Search: 1000 results found for "EGF"

Description:

Fibroblast Growth Factor-Basic Human Recombinant, His

Prostatropin, FGF-basic, fgf2, Basic FGF, HBGF-2, FGF-2, FGF-b.

Product # :

cyt-1270

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Description

Fibroblast Growth Factor-2 Human Recombinant (FGF-2) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 155 amino acids (134-288 a.a) and having a molecular mass of 18.1kDa.
The FGF2 is conjugated to 6xHis Tag at N-terminus and is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FGF2 Human His protein is provided at a concentration of 1mg/ml in PBS Ph-7.2.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
FGF2 Human has an important role in cell growth and tissue regeneration. Recent findings show that FGF2 and IGF-1 improve muscle stem cell growth, muscle regeneration, and functional recovery in an animal model of severe muscle loss. FGF2 accelerates wound closure, collagen deposition, and blood vessel formation in diabetic mice. FGF2 forms condensates inside the nucleus thus plays an important role in critical functions in cellular signaling and gene transcription.
Synonyms
Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.
Physical Appearance
Sterile Filtered colorless clear solution.
Stability
FGF-2 although stable at 4°C for 1 month, should be stored below -18°C.
Please prevent freeze thaw cycles.
Background
What is the major role of FGF2 Human His Tag?
FGF2 Human His Tag enables detection with anti-His antibodies in W.B. or suitable ELISA assays, without the need for an FGF2-specific antibody. FGF2 Human His Tag allows capture on metal-chelate plates or beads for binding studies in assay immobilization.
FGF2 stimulates growth of embryonic stem cells and induced pluripotent stem cells as well as stimulation of fibroblast and endothelial-cell growth.

What is the molecular weight / Mw of FGF2 Human His tag?
FGF2 Human His has a total Mw of 18.1kDa.

What is the source or expression system of FGF2 Human His?
E.Coli.

What is the Purity of FGF2 Human His?
FGF2 Human His is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF2 Human His?
The biological functionality of FGF2 Human His will be determined in the future.

What is the amino acid sequence of FGF2 Human His?
FGF2 Human His is composed from 134-288 amino acids.

What applications can FGF2 Human His be used in?
FGF2 Human His protein may be suitable for use in Western blot (WB) and ELISA, depending on the assay design.

What is the endotoxin level for FGF2 Human His?
The endotoxin level is minimal, FGF2 Human His was purified using conventional chromatography techniques.

Who supplies recombinant FGF2 Human His 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 FGF2 Human His?
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:

Vascular Endothelial Growth Factor Receptor-1 Human Recombinant

FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

Product # :

PKA-240

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Description

Soluble FLT1 Human Recombinant produced in baculovirus is monomeric, glycosylated, polypeptide containing 687 amino acids and having a molecular mass of 96 kDa. The soluble receptor protein contains only the first 6 extracellular domains, which contain all the information necessary for binding of VEGF.The FLT1 is purified by proprietary chromatographic techniques.

Source

Insect Cells.

Formulation

FLT1 was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.

Purity

Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The activity of FLT1 was determined by its ability to inhibit the VEGF (165)-induced proliferation of HUVECs.

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Introduction
Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.
Synonyms
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FLT-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FLT1 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 FLT1 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SKLK DPELSLKGTQ HIMQAGQTLH LQCRGEAAHK WSLPEMVSKE SERLSITKSA CGRNGKQFCS TLTLNTAQAN HTGFYSCKYL AVPTSKKKET ESAIYIFISD TGRPFVEMYS EIPEIIHMTE GRELVIPCRV TSPNITVTLK KFPLDTLIPD GKRIIWDSRK GFIISNATYK EIGLLTCEAT VNGHLYKTNY LTHRQTNTII DVQISTPRPV KLLRGHTLVL NCTATTPLNT RVQMTWSYPD EKNKRASVRR RIDQSNSHAN IFYSVLTIDK MQNKDKGLYT CRVRSGPSFK SVNTSVHIYD KAFITVKHRK QQVLETVAGK RSYRLSMKVK AFPSPEVVWL KDGLPATEKS ARYLTRGYSL IIKDVTEEDA GNYTILLSIK QSNVFKNLTA TLIVNVKPQI YEKAVSSFPD PALYPLGSRQ ILTCTAYGIP QPTIKWFWHP CNHNHSEARC DFCSNNEESF ILDADSNMGN RIESITQRMA IIEGKNKMAS TLVVADSRIS GIYICIASNK VGTVGRNISF YITDVPNGFH VNLEKMPTEG EDLKLSCTVN KFLYRDVTWI LLRTVNNRTM HYSISKQKMA ITKEHSITLN LTIMNVSLQD SGTYACRARN VYTGEEILQK KEITIRGEHC NKKAVFSRIS KFKSTRNDCT TQSNVKH

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 3 Mouse Recombinant

Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.

Product # :

CYT-143

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Description

TGF-β 3 Mouse Recombinant produced in E.Coli is a disulfide-linked homodimeric, non-glycosylated, polypeptide chain containing two 113 amino acid chains and having a total molecular mass of 25.7kDa. The TGF-β 3 is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Mouse TGFB3 protein solution contains 20% Ethanol and 10mM Acetic acid.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The activity is determined by the ability to induce chondrogenic differentiation.

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Introduction
Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. Three TGF Betas have been identified in mammals. TGF Beta 1, TGF Beta 2 and TGF Beta 3 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-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.
Physical Appearance
Sterile Filtered clear solution.
Stability
Mouse TGF-beta 3 although stable at room temperature for 3 weeks, should be stored at 4°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Amino Acid Sequence
MALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSADTTHST VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.718 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of TGF-b 3 as a Reference Standard.

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:

Hepatoma-Derived Growth Factor (32-285 a.a) Human Recombinant

Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF, DFNB39.

Product # :

CYT-294

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Description

HGF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 255 amino acids (32-285 a.a.) and having a molecular mass of 29.8kDa. HGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

HGF protein 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.

SDS-PAGE

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Introduction
Hepatocyte Growth Factor (HGF) is a multifunctional growth factor which regulates both cell growth and cell motility. It exerts a strong mitogenic effect on hepatocytes and primary epithelial cells. HGF synergizes with Interleukin-3 and GM-CSF to stimulate colony formation of hematopoietic progenitor cells in vitro and may, therefore, also modulate hematopoiesis.
Synonyms
Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF, DFNB39.
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
MQRKRRNTIH EFKKSAKTTL IKIDPALKIK TKKVNTADQC ANRCTRNKGL PFTCKAFVFD KARKQCLWFP FNSMSSGVKK EFGHEFDLYE NKDYIRNCII GKGRSYKGTV SITKSGIKCQ PWSSMIPHEH SYRGKDLQEN YCRNPRGEEG GPWCFTSNPE VRYEVCDIPQ CSEVECMTCN GESYRGLMDH TESGKICQRW DHQTPHRHKF LPERYPDKGF DDNYCRNPDG QPRPWCYTLD PHTRWEYCAI KTCET.
Background
What is the molecular weight/Mw of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein has a total Mw of 29.8kDa.

What is the source or expression system of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
Escherichia Coli.

What is the Purity of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein is >80% pure as determined by SDS-PAGE.

What is the Biological Activity of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
What is the molecular weight/Mw of HGF (32-285) HUMAN Protein? HGF (32-285) HUMAN Protein has a total Mw of 29.8kDa. What is the source or expression system of HGF (32-285) HUMAN Protein? Escherichia Coli. What is the Purity of HGF (32-285) HUMAN Protein? HGF (32-285) HUMAN Protein is >80% pure as determined by SDS-PAGE. What is the Biological Activity of HGF (32-285) HUMAN Protein? The biological functionality of HGF (32-285) HUMAN Protein will be determined in the future. What is the amino acid sequence of HGF (32-285) HUMAN Protein? MQRKRRNTIH EFKKSAKTTL IKIDPALKIK TKKVNTADQC ANRCTRNKGL PFTCKAFVFD KARKQCLWFP FNSMSSGVKK EFGHEFDLYE NKDYIRNCII GKGRSYKGTV SITKSGIKCQ PWSSMIPHEH SYRGKDLQEN YCRNPRGEEG GPWCFTSNPE VRYEVCDIPQ CSEVECMTCN GESYRGLMDH TESGKICQRW DHQTPHRHKF LPERYPDKGF DDNYCRNPDG QPRPWCYTLD PHTRWEYCAI KTCET. What applications can HGF (32-285) HUMAN Protein be used in? HGF (32-285) HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow. What is the endotoxin level for HGF (32-285) HUMAN Protein? The endotoxin level is minimal, HGF (32-285) HUMAN Protein was purified using conventional chromatography techniques.

What is the amino acid sequence of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
MQRKRRNTIH EFKKSAKTTL IKIDPALKIK TKKVNTADQC ANRCTRNKGL PFTCKAFVFD KARKQCLWFP FNSMSSGVKK EFGHEFDLYE NKDYIRNCII GKGRSYKGTV SITKSGIKCQ PWSSMIPHEH SYRGKDLQEN YCRNPRGEEG GPWCFTSNPE VRYEVCDIPQ CSEVECMTCN GESYRGLMDH TESGKICQRW DHQTPHRHKF LPERYPDKGF DDNYCRNPDG QPRPWCYTLD PHTRWEYCAI KTCET.

What applications can HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein be used in?
HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
The endotoxin level is minimal, HEPATOCYTE GROWTH FACTOR (32-285) HUMAN 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:

Ephrin A1 Human Recombinant

Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.

Product # :

PRO-971

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Description

EFNA1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 185 amino acids (19-182) and having a molecular mass of 21.6 kDa.EFNA1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The EFNA1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
EFNA1 belongs to the ephrin (EPH) family. The EPH subfamily is the biggest group of receptor protein kinases and they take part in vital nervous system function and development.
Synonyms
Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 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 MDRHTVFWNS SNPKFRNEDY TIHVQLNDYV DIICPHYEDH SVADAAMEQY ILYLVEHEEY QLCQPQSKDQ VRWQCNRPSA KHGPEKLSEK FQRFTPFTLG KEFKEGHSYY YISKPIHQHE DRCLRLKVTV SGKITHSPQA HVNPQEKRLA ADDPEVRVLH SIGHS

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:

FGFR1 Oncogene Partner (1-80 a.a.) Human Recombinant

FGFR1 oncogene partner, FGFR1OP, FOP.

Product # :

PKA-138

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Quantity :

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Shipped at Room temp

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Description

The FGFR1O PHuman is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The FGFR1OP His-Tagged Fusion Protein, produced in E. coli, is a 12kDa protein containing 80 amino acid residues of the FGFR1OP Human, 1-80 amino acids.

Source

Escherichia Coli.

Formulation

Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Synonyms
FGFR1 oncogene partner, FGFR1OP, FOP.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized FGFR1OP at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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 on cell culture.
Amino Acid Sequence
L MAATAAAVVA EEDTELRDLL VQTLENSGVL NRIKAELRAA VFLALEEQEK VENKTPLVNE SLRKFLNTKD GRLVASLVA
Background
FGFR1 oncogene partner also known as FGFR1OP is a leucine-rich member of the FGFR1OP family. The ensuing chimeric protein contains the N-terminal leucine-rich region of the FGFR1OP protein fused to the catalytic domain of FGFR1. The FGFR1OP plays a main role in normal proliferation and differentiation of the erythroid lineage.

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:

Pro-Nerve Growth Factor Human Recombinant

Human Pro-NGF, ProNGF, NGFB.

Product # :

CYT-426

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Shipped at Room temp

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Description

Pro-NGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 224 amino acids and having a molecular mass of 25 kDa.ProNGF Human Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ProNGF was lyophilized from a 0.2 μM filtered solution of 20m Tris-HCL, 0.5M NaCl, 5% Trehalose, 5% Mannitol. 0.01% Tween-80 and 1mM EDTA pH-8.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Synonyms
Human Pro-NGF, ProNGF, NGFB.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized ProNGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ProNGF 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 ProNGF in distilled water to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MEPHSESNVPAGHTIPQAHWTKLQHSLDTALRRARSAPAAAIAARVAGQTRNI
TVDPRLFKKRRLRSPRVLFSTQPPREAADTQDLDFEVGGAAPFNRTHRSKRS
SSHPIFHRGEFSVCDSVSVWVGDKTTATDIKGKEVMVLGEVNINNSVFKQYFFET
KCRDPNPVDSGCRGIDSKHWNSYCTTTHTFVKALTMDGKQAAWRFIRIDTAC
VCVLSRKAVRRA.
Background
Pro-Nerve Growth Factor Human Recombinant: Unveiling its Potential in Neuroregulation and Disease Pathogenesis
Abstract:
Pro-Nerve Growth Factor (Pro-NGF) human recombinant is a crucial precursor protein involved in neuronal development, survival, and degenerative processes. This research paper aims to provide a comprehensive analysis of Pro-NGF, including its characteristics, processing mechanisms, and implications in neuroregulation and disease pathogenesis. Additionally, innovative methodologies for the production and manipulation of Pro-NGF human recombinant are proposed, highlighting its potential as a therapeutic target for neurological disorders and neurodegenerative diseases.
Introduction:
Neuroregulation and maintenance of neuronal health are intricate processes governed by a network of signaling molecules. Pro-NGF, the precursor form of Nerve Growth Factor (NGF), acts as a key player in neuronal development, synaptic plasticity, and cell survival. This paper delves into the distinctive features of Pro-NGF and presents novel approaches for the production and manipulation of Pro-NGF human recombinant, aiming to unravel its role in neuroregulation and disease pathogenesis.
Characteristics and Processing Mechanisms:
Pro-NGF is initially synthesized as an inactive precursor, requiring proteolytic cleavage for conversion into mature NGF. The processing of Pro-NGF involves the action of proteases, such as furin, and the formation of distinct protein complexes. The balance between Pro-NGF and mature NGF levels plays a critical role in modulating neuronal function and fate, influencing processes such as neuronal survival, axonal growth, and synaptic plasticity.
Production and Manipulation of Pro-NGF Human Recombinant:
Efficient production methodologies and manipulation strategies are crucial for studying the role of Pro-NGF in neuroregulation and disease pathogenesis. Recombinant protein expression systems, including mammalian cell culture and bacterial expression systems, have been employed to produce functional Pro-NGF human recombinant. Techniques such as mutagenesis, protein purification, and specific inhibitors targeting Pro-NGF processing pathways enable the manipulation of Pro-NGF levels and investigation of its downstream effects.
Implications in Neuroregulation and Disease Pathogenesis:
Pro-NGF human recombinant holds significant potential in understanding the intricate mechanisms underlying neuroregulation and disease pathogenesis. Dysregulation of Pro-NGF processing and altered Pro-NGF/mature NGF ratios have been implicated in various neurological disorders, including Alzheimer's disease, Parkinson's disease, and ischemic stroke. Manipulating Pro-NGF levels and the balance between its mature form may offer therapeutic strategies for modulating neurotrophic signaling and promoting neuronal health in these conditions.
Conclusion:
Pro-NGF human recombinant emerges as a key regulator in neuroregulation and disease pathogenesis, offering promising avenues for therapeutic intervention. Enhancing our understanding of Pro-NGF processing mechanisms and its downstream signaling cascades will provide valuable insights into neurodevelopment, neurodegeneration, and potential therapeutic strategies. Targeting Pro-NGF as a therapeutic intervention may hold immense promise in treating neurological disorders and promoting neuronal health.
What is the molecular weight / Mw of ProNGF Protein?
ProNGF Protein has a total Mw of 25kDa.

What is the source or expression system of ProNGF Protein?
Escherichia Coli.

What is the Purity of ProNGF Protein?
ProNGF Protein is >95% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of ProNGF Protein?
MEPHSESNVPAGHTIPQAHWTKLQHSLDTALRRARSAPAAAIAARVAGQTRNI
TVDPRLFKKRRLRSPRVLFSTQPPREAADTQDLDFEVGGAAPFNRTHRSKRS
SSHPIFHRGEFSVCDSVSVWVGDKTTATDIKGKEVMVLGEVNINNSVFKQYFFET
KCRDPNPVDSGCRGIDSKHWNSYCTTTHTFVKALTMDGKQAAWRFIRIDTAC
VCVLSRKAVRRA

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

What is the endotoxin level for ProNGF Protein?
The endotoxin level is minimal, ProNGF 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:

Ephrin- B3 Human Recombinant

Ephrin-B3, EPH-related receptor transmembrane ligand ELK-L3, EPH-related receptor tyrosine kinase ligand 8, LERK-8, EFNB3, EPLG8, LERK8, EFL6.

Product # :

PRO-1169

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Description

EFNB3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 224 amino acids (28-226 a.a) and having a molecular mass of 24.6kDa.EFNB3 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

EFNB3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2M urea.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Ephrin-B3 (EFNB3) which belongs to the ephrin gene family is essential in brain development as well as in its maintenance. EFNB3 binds to, and induces the collapse of, commissural axons/growth cones in vitro. EFNB3 loosely binds Eph receptors located on bordering cells, leading to contact-dependent bidirectional signaling into neighboring cells. The EPH and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and are implicated in mediating developmental events, mostly in the nervous system.
Synonyms
Ephrin-B3, EPH-related receptor transmembrane ligand ELK-L3, EPH-related receptor tyrosine kinase ligand 8, LERK-8, EFNB3, EPLG8, LERK8, EFL6.
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 MGSHMLSLEP VYWNSANKRF QAEGGYVLYP QIGDRLDLLC PRARPPGPHS SPNYEFYKLY LVGGAQGRRC EAPPAPNLLL TCDRPDLDLR FTIKFQEYSP NLWGHEFRSH HDYYIIATSD GTREGLESLQ GGVCLTRGMK VLLRVGQSPR GGAVPRKPVS EMPMERDRGA AHSLEPGKEN LPGDPTSNAT SRGAEGPLPP PSMP.

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:

Fibroblast Growth Factor-23 Human Recombinant, His Tag

Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.

Product # :

CYT-374

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Fibroblast Growth Factor-23 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain expressed with a -6xHis tag containing a total of 257 amino acids (251 a.a. FGF23+ 6 a.a. His tag) and having a molecular mass of 28629.5 Dalton. The FGF-23 is and purified by chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein (0.5mg/ml) was lyophilized from 25mM Tris pH7.5 and 0.6M NaCl solution.

Purity

Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Treatment with hrFGF23 has been shown to induce FGFR mediated Erk phosphorylation, reduce plasma PTH levels in rats and to reduce blood phosphate levels.

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Introduction
FGF-23 is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities and are involved in a variety of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF-23 inhibits renal tubular phosphate transport. This gene was identified by its mutations associated with autosomal dominant hypophosphatemic rickets (ADHR), an inherited phosphate wasting disorder. Abnormally high level expression of FGF23 was found in oncogenic hypophosphatemic osteomalacia (OHO), a phenotypically similar disease caused by abnormal phosphate metabolism. Mutations FGF23 have also been shown to cause familial tumoral calcinosis with hyperphosphatemia.
Synonyms
Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.
Physical Appearance
Sterile Filtered white lyophilized powder.
Stability
Lyophilized Fibroblast Growth Factor 23 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-23 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 Fibroblast Growth Factor-23 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MLGARLRLWVCALCSVCSMSVLRAYPNASPLLGSSWGGLIHLYTATARN
SYHLQIHKNGHVDGAPHQTIYSALMIRSEDAGFVVITGVMSRRYLCMDFR
GNIFGSHYFDPENCRFQHQTLENGYDVYHSPQYHFLVSLGRAKRAFLPG
MNPPPYSQFLSRRNEIPLIHFNTPIPRRHTRSAEDDSERDPLNVLKPRAR
MTPAPASCSQELPSAEDNSPMASDPLGVVRGGRVNTHAGGTGPEGCRP
FAKFIHHHHHH.
Background
What is the molecular weight/Mw of FGF23 HUMAN, HIS Protein?
FGF23 HUMAN, HIS Protein has a total Mw of 28.6kDa.

What is the source or expression system of FGF23 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of FGF23 HUMAN, HIS Protein?
FGF23 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF23 HUMAN, HIS Protein?
Treatment with hrFGF23 has been shown to induce FGFR mediated Erk phosphorylation, reduce plasma PTH levels in rats and to reduce blood phosphate levels.

What is the amino acid sequence of FGF23 HUMAN, HIS Protein?
MLGARLRLWVCALCSVCSMSVLRAYPNASPLLGSSWGGLIHLYTATARN
SYHLQIHKNGHVDGAPHQTIYSALMIRSEDAGFVVITGVMSRRYLCMDFR
GNIFGSHYFDPENCRFQHQTLENGYDVYHSPQYHFLVSLGRAKRAFLPG
MNPPPYSQFLSRRNEIPLIHFNTPIPRRHTRSAEDDSERDPLNVLKPRAR
MTPAPASCSQELPSAEDNSPMASDPLGVVRGGRVNTHAGGTGPEGCRP
FAKFIHHHHHH.

What applications can FGF23 HUMAN, HIS Protein be used in?
FGF23 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF23 HUMAN, HIS Protein?
The endotoxin level is minimal, FGF23 HUMAN, HIS 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:

Transforming Growth Factor-Beta 2 Rat Recombinant

Transforming growth factor beta-2, TGF-beta-2, G-TSF, Tgfb-2, TGFbeta2.

Product # :

CYT-1267

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Description

Transforming Growth Factor-Beta 2 Rat Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.4kDa.
TGFB2 Rat Recombinant is purified by proprietary chromatographic techniques.

Source

CHO Cells.

Formulation

The protein was lyophilized with 0.1% (v/v) TFA and 35% (v/v) Acetonitrile.

Purity

Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.

Biological Activity

The biological activity was determined by TGFB2 ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells. The expected ED50 for this effect is <0.05ng/ml, corresponding to a specific activity of ≥ 2.0 × 107 units/mg.

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Synonyms
Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGFB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Transforming Growth Factor-Beta 2 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 Transforming Growth Factor-Beta 2 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHTK VLSLYNTINP EASASPCCVS QDLEPLTILY YIGNTPKIEQ LSNMIVKSCK CS.
Background
Rat TGFB22 signals through TGFBR2, TGFBR1 using an accessory co-receptor TGFBR3 (betaglycan) that enhances presentation of TGFβ2
Rat TGFB2 is a potent inducer of epithelial–mesenchymal transition (EMT) therefore is used in Cancer metastasis, Fibrosis, Retinal disorders, Developmental biology and Wound healing

What is the source or expression system of Rat TGFB2 Protein?
CHO Cells

What is the Purity of Rat TGFB2 Protein?
Rat TGFB2 Protein is >97% pure as determined by SDS-PAGE.

What is the molecular weight / Mw of Rat TGFB2 Protein?
Rat TGFB2 Protein having a total Mw of 25.6kDa.

What is the Biological Activity of Rat TGFB2 Protein?
The biological functionality of Rat TGFB2 Protein is determined by mouse HT-2 cells.

What is the endotoxin level for Rat TGFB2 Protein?
The endotoxin level is minimal, Rat TGFB2 Protein was purified using conventional chromatography techniques.

What is the amino acid sequence of Rat TGF beta 2 Protein?
If there is sequence put it instead of the sentence

Is TGFB2 a homodimer / homodimeric protein?
Yes, TGFB1 is homo dimer consisting of 2 identical chains.

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:

Platelet Derived Growth Factor-BB Human Recombinant, Yeast

Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.

Product # :

CYT-242

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Description

Platelet-Derived Growth Factor BB Human Recombinant is a glycosylated homodimer produced in Saccharomyces cerevisiae, containing 2x109 amino acids and having a molecular mass of 32kDa. PDGF-BB is purified by proprietary chromatographic techniques.

Source

Saccharomyces cerevisiae.

Formulation

The PDGF-BB was lyophilized from 0.2 µm filtered solution in 20mM sodium phosphate in absence of any carrier protein.

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as measured by its ability to stimulate proliferation of mouse 3T3 fibroblasts is typically 1 ng/ml, corresponding to a Specific Activity of 1,000,000IU/mg.

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Introduction
PDGF-BB is a member of the platelet-derived growth factor family. The four members of this family are mitogenic factors for cells of mesenchymal origin and are characterized by a motif of eight cysteines. This gene product can exist either as a homodimer (PDGF-BB) or as a heterodimer with the platelet-derived growth factor alpha polypeptide (PDGF-AB), where the dimers are connected by disulfide bonds. Mutations in this gene are associated with meningioma. Reciprocal translocations between chromosomes 22 and 7, at sites where this gene and that for COL1A1 are located, are associated with a particular type of skin tumor called dermatofibrosarcoma protuberans resulting from unregulated expression of growth factor. Two splice variants have been identified for this gene.
Synonyms
Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Platelet-derived Growth Factor BB although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF BB 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 Platelet-derived Growth Factor-BB in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Leu-Gly-Ser-Leu.

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:

Vascular Endothelial Growth Factor Receptor-2 Fc Chimera Human Recombinant

KDR D1-7, sKDR D1-7, Kinase insert domain receptor, Protein-tyrosine kinase receptor Flk-1, CD309, type III receptor tyrosine kinase, FLK1, VEGFR-2.

Product # :

PKA-243

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Description

Soluble VEGFR2 Fc Human Recombinant fused with the Fc part of human IgG1 produced in baculovirus is a disulfide-linked homodimeric, glycosylated, polypeptide containing 968 amino acids and having a molecular mass of 145 kDa. The soluble receptor protein contains only the first 7 extracellular domains, which contain all the information necessary for ligand binding.The sKDR Fc Chimera is purified by proprietary chromatographic techniques.

Source

Insect Cells.

Formulation

KDR fusion protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS pH-7.2.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The activity of sVEGFR2/Fc was determined by its ability to inhibit the VEGF-dependent proliferation of human umbilical vein endothelial cells.

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Introduction
Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation.
Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occuring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.
Synonyms
KDR D1-7, sKDR D1-7, Kinase insert domain receptor, Protein-tyrosine kinase receptor Flk-1, CD309, type III receptor tyrosine kinase, FLK1, VEGFR-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized VEGFR-2 Fc/Chimera protein although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FLK1 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 VEGFR2 in sterile water not less than 50 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ASVGLPSVSL DLPRLSIQKD ILTIKANTTL QITCRGQRDL DWLWPNNQSG SEQRVEVTEC SDGLFCKTLT IPKVIGNDTG AYKCFYRETD LASVIYVYVQ DYRSPFIASV SDQHGVVYIT ENKNKTVVIP CLGSISNLNV SLCARYPEKR FVPDGNRISW DSKKGFTIPS YMISYAGMVF CEAKINDESY QSIMYIVVVV GYRIYDVVLS PSHGIELSVG EKLVLNCTAR TELNVGIDFN WEYPSSKHQH KKLVNRDLKT QSGSEMKKFL STLTIDGVTR SDQGLYTCAA SSGLMTKKNS TFVRVHEKPF VAFGSGMESL VEATVGERVR IPAKYLGYPP PEIKWYKNGI PLESNHTIKA GHVLTIMEVS ERDTGNYTVI LTNPISKEKQ SHVVSLVVYV PPQIGEKSLI SPVDSYQYGT TQTLTCTVYA IPPPHHIHWY WQLEEECANE PSQAVSVTNP YPCEEWRSVE DFQGGNKIEV NKNQFALIEG KNKTVSTLVI QAANVSALYK CEAVNKVGRG ERVISFHVTR GPEITLQPDM QPTEQESVSL WCTADRSTFE NLTWYKLGPQ PLPIHVGELP TPVCKNLDTL WKLNATMFSN STNDILIMEL KNASLQDQGD YVCLAQDRKT KKRHCVVRQL TVLERVAPTI TGNLENQTTS IGESIEVSCT ASGNPPPQIM WFKDNETLVE DSGIVLKDGN RNLTIRRVRK EDEGLYTCQA CSVLGCAKVE AFFIIEGANA SDKTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSREEMT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPMLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGK.

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:

Fibroblast Growth Factor-21 Human Recombinant

Fibroblast growth factor 21, FGF-21.

Product # :

CYT-474

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Description

Fibroblast Growth Factor -21 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 181 amino acids, having a molecular weight of 19.4 kDa. The FGF-21 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from PBS, pH 7.4.

Purity

Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by thymidine uptake assay using FGF-receptors transfected BaF3 cells is less than 0.5 μg/ml, corresponding to a specific activity of > 2.0 × 10³ IU/mg in the presence of 5µg/ml of rMuKlotho-β and 10µg/ml of heparin.

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Introduction
The FGFs are a family of more than 20 small (~17–26 kDa) secreted peptides. The initial characterization of these proteins focused on their ability to stimulate fibroblast proliferation. This mitogenic activity was mediated through FGF receptors (FGFRs) 1, 2, or 3. A fourth closely related tyrosine kinase receptor (FGFR4) was able to bind the FGFs but did not lead to a mitogenic response.
FGFs modulate cellular activity via at least 5 distinct subfamilies of high-affinity FGF receptors (FGFRs): FGFR-1, -2, -3, and -4, all with intrinsic tyrosine kinase activity and, except for FGFR-4, multiple splice isoforms, and FGFR-5, which lacks an intracellular kinase domain. There is growing evidence that FGFRs can be important for regulation of glucose and lipid homeostasis. The overexpression of a dominant negative form of FGFR-1 in cells leads to diabetes in mice, which thus implies that proper FGF signaling is required for normal cell function and glycemia maintenance. FGFR-2 appears to be a key molecule during pancreatic development. Moreover, FGFR-4 has been implicated in cholesterol metabolism and bile acid synthesis.
FGF-19, has been shown to cause resistance to diet-induced obesity and desensitization and to improve glucose and lipid profiles in diabetic rodents. Since these effects, at least in part, are mediated through the observed changes in metabolic rates, FGF-19 can be considered as a regulator of energy expenditure.
FGF-21 is preferentially expressed in liver, but an exact knowledge of FGF-21 bioactivity and its mode of action have been lacking to date. FGF-21 is a potent activator of glucose uptake on adipocytes, protects animals from diet-induced obesity when overexpressed in transgenic mice, and lowers blood glucose and triglyceride levels when therapeutically administered to diabetic rodents.
Synonyms
Fibroblast growth factor 21, FGF-21.
Physical Appearance
Sterile Filtered white lyophilized powder.
Stability
Lyophilized FGF-21 Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor 21 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 Fibroblast Growth Factor-21 Human Recombinant sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HPIPDS SPLLQFGGQV RQRYLYTDDA QQTEAHLEIR EDGTVGGAAD QSPESLLQLK ALKPGVIQIL GVKTSRFLCQ RPDGALYGSL HFDPEACSFR ELLLEDGYNV YQSEAHGLPL HLPGNKSPHR DPAPRGPARF LPLPGLPPAP PEPPGILAPQ PPDVGSSDPL SMVGPSQGRS PSYAS.
Background
What is the molecular weight/Mw of FGF21 Protein?
FGF21 Protein has a total Mw of 19.4kDa.

What is the source or expression system of FGF21 Protein?
Escherichia Coli.

What is the Purity of FGF21 Protein?
FGF21 Protein is >96% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF21 Protein?
The ED50 as determined by thymidine uptake assay using FGF-receptors transfected BaF3 cells is less than 0.5 μg/ml, corresponding to a specific activity of > 2.0 × 103 IU/mg in the presence of 5µg/ml of rMuKlotho-β and 10µg/ml of heparin.

What is the amino acid sequence of FGF21 Protein?
HPIPDS SPLLQFGGQV RQRYLYTDDA QQTEAHLEIR EDGTVGGAAD QSPESLLQLK ALKPGVIQIL GVKTSRFLCQ RPDGALYGSL HFDPEACSFR ELLLEDGYNV YQSEAHGLPL HLPGNKSPHR DPAPRGPARF LPLPGLPPAP PEPPGILAPQ PPDVGSSDPL SMVGPSQGRS PSYAS.

What applications can FGF21 Protein be used in?
FGF21 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF21 Protein?
The endotoxin level is minimal, FGF21 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:

Nerve Growth Factor Receptor Human Recombinant

Tumor necrosis factor receptor superfamily member 16, Gp80-LNGFR, Low affinity neurotrophin receptor p75NTR, Low-affinity nerve growth factor receptor, NGF receptor, p75 ICD, CD271.

Product # :

CYT-915

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Description

NGFR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 230 amino acids (29-250 a.a.) and having a molecular mass of 24.6kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). NGFR is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

NGFR protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Tumor necrosis factor receptor superfamily member 16 (NGFR) BELONGS TO the tumor necrosis factor receptor superfamily with an extensive pattern of expression in tissues such as the brain, liver, lung, and muscle. NGFR has a role in the regulation of the translocation of GLUT4 to the cell surface in adipocytes and skeletal muscle cells in response to insulin, possibly by regulating RAB31 activity, and thus contributes to the regulation of insulin-dependent glucose uptake. NGFRs are low affinity receptors which can bind to NGF, BDNF, NT-3, and NT-4. NGFR mediates cell survival as well as cell death of neural cells.
Synonyms
Tumor necrosis factor receptor superfamily member 16, Gp80-LNGFR, Low affinity neurotrophin receptor p75NTR, Low-affinity nerve growth factor receptor, NGF receptor, p75 ICD, CD271.
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
KEACPTGLYT HSGECCKACN LGEGVAQPCG ANQTVCEPCL DSVTFSDVVS ATEPCKPCTE CVGLQSMSAP CVEADDAVCR CAYGYYQDET TGRCEACRVC EAGSGLVFSC QDKQNTVCEE CPDGTYSDEA NHVDPCLPCT VCEDTERQLR ECTRWADAEC EEIPGRWITR STPPEGSDST APSTQEPEAP PEQDLIASTV AGVVTTVMGS SQPVVTRGTT DNLEHHHHHH.

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:

Connective Tissue Growth Factor Human Recombinant, His Tag

CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.

Product # :

CYT-438

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Description

CTGF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (27-349) and having a molecular mass of 37.7kDa.The CTGF is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CTGF protein (1mg/ml) is supplied in 20mM Tris-HCl, pH-8 and 10% Glycerol.

Purity

Greater than 85.0% as determined by Analysis by SDS-PAGE.

sds-page

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Introduction
Connective Tissue Growth Factor belongs to the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 (Cystein rich 61), CTGF (Connective Tissue Growth Factor), Nov (Nephroblastoma Overexpressed gene), WISP-1, 2 and 3 (Wnt-1 Induced Secreted Proteins). The CCN genes encode secreted proteins associated with the Extracellular Matrix (ECM) and cell membrane. CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: fibrosis, vascular ailments and tumorigenesis.
Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes. The full length protein consists of four modulesModule I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins (IGFBPs).
Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat (VWC).
Module III contains sequences sharing identity with the Thrombospondin type 1 repeat (TSP1) (WSXCSXXCG), which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion. Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand's factor and mucins. Sequence similarities to heparin-binding motifs are also found within this domain.
Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy. In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells. CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.
Synonyms
CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth 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).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQNCSGPCRC PDEPAPRCPA GVSLVLDGCG CCRVCAKQLG ELCTERDPCD PHKGLFCDFG SPANRKIGVC TAKDGAPCIF GGTVYRSGES FQSSCKYQCT CLDGAVGCMP LCSMDVRLPS PDCPFPRRVK LPGKCCEEWV CDEPKDQTVV GPALAAYRLE DTFGPDPTMI RANCLVQTTE WSACSKTCGM GISTRVTNDN ASCRLEKQSR LCMVRPCEAD LEENIKKGKK CIRTPKISKP IKFELSGCTS MKTYRAKFCG VCTDGRCCTP HRTTTLPVEF KCPDGEVMKK NMMFIKTCAC HYNCPGDNDI FESLYYRKMY GDMA.
Background
What is the molecular weight/Mw of CTGF Protein?
CTGF Protein has a total Mw of 37.7kDa.

What is the source or expression system of CTGF Protein?
Escherichia Coli.

What is the Purity of CTGF Protein?
CTGF Protein is >85% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of CTGF Protein?
MGSSHHHHHH SSGLVPRGSH MQNCSGPCRC PDEPAPRCPA GVSLVLDGCG CCRVCAKQLG ELCTERDPCD PHKGLFCDFG SPANRKIGVC TAKDGAPCIF GGTVYRSGES FQSSCKYQCT CLDGAVGCMP LCSMDVRLPS PDCPFPRRVK LPGKCCEEWV CDEPKDQTVV GPALAAYRLE DTFGPDPTMI RANCLVQTTE WSACSKTCGM GISTRVTNDN ASCRLEKQSR LCMVRPCEAD LEENIKKGKK CIRTPKISKP IKFELSGCTS MKTYRAKFCG VCTDGRCCTP HRTTTLPVEF KCPDGEVMKK NMMFIKTCAC HYNCPGDNDI FESLYYRKMY GDMA.

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

What is the endotoxin level for CTGF Protein?
The endotoxin level is minimal, CTGF 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:

Fibroblast Growth Factor-Basic Bovine Recombinant

HBGH-2, HBGF-2, Prostatropin, FGF-2, FGB-b.

Product # :

CYT-288

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Quantity :

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Description

FGF-2 Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of 17250 Dalton. The Fibroblast Growth Factor 2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The FGF-b Bovine was lyophilized from a concentrated (1mg/ml) sterile solution containing 1% HSA.

Purity

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

Biological Activity

The ED₅₀, measured in a mitogenic assay using quiescent NR6R-3T3 fibroblasts was found to be <0.1ng/ml, corresponding to a specific activity of 3 x 10⁶Units/mg.

More Info

Introduction
FGF-basic is a member of the fibroblast growth factor (FGF) family. FGF family members bind heparin and possess broad mitogenic and angiogenic activities. This protein has been implicated in diverse biological processes, such as limb and nervous system development, wound healing, and tumor growth. The mRNA for this gene contains multiple polyadenylation sites, and is alternatively translated from AUG and non-AUG (CUG) initiation codons resulting in five different isoforms with distinct properties. The CUG-initiated isoforms are localized in the nucleus and are responsible for the intracrine effect, whereas, the AUG-initiated form is mostly cytosolic and is responsible for the paracrine and autocrine effects of this FGF.
The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. there are differences in the tissue distribution and concentration of these 2 growth factors.
Synonyms
HBGH-2, HBGF-2, Prostatropin, FGF-2, FGB-b.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Fibroblast Growth Factor 2 Bovine although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-b Bovine Recombinant 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 Fibroblast Growth Factor-2 Bovine Recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Ala-Gly-Ser.
Background
What is the molecular weight/Mw of FGF-2 BOVINE Protein?
FGF-2 BOVINE Protein has a total Mw of 17.5kDa.

What is the source or expression system of FGF-2 BOVINE Protein?
Escherichia Coli.

What is the Purity of FGF-2 BOVINE Protein?
FGF-2 BOVINE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF-2 BOVINE Protein?
The ED50, measured in a mitogenic assay using quiescent NR6R-3T3 fibroblasts was found to be <0.1ng/ml, corresponding to a specific activity of 3 x 106 Units/mg.

What is the amino acid sequence of FGF-2 BOVINE Protein?
FGF-2 BOVINE Protein is composed from 155 amino acids.

What applications can FGF-2 BOVINE Protein be used in?
FGF-2 BOVINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF-2 BOVINE Protein?
The endotoxin level is minimal, FGF-2 BOVINE Protein was purified using conventional chromatography techniques.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.85 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).2. Analysis by RP-HPLC, using a calibrated solution of FGF-2 Bovine as a Reference Standard.

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:

Elongator Acetyltransferase Complex Subunit 5 Human Recombinant

C17orf81, DERP6, HSPC002, MST071, MSTP071, Dermal papilla-derived protein 6, S-phase 2 protein, ELP5.

Product # :

PRO-1660

Price :

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Shipped with Ice Packs

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Description

ELP5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 339 amino acids (1-316 a.a.) and having a molecular mass of 37.2kDa.ELP5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ELP5 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

Purity

Greater than 80.0% as determined by SDS-PAGE.

More Info

Introduction
Elongator acetyltransferase complex subunit 5 (ELP5) is a member of the ELP5 family. ELP5 functions as subunit of the RNA polymerase II elongator complex, which is a histone acetyltransferase component of the RNA polymerase II (Pol II) holoenzyme and is participated in transcriptional elongation. Elongator plays a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4. ELP5 takes part in cell migration and is widely expressed in in heart, brain, liver, skeletal muscle and testis.
Synonyms
C17orf81, DERP6, HSPC002, MST071, MSTP071, Dermal papilla-derived protein 6, S-phase 2 protein, ELP5.
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 MGSMTPSEGA RAGTGRELEM LDSLLALGGL VLLRDSVEWE GRSLLKALVK KSALCGEQVH ILGCEVSEEE FREGFDSDIN NRLVYHDFFR DPLNWSKTEE AFPGGPLGAL RAMCKRTDPV PVTIALDSLS WLLLRLPCTT LCQVLHAVSH QDSCPGDSSS VGKVSVLGLL HEELHGPGPV GALSSLAQTE VTLGGTMGQA SAHILCRRPR QRPTDQTQWF SILPDFSLDL QEGPSVESQP YSDPHIPPVD PTTHLTFNLH LSKKEREARD SLILPFQFSS EKQQALLRPR PGQATSHIFY EPDAYDDLDQ EDPDDDLDI.

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:

Fibroblast Growth Factor-22 Human Recombinant

Fibroblast growth factor 22, FGF-22.

Product # :

CYT-428

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Fibroblast Growth Factor-22 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 149 amino acids and having a molecular mass of 17.3 kDa. The FGF-22 is purified by chromatographic techniques.

Source

Escherichia Coli.

Formulation

The sterile protein powder is lyophilized with no additives.

Purity

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

More Info

Introduction
FGF22 is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities and are involved in a variety of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. The mouse homolog of this gene was found to be preferentially expressed in the inner root sheath of the hair follicle, which suggested a role in hair development.
Synonyms
Fibroblast growth factor 22, FGF-22.
Physical Appearance
Sterile Filtered white lyophilized powder.
Stability
Lyophilized Fibroblast Growth Factor 22 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-22 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 Fibroblast Growth Factor-22 sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MTPSASRGPR SYPHLEGDVR WRRLFSSTHF FLRVDPGGRV QGTRWRHGQD SILEIRSVHV GVVVIKAVSS GFYVAMNRRG RLYGSRLYTV DCRFRERIEE NGHNTYASQR WRRRGQPMFL ALDRRGGPRP GGRTRRYHLS AHFLPVLVS.
Background
What is the molecular weight/Mw of FGF22 HUMAN Protein?
FGF22 HUMAN Protein has a total Mw of 17.3kDa.

What is the source or expression system of FGF22 HUMAN Protein?
Escherichia Coli.

What is the Purity of FGF22 HUMAN Protein?
FGF22 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF22 HUMAN Protein?
The biological functionality of FGF22 HUMAN Protein will be determined in the future.

What is the amino acid sequence of FGF22 HUMAN Protein?
MTPSASRGPR SYPHLEGDVR WRRLFSSTHF FLRVDPGGRV QGTRWRHGQD SILEIRSVHV GVVVIKAVSS GFYVAMNRRG RLYGSRLYTV DCRFRERIEE NGHNTYASQR WRRRGQPMFL ALDRRGGPRP GGRTRRYHLS AHFLPVLVS.

What applications can FGF22 HUMAN Protein be used in?
FGF22 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF22 HUMAN Protein?
The endotoxin level is minimal, FGF22 HUMAN 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:

FGFR1 Oncogene Partner Human Recombinant

FGFR1 oncogene partner, FGFR1OP, FOP.

Product # :

PKA-031

Price :

Quantity :

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Shipped with Ice Packs

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Description

FGFR1OP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 403 amino acids (1-379 a.a) and having a molecular mass of 43.5kDa.FGFR1OP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FGFR1OP protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 1mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

More Info

Introduction
FGFR1 oncogene partner (FGFR1OP) is a member of the FGFR1OP family. The FGFR1OP protein is an essentially hydrophilic protein proposed to be a leucine-rich protein family member. A t(6;8)(q27;p11) chromosomal translocation, fusing the FGFR1OP gene and the FGFR1 gene, is seen in cases of myeloproliferative disorder. The ensuing chimeric protein contains the N-terminal leucine-rich region of the FGFR1OP protein fused to the catalytic domain of FGFR1. The FGFR1OP gene is believed to play a significant role in normal proliferation and differentiation of the erythroid lineage.
Synonyms
FGFR1 oncogene partner, FGFR1OP, FOP.
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 MGSHMAATAA AVVAEEDTEL RDLLVQTLEN SGVLNRIKAE LRAAVFLALE EQEKVENKTP LVNESLKKFL NTKDGRLVAS LVAEFLQFFN LDFTLAVFQP ETSTLQGLEG RENLARDLGI IEAEGTVGGP LLLEVIRRCQ QKEKGPTTGE GALDLSDVHS PPKSPEGKTS AQTTPSKKAN DEANQSDTSV SLSEPKSKSS LHLLSHETKI GSFLSNRTLD GKDKAGLCPD EDDMEGDSFF DDPIPKPEKT YGLRKEPRKQ AGSLASLSDA PPLKSGLSSL AGAPSLKDSE SKRGNTVLKD LKLISDKIGS LGLGTGEDDD YVDDFNSTSH RSEKSEISIG EEIEEDLSVE IDDINTSDKL DDLTQDLTVS QLSDVADYLE DVA.

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:

Fibroblast Growth Factor-21 Bovine Recombinant

Fibroblast growth factor 21, FGF-21, FGF21.

Product # :

CYT-657

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Fibroblast Growth Factor -21 Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 182 amino acids, having a molecular weight of 19.5 kDa.The FGF-21 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (0.8 mg/ml) solution with 0.4 mg/ml of NaHCO3, pH 8.

