Search: 1000 results found for "Stem Cell Factor"

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:

Transforming Growth Factor-beta 1 Human

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

Product # :

CYT-561

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Description

Human Transforming Growth Factor-beta 1 purified from Human Platelets having a molecular mass of 25kDa.The TGF-b 1 is purified by proprietary chromatographic techniques.

Source

Human Platelets.

Formulation

TGF-Beta1 protein was lyophilized from a solution containing 30% acetonitrile and 0.1% trifluoroacetic acid.

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

Stimulates the growth of NRK-1 cells in soft agar at concentrations ranging from 0.1 to 5ng/ml corresponding to a specific activity of 200,000-10,000,000IU/mg. Effective concentration ranges must be experimentally determined. Purified EGF and/or TGF- must be present for observation of the biological activity.

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Introduction
Transforming growth factor betas (TGF Betas) 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 lyophilized powder.
Stability
Lyophilized TGF-beta 1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGF-beta 1 should be stored at 4°C between 2-7 days and for future use below -18°C.DO NOT RECONSTITE WITH NEUTRAL BUFFERS.DO NOT USE GLASS IMPLEMENTS OR EXTENSIVE MANIPULATIONS.PREVENT FREEZE THAW CYCLES.
Solubility
It is recommended to reconstitute lyophilized TGF-beta 1 in 0.5% BSA in 0.1N acetic acid, which can then be further diluted to the desired aliquot with 30% acetonitrile and 0.1% trifluoroacetic acid.
Background
Title: Transforming Growth Factor-Beta 1 Human: An Insight into its Role in Cellular Regulation
Abstract:

Transforming Growth Factor-Beta 1 (TGF-β1) is a multifunctional cytokine that plays a critical role in various cellular processes, including cell growth, differentiation, apoptosis, and immune regulation. This research paper aims to provide a comprehensive overview of the structure, synthesis, signaling pathways, and biological functions of TGF-β1 in human cells. Additionally, this article highlights the relevance of TGF-β1 in various physiological and pathological conditions, including cancer, fibrosis, and immune disorders. Furthermore, potential therapeutic strategies targeting TGF-β1 signaling are also discussed. The information presented in this paper consolidates the current understanding of TGF-β1 and its significance in cellular regulation.
Introduction:

Transforming Growth Factor-Beta 1 (TGF-β1) belongs to a superfamily of growth factors that regulate various cellular processes. It is synthesized as a precursor protein and undergoