-H, TG2, TGM2.

Product # :

ENZ-303

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Description

Tissue Transglutaminase Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a molecular mass of 83 kDa. tTG is expressed with a -6xHis tag and purified by proprietary chromatographic techniques. By point mutation of the active center the catalytic transglutaminase activity has been eliminated, resulting in increased stability during storage and coating.

Source

Sf9 insect cells.

Formulation

TGM2 is supplied in 16mM HEPES buffer pH-8.0, 320mM NaCl and 20% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
Celiac disease is an enteropathy that is characterized by intestinal lesions of variable severity. Tissue-type transglutaminase (tTG) is believed to be the predominant autoantigen for celiac disease and the corresponding autoantibodies show higher sensitivity and specificity than anti-gliadin antibodies. Highly pure recombinant human tTG is now available to replace the traditionally used tTG fraction from guinea pig.
Tissue-type transglutaminase antigens have been specifically modified for improved handling: exchange of an active site amino acid eliminates the protein cross-linking activity of the enzyme, while maintaining the native three-dimensional structure and the enzyme's secondary GTPase activity. This engineering assures reproducible properties of the antigen preparations through the absence of variable and ill-defined covalent aggregates of tTG antigen and host cell proteins.
Synonyms
Protein-glutamine gamma-glutamyltransferase 2, EC 2.3.2.13, Tissue transglutaminase, TGase C, TGC, TG(C), Transglutaminase-2, TGase-H, TG2, TGM2.
Stability
Store at 4°C if entire vial will be used within 2-4weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

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.

Description:

Holo Transferrin Human Recombinant

Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.

Product # :

PRO-2844

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Description

Human Holo Transferrin Recombinant produced in HEK Cells is a glycosylated polypeptide containing 679 amino acids and having a Mw of of 76 kDa.

Source

HEK Cells

Formulation

The protein was lyophilized from 1x PBS pH-7.4.

Purity

Protein is >98% pure as determined by 10% PAGE (coomassie staining).

Biological Activity

The activity of Recombinant Holo Transferrin was determined by the proliferation assay using MDCK cells stimulated with recombinant human Holo Transferrin. The protein was found biologically active

sds-page, activity

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Introduction
Recombinant Human Holo Transferrin is an iron-delivery signaling protein which functions in the delivery of Fe³⁺ iron to cells using transferrin receptor-1 (TfR1/CD71).
Holo-transferrin binds TfR1, undergoes receptor-mediated endocytosis and the iron is released intracellularly. Transferrin Human Recombinant is crucial for brain and the nervous system, neuronal mitochondrial metabolism, neurotransmitter synthesis, oligodendrocyte myelination and synaptic activity. Recombinant holo-transferrin can be used in cell therapy, stem-cell expansion, CHO production, or drug-delivery platforms.
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
Physical Appearance
Sterile Filtered lyophilized (freeze-dried) powder.
Stability
Store the lyophilized Holo Transferrin recombinant between 2-8°C, do not freeze.
Upon reconstitution Holo Transferrin should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Holo Transferrin recombinant in sterile 18MΩ-cm H2O at 1mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VPDKTVRWCA VSEHEATKCQ SFRDHMKSVI PSDGPSVACV KKASYLDCIR AIAANEADAV TLDAGLVYDA YLAPNNLKPV VAEFYGSKED PQTFYYAVAV VKKDSGFQMN QLRGKKSCHT GLGRSAGWNI PIGLLYCDLP EPRKPLEKAV ANFFSGSCAP CADGTDFPQL CQLCPGCGCS TLNQYFGYSG AFKCLKDGAG DVAFVKHSTI FENLANKADR DQYELLCLDN TRKPVDEYKD CHLAQVPSHT VVARSMGGKE DLIWELLNQA QEHFGKDKSK EFQLFSSPHG KDLLFKDSAH GFLKVPPRMD AKMYLGYEYV TAIRNLREGT CPEAPTDECK PVKWCALSHH ERLKCDEWSV NSVGKIECVS AETTEDCIAK IMNGEADAMS LDGGFVYIAG KCGLVPVLAE NYNKSDNCED TPEAGYFAVA VVKKSASDLT WDNLKGKKSC HTAVGRTAGW NIPMGLLYNK INHCRFDEFF SEGCAPGSKK DSSLCKLCMG SGLNLCEPNN KEGYYGYTGA FRCLVEKGDV AFVKHQTVPQ NTGGKNPDPW AKNLNEKDYE LLCLDGTRKP VEEYANCHLA RAPNHAVVTR KDKEACVHKI LRQQQHLFGS NVTDCSGNFC LFRSETKDLL FRDDTVCLAK LHDRNTYEKY LGEEYVKAVG NLRKCSTSSL LEACTFRRP.

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.

Description:

Transferrin Human Recombinant, CHO

Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.

Product # :

PRO-2782

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Shipped at Room temp

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Description

Recombinant Human Transferrin produced in CHO cells is a glycosylated, polypeptide chain containing having a molecular mass of 76 kDa. Human Transferrin has homologous C and N-terminal domains, each of which binds one ion of ferric iron.

Source

Chinese Hamster Ovary cells.

Formulation

Transferrin solution contains 0.05% NaN3 and PBS.

Purity

Protein is >95% pure as determined by 10% PAGE (coomassie staining).

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Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
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.
Applications
Immunoassay, cell culture.
Background
Human recombinant transferrin, a glycoprotein responsible for iron transport in the body, has gained increasing attention in the fields of biomedicine and health sciences. This multifaceted protein serves as an essential carrier of iron and is crucial for cellular growth, immunity, and various physiological processes. Its recombinant form, produced through advanced biotechnological methods, offers several advantages for therapeutic and research purposes. This study aims to provide a comprehensive exploration of human recombinant transferrin, shedding light on its various functions and potential applications in health and biomedicine.
The primary objective of this research is to elucidate the essential role of transferrin in iron homeostasis and its significance for human health. In vitro and in vivo experiments will be conducted to investigate how recombinant transferrin interacts with cellular receptors, regulates iron uptake, and influences cellular proliferation. Understanding these mechanisms is fundamental for deciphering the complexities of iron metabolism and its impact on health and disease.
The second objective is to assess the clinical relevance of human recombinant transferrin in medical interventions. Clinical trials and studies involving individuals with iron-related disorders, such as iron-deficiency anemia, will be conducted to evaluate the efficacy and safety of recombinant transferrin supplementation. These investigations may provide insights into the use of recombinant transferrin as a therapeutic agent in various clinical settings.
The third objective is to explore the broader implications of human recombinant transferrin in biomedicine and research. Research will investigate its potential roles in areas beyond iron transport, such as drug delivery, tissue engineering, and cell culture. Understanding the multifaceted properties of recombinant transferrin may open new avenues for innovative approaches in various medical specialties and scientific research.
By delving into the diverse functions of human recombinant transferrin, this research aims to expand our understanding of its physiological roles and clinical applications. The findings may contribute to the development of innovative strategies for the treatment of iron-related disorders and the advancement of biomedicine and scientific research.

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.

Description:

Transforming Growth Factor-Beta 1 (113 a.a.) Human Recombinant

Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1.

Product # :

CYT-679

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Quantity :

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Shipped with Ice Packs

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Description

TGF-b 1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 113 amino acids (279-390 a.a.) and having a total molecular mass of 12.9 kDa. TGF-b 1 (113 a.a.) is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TGF-b 1 solution contains 10mM Sodium Citrate (pH3.5) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Transforming growth factor betas (TGFBetas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
Synonyms
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1.
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
MALDTNYCFS STEKNCCVRQ LYIDFRKDLG WKWIHEPKGY HANFCLGPCP YIWSLDTQYS KVLALYNQHN PGASAAPCCV PQALEPLPIVYYVGRKPKVE QLSNMIVRSC KCS.
Background
Title: Transforming Growth Factor-Beta 1 (113 a.a.) Human Recombinant: A Key Regulator of Cellular Processes with Therapeutic Potential
Abstract:

Transforming Growth Factor-Beta 1 (TGF-β1) is a multifunctional cytokine that plays a crucial role in various cellular processes, including cell growth, differentiation, and immune modulation. The development of TGF-β1 human recombinant proteins has provided valuable tools for studying its biological functions and therapeutic applications. This research paper explores the production process, characteristics, and potential therapeutic uses of TGF-β1 human recombinant, highlighting its importance and clinical significance.
Introduction:

TGF-β1 is a pivotal cytokine involved in numerous physiological and pathological processes, such as embryonic development, tissue repair, and immune regulation. Harnessing the therapeutic potential of TGF-β1 has been facilitated by the development of TGF-β1 human recombinant proteins using recombinant DNA technology. These recombinant proteins have become valuable tools for investigating the biological functions of TGF-β1 and exploring its therapeutic applications.
Production Process and Characteristics:

TGF-β1 human recombinant proteins are produced using recombinant DNA technology, allowing for the expression of the TGF-β1 gene in different host systems. The resulting recombinant proteins possess similar structural and functional characteristics to native TGF-β1. They exhibit the ability to bind to the TGF-β receptor, initiate intracellular signaling pathways, and modulate various cellular responses.
Therapeutic Applications:

TGF-β1 human recombinant proteins have shown promise in a wide range of therapeutic applications. They have been investigated for their potential in tissue regeneration and wound healing, as TGF-β1 plays a crucial role in promoting cell proliferation and extracellular matrix production. Additionally, TGF-β1 has been studied in the context of fibrotic diseases, such as pulmonary fibrosis and liver fibrosis, where it is implicated in the fibrotic cascade. Furthermore, TGF-β1 has been explored as a potential target for antitumor therapies due to its involvement in tumor progression and immune evasion.
Advantages and Challenges:

The use of TGF-β1 human recombinant proteins offers several advantages, including the ability to study and manipulate its biological functions in a controlled manner. Recombinant proteins also provide a consistent and reproducible source of TGF-β1, overcoming the challenges associated with sourcing native TGF-β1 from biological samples. However, challenges remain in optimizing production processes, ensuring correct protein folding, and maintaining protein stability.
Conclusion:

TGF-β1 human recombinant proteins have emerged as valuable tools for studying the biological functions of TGF-β1 and exploring its therapeutic applications. The production of TGF-β1 recombinant proteins using recombinant DNA technology allows for the investigation of its diverse roles in cellular processes. The therapeutic potential of TGF-β1 human recombinant proteins extends to tissue regeneration, fibrotic diseases, and cancer research. Continued research and development efforts are essential to further optimize production processes, address challenges, and fully exploit the clinical benefits of TGF-β1 human recombinant proteins.

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.

Description:

Tubulin Polyglutamylase Complex Subunit 2 Human Recombinant

Tubulin polyglutamylase complex subunit 2, C18orf10; HMFN0601, HsT3006, L17, PGs2, TPGS2.

Product # :

PRO-1668

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TPGS2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-300) and having a molecular mass of 35.7kDa.TPGS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TPGS2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol, 2mM DTT and 2mM EDTA.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Tubulin Polyglutamylase Complex Subunit 2 (TPGS2) is a component of the neuronal polyglutamylase complex, which takes part in post-translational addition of glutamate residues to C-terminal tubulin tails. Alternatively spliced transcript variants encoding multiple isoforms have been monitored for TPGS2.
Synonyms
Tubulin polyglutamylase complex subunit 2, C18orf10; HMFN0601, HsT3006, L17, PGs2, TPGS2.
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 MGSMEEEASS PGLGCSKPHL EKLTLGITRI LESSPGVTEV TIIEKPPAER HMISSWEQKN NCVMPEDVKN FYLMTNGFHM TWSVKLDEHI IPLGSMAINS ISKLTQLTQS SMYSLPNAPT LADLEDDTHE ASDDQPEKPH FDSRSVIFEL DSCNGSGKVC LVYKSGKPAL AEDTEIWFLD RALYWHFLTD TFTAYYRLLI THLGLPQWQY AFTSYGISPQ AKQWFSMYKP ITYNTNLLTE ETDSFVNKLD PSKVFKSKNK IVIPKKKGPV QPAGGQKGPS GPSGPSTSST SKSSSGSGNP TRK.