Purity

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

More Info

Introduction
The FGFs are a family of more than 20 small (~17–26 kDa) secreted peptides. The initial characterization of these proteins focused on their ability to stimulate fibroblast proliferation. This mitogenic activity was mediated through FGF receptors (FGFRs) 1, 2, or 3. A fourth closely related tyrosine kinase receptor (FGFR4) was able to bind the FGFs but did not lead to a mitogenic response.
FGFs modulate cellular activity via at least 5 distinct subfamilies of high-affinity FGF receptors (FGFRs): FGFR-1, -2, -3, and -4, all with intrinsic tyrosine kinase activity and, except for FGFR-4, multiple splice isoforms, and FGFR-5, which lacks an intracellular kinase domain. There is growing evidence that FGFRs can be important for regulation of glucose and lipid homeostasis. The overexpression of a dominant negative form of FGFR-1 in ? cells leads to diabetes in mice, which thus implies that proper FGF signaling is required for normal ? cell function and glycemia maintenance. FGFR-2 appears to be a key molecule during pancreatic development. Moreover, FGFR-4 has been implicated in cholesterol metabolism and bile acid synthesis.
FGF-19, has been shown to cause resistance to diet-induced obesity and desensitization and to improve, glucose, and lipid profiles in diabetic rodents. Since these effects, at least in part, are mediated through the observed changes in metabolic rates, FGF-19 can be considered as a regulator of energy expenditure.
FGF-21 is preferentially expressed in liver, but an exact knowledge of FGF-21 bioactivity and its mode of action have been lacking to date. FGF-21 is a potent activator of glucose uptake on adipocytes, protects animals from diet-induced obesity when overexpressed in transgenic mice, and lowers blood glucose and triglyceride levels when therapeutically administered to diabetic rodents.
Synonyms
Fibroblast growth factor 21, FGF-21, FGF21.
Physical Appearance
Sterile Filtered white lyophilized powder.
Stability
Lyophilized FGF-21 Bovine Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor 21 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 Bovine FGF-21 in sterile water or 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in presence of carrier protein.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-His-Pro-Ile-Pro.
Background
What is the molecular weight/Mw of FGF 21 BOVINE Protein?
FGF 21 BOVINE Protein has a total Mw of 19.5kDa.

What is the source or expression system of FGF 21 BOVINE Protein?
Escherichia Coli.

What is the Purity of FGF 21 BOVINE Protein?
FGF 21 BOVINE Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF 21 BOVINE Protein?
The biological functionality of FGF 21 BOVINE Protein will be determined in the future.

What is the amino acid sequence of FGF 21 BOVINE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-His-Pro-Ile-Pro.

What applications can FGF 21 BOVINE Protein be used in?
FGF 21 BOVINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF 21 BOVINE Protein?
The endotoxin level is minimal, FGF 21 BOVINE Protein was purified using conventional chromatography techniques.
Protein content
Bovine FGF-21 quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.47 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of FGF-21 Recombinant as a Reference Standard.

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:

Beta Nerve Growth Factor Human Recombinant

Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

Product # :

CYT-579

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Nerve Growth Factor-beta Human Recombinant produced in E.Coli is a non-covalently disulfide-linked homodimer, non-glycosylated, polypeptide chain containing 2 identical 121 amino acids with a molecular weight of two 13.6 kDa polypeptide monomers.The NGF-b is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The beta-NGF protein was lyophilized from a 0.2µm filtered solution containing 0.1% Trifluoroacetic Acid (TFA).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, calculated by its ability to stimulate proliferation of TF-1 cells and is typically 1.31 ng/ml, corresponding to a specific activity of 7.6x10⁵units/mg.

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Introduction
NGF-beta has nerve growth stimulating activity and the complex is involved in the regulation of growth and the differentiation of sympathetic and certain sensory neurons. Mutations in this gene have been associated with hereditary sensory and autonomic neuropathy, type 5 (HSAN5), and dysregulation of this gene's expression is associated with allergic rhinitis.
Synonyms
Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Beta-NGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NGF-Beta 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 NGF-b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSSSHPIFHRG EFSVCDSVSV WVGDKTTATD IKGKEVMVLG EVNINNSVFK QYFFETKCRD PNPVDSGCRG IDSKHWNSYC TTTHTFVKAL TMDGKQAAWR FIRIDTACVC VLSRKAVRRA.
Background
What is the molecular weight/Mw of B NGF Protein?
B NGF Protein has a total Mw of 13.6kDa.

What is the source or expression system of B NGF Protein?
Escherichia Coli.

What is the Purity of B NGF Protein?
B NGF Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of B NGF Protein?
The ED50, calculated by its ability to stimulate proliferation of TF-1 cells and is typically 1.31 ng/ml, corresponding to a specific activity of 7.6x105units/mg.

What is the amino acid sequence of B NGF Protein?
MSSSHPIFHRG EFSVCDSVSV WVGDKTTATD IKGKEVMVLG EVNINNSVFK QYFFETKCRD PNPVDSGCRG IDSKHWNSYC TTTHTFVKAL TMDGKQAAWR FIRIDTACVC VLSRKAVRRA.

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

What is the endotoxin level for B NGF Protein?
The endotoxin level is minimal, B NGF 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:

Hepatocyte Growth Factor Human Recombinant, HEK

Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF.

Product # :

CYT-090

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

HGF Human Recombinant produced in HEK cells is a glycosylated disulfide-linked heterodimer, containing 697 a.a. (Gln-32 to Ser-728) having a total molecular weight of 80kDa. The HGF is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

The HGF was lyophilized from a solution (1mg/ml) containing 10mM Sodium phosphate, 150mM NaCl, 0.01% Tween 80 and 100mM L-Arginine, pH 6.5.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The activity was measured in a cell proliferation assay using 4MBr-5 rhesus monkey epithelial cells (ATCC CCL-208). The EC₅₀for this effect is typically 20-40ng/ml.

More Info

Introduction
Hepatocyte Growth Factor (HGF) is a multifunctional growth factor which regulates both cell growth and cell motility. It exerts a strong mitogenic effect on hepatocytes and primary epithelial cells. HGF synergizes with Interleukin-3 and GM-CSF to stimulate colony formation of hematopoietic progenitor cells in vitro and may, therefore, also modulate hematopoiesis.
Synonyms
Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized HGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HGF 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 Hepatocyte Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
32-QRKRRNTIHE FKKSAKTTLI KIDPALKIKT KKVNTADQCA NRCTRNKGLP FTCKAFVFDK ARKQCLWFPF NSMSSGVKKE FGHEFDLYEN KDYIRNCIIG KGRSYKGTVS ITKSGIKCQP WSSMIPHEHS FLPSSYRGKD LQENYCRNPR GEEGGPWCFT SNPEVRYEVC DIPQCSEVEC MTCNGESYRG LMDHTESGKI CQRWDHQTPH RHKFLPERYP DKGFDDNYCR NPDGQPRPWC YTLDPHTRWE YCAIKTCADN TMNDTDVPLE TTECIQGQGE GYRGTVNTIW NGIPCQRWDS QYPHEHDMTP ENFKCKDLRE NYCRNPDGSE SPWCFTTDPN IRVGYCSQIP NCDMSHGQDC YRGNGKNYMG NLSQTRSGLT CSMWDKNMED LHRHIFWEPD ASKLNENYCR NPDDDAHGPW CYTGNPLIPW DYCPISRCEG DTTPTIVNLD HPVISCAKTK QLRVVNGIPT RTNIGWMVSL RYRNKHICGG SLIKESWVLT ARQCFPSRDL KDYEAWLGIH DVHGRGDEKC KQVLNVSQLV YGPEGSDLVL MKLARPAVLD DFVSTIDLPN YGCTIPEKTS CSVYGWGYTG LINYDGLLRV AHLYIMGNEK CSQHHRGKVT LNESEICAGA EKIGSGPCEG DYGGPLVCEQ HKMRMVLGVI VPGRGCAIPN RPGIFVRVAY YAKWIHKIIL TYKVPQS-728
Background
What is the molecular weight/Mw of HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein has a total Mw of 80kDa.