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.

Description:

TNF receptor-Associated Factor 1 Human Recombinant

TRAF-1, EBI6, Epstein-Barr virus-induced protein 6, TNF Receptor-Associated Factor 1, MGC:10353.

Product # :

PRO-834

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Description

TRAF1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 172 amino acids (266-416 a.a.) and having a molecular mass of 19.5 kDa. TRAF1 protein is fused to a 21 amino acid His tag at N-terminus and is purified by standard chromatography.

Source

Escherichia Coli.

Formulation

TRAF1 Human solution containing 20mM Tris-HCl pH-8, 0.1M NaCl, 1mM DTT & 20% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
TRAF1 is an adapter protein and signal transducer that connects members of the TNFR family to different signaling pathways by association with the receptor cytoplasmic domain and kinases. TRAF1 mediates activation of NF-kappa-B and JNK and participates in apoptosis. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2.
Synonyms
TRAF-1, EBI6, Epstein-Barr virus-induced protein 6, TNF Receptor-Associated Factor 1, MGC:10353.
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 MDGTFLWKIT NVTRRCHESA CGRTVSLFSP AFYTAKYGYK LCLRLYLNGD GTGKRTHLSL FIVIMRGEYD ALLPWPFRNK VTFMLLDQNN REHAIDAFRP DLSSASFQRP QSETNVASGC PLFFPLSKLQ SPKHAYVKDD TMFLKCIVET ST.

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.

Description:

Twisted Gastrulation Protein Human Recombinant

Twisted Gastrulation BMP Signaling Modulator 1, TSG, Twisted Gastrulation Homolog 1 (Drosophila), Twisted Gastrulation Protein Homolog 1, Twisted Gastrulation Homolog 1, TWSG1.

Product # :

CYT-873

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Shipped at Room temp

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Description

TWSG1 Human Recombinant (26-223) produced in CHO is a single, glycosylated, polypeptide chain containing 198 amino acids and having a molecular mass ranging from 35-43kDa on SDS-PAGE due to glycosylation.The TWSG1 is purified by proprietary chromatographic techniques.

Source

CHO.

Formulation

Lyophilized from a 0.2µm filtered solution in PBS.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as measured by its ability to inhibit alkaline phosphatase production induced by rHuBMP-6 in mouse ATDC5 cells, is less than 16µg/ml.

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Introduction
Twisted gastrulation Protein (TSG) is a secreted, cysteine-rich protein which has a role in dorsal/ventral patterning in Drosophila and Xenopus by regulating BMP signaling. TSG functions as an agonist for BMP signaling by controlling the inhibitory actions of the BMP antagonist, Chordin/Sog, and the cleavage properties of the metalloprotease, xolloid/tolloid. TSG N-terminal domain binds BMP protein directly and displays BMP antagonist activity.
Synonyms
Twisted Gastrulation BMP Signaling Modulator 1, TSG, Twisted Gastrulation Homolog 1 (Drosophila), Twisted Gastrulation Protein Homolog 1, Twisted Gastrulation Homolog 1, TWSG1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TSG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TSG should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized TSG in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
CNKALCASDV SKCLIQELCQ CRPGEGNCSC CKECMLCLGA LWDECCDCVG MCNPRNYSDT PPTSKSTVEE LHEPIPSLFR ALTEGDTQLN WNIVSFPVAE ELSHHENLVS FLETVNQPHH QNVSVPSNNV HAPYSSDKEH MCTVVYFDDC MSIHQCKISC ESMGASKYRW FHNACCECIG PECIDYGSKT VKCMN CMF.

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.

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