What is the source or expression system of HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
HEK.
What is the Purity of HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
The activity was measured in a cell proliferation assay using 4MBr-5 rhesus monkey epithelial cells (ATCC CCL-208). The EC50 for this effect is typically 20-40ng/ml.
What is the amino acid sequence of HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
32-QRKRRNTIHE FKKSAKTTLI KIDPALKIKT KKVNTADQCA NRCTRNKGLP FTCKAFVFDK ARKQCLWFPF NSMSSGVKKE FGHEFDLYEN KDYIRNCIIG KGRSYKGTVS ITKSGIKCQP WSSMIPHEHS FLPSSYRGKD LQENYCRNPR GEEGGPWCFT SNPEVRYEVC DIPQCSEVEC MTCNGESYRG LMDHTESGKI CQRWDHQTPH RHKFLPERYP DKGFDDNYCR NPDGQPRPWC YTLDPHTRWE YCAIKTCADN TMNDTDVPLE TTECIQGQGE GYRGTVNTIW NGIPCQRWDS QYPHEHDMTP ENFKCKDLRE NYCRNPDGSE SPWCFTTDPN IRVGYCSQIP NCDMSHGQDC YRGNGKNYMG NLSQTRSGLT CSMWDKNMED LHRHIFWEPD ASKLNENYCR NPDDDAHGPW CYTGNPLIPW DYCPISRCEG DTTPTIVNLD HPVISCAKTK QLRVVNGIPT RTNIGWMVSL RYRNKHICGG SLIKESWVLT ARQCFPSRDL KDYEAWLGIH DVHGRGDEKC KQVLNVSQLV YGPEGSDLVL MKLARPAVLD DFVSTIDLPN YGCTIPEKTS CSVYGWGYTG LINYDGLLRV AHLYIMGNEK CSQHHRGKVT LNESEICAGA EKIGSGPCEG DYGGPLVCEQ HKMRMVLGVI VPGRGCAIPN RPGIFVRVAY YAKWIHKIIL TYKVPQS-728

What applications can HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein be used in?
HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for HEPATOCYTE GROWTH FACTOR HUMAN,HEK Protein?
The endotoxin level is minimal, HEPATOCYTE GROWTH FACTOR HUMAN,HEK 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:

EPH Receptor A3 Mouse Recombinant

Cek4, EK4, End3, ETK1, Hek, Hek4, Mek4, Tyro4, ephrin type-A receptor 3, ephrin type-A receptor 3 isoform1, receptor protein-tyrosine kinase, EPH-like kinase 4, tyrosine-protein kinase TYRO4, tyrosine-protein kinase receptor ETK1, Eph receptor A3, AW492086.

Product # :

PRO-2817

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Description

EPHA3 Mouse Recombinant produced in HEK293 cells is a single, polypeptide chain containing 527 amino acids (21-541 a.a.) and having a molecular mass of 59.5kDa. EPHA3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

EPHA3 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

Measured by its binding ability in a functional ELISA with cat#pro-2816.

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Synonyms
Cek4, EK4, End3, ETK1, Hek, Hek4, Mek4, Tyro4, ephrin type-A receptor 3, ephrin type-A receptor 3 isoform1, receptor protein-tyrosine kinase, EPH-like kinase 4, tyrosine-protein kinase TYRO4, tyrosine-protein kinase receptor ETK1, Eph receptor A3, AW492086.
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
ELSPQPSNEV NLLDSKTIQG ELGWISYPSH GWEEISGVDE HYTPIRTYQV CNVMDHSQNN WLRTNWVPRN SAQKIYVELK FTLRDCNSIP LVLGTCKETF NLYYMESDDD HGVKFREHQF TKIDTIAADE SFTQMDLGDR ILKLNTEIRE VGPVNKKGFY LAFQDVGACV ALVSVRVYFK KCPFTVKNLA MFPDTVPMDS QSLVEVRGSC VNNSKEEDPP RMYCSTEGEW LVPIGKCTCN AGYEERGFIC QACRPGFYKA SDGAAKCAKC PPHSSTQEDG SMNCRCENNY FRAEKDPPSM ACTRPPSAPR NVISNINETS VILDWSWPLD TGGRKDITFN IICKKCGWNV RQCEPCSPNV RFLPRQLGLT NTTVTVTDLL AHTNYTFEID AVNGVSELSS PPRQYAAVSI TTNQAAPSPV MTIKKDRTSR NSISLSWQEP EHPNGIILDY EVKYYEKQEQ ETSYTILRAR GTNVTISSLK PDTTYVFQIR ARTAAGYGTN SRKFEFETSP DSFSISGENS HHHHHHH.
Background
Research on EphA3 in mice has highlighted its critical involvement in the development of the nervous system, cardiovascular system, and skeletal system. EphA3 signaling influences axon pathfinding, synaptic plasticity, and the formation of tissue boundaries, ensuring proper tissue and organ development. Dysregulation of EphA3 has been implicated in various pathologies, including cancer, where it contributes to tumor growth, angiogenesis, and metastasis.

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:

Vascular Endothelial Growth Factor receptor-1 Human Recombinant, HEK Active

FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

Product # :

PKA-134

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description
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Description

FLT1 Human Recombinant is a single, glycosylated polypeptide chain containing 535 amino acids (27-328a.a) and having a molecular mass of 60.3kDa (calculated). FLT1 is fused to a 233 amino acid hIgG-Tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293

Formulation

FLT1 protein solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The ED50 range ≤ 60ng/ml and is measured by its ability to inhibit proliferation using HUVEC human umbilical vein endothelial cells in the
presence of Human VEGF165.

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Synonyms
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
Physical Appearance
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.
Amino Acid Sequence
SKLKDPELSL KGTQHIMQAG QTLHLQCRGE AAHKWSLPEM VSKESERLSI TKSACGRNGK QFCSTLTLNT AQANHTGFYS CKYLAVPTSK KKETESAIYI FISDTGRPFV EMYSEIPEII HMTEGRELVI PCRVTSPNIT VTLKKFPLDT LIPDGKRIIW DSRKGFIISN ATYKEIGLLT CEATVNGHLY KTNYLTHRQT NTIIDVQIST PRPVKLLRGH TLVLNCTATT PLNTRVQMTW SYPDEKNKRA SVRRRIDQSN SHANIFYSVL TIDKMQNKDK GLYTCRVRSG PSFKSVNTSV HILEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGK.
Background
VEGFR-1 (Vascular Endothelial Growth Factor Receptor-1), also known as Flt-1 (Fms-like tyrosine kinase 1), is a critical receptor involved in angiogenesis and vascular development. This research paper delves into the structure, function, and therapeutic implications of VEGFR-1, shedding light on its multifaceted role in various physiological and pathological processes.
VEGFR-1 is a transmembrane receptor tyrosine kinase belonging to the VEGF receptor family. It is primarily expressed on endothelial cells and plays a pivotal role in mediating the cellular responses to VEGF ligands. Upon ligand binding, VEGFR-1 initiates intracellular signaling cascades that regulate endothelial cell proliferation, migration, and survival, ultimately contributing to the formation of new blood vessels.
The structure of VEGFR-1 comprises distinct domains, including an extracellular ligand-binding domain, a transmembrane domain, and an intracellular tyrosine kinase domain. The extracellular domain facilitates the interaction between VEGF ligands and the receptor, while the intracellular domain transduces downstream signals by phosphorylating specific tyrosine residues.
VEGFR-1 exhibits not only ligand-dependent but also ligand-independent functions. In addition to its role as a VEGF receptor, it can act as a decoy receptor, sequestering VEGF and modulating the bioavailability of VEGF ligands. This unique property allows VEGFR-1 to regulate VEGF signaling and influence angiogenic processes.
The signaling pathways activated by VEGFR-1 are diverse and intricate, involving multiple downstream effectors, such as PI3K/AKT, MAPK/ERK, and STAT proteins. These pathways regulate endothelial cell behaviors, including proliferation, migration, and differentiation, which are crucial for angiogenesis. Perturbations in VEGFR-1 signaling have been implicated in various pathological conditions, including cancer, retinopathy, and inflammatory disorders.
The therapeutic targeting of VEGFR-1 has gained considerable attention for its potential in managing angiogenesis-related diseases. Inhibitors specifically designed to block VEGFR-1 have been developed to suppress aberrant angiogenesis and impede tumor growth. Moreover, VEGFR-1-based therapies have been explored for ocular diseases like wet age-related macular degeneration (AMD) and diabetic retinopathy, aiming to alleviate pathological neovascularization.
The availability of VEGFR-1 human recombinant proteins has facilitated in-depth research and the development of potential therapeutic interventions. Recombinant VEGFR-1 proteins serve as valuable tools for investigating VEGF-VEGFR-1 interactions, screening drug candidates, and elucidating the underlying molecular mechanisms of VEGFR-1-mediated signaling pathways.

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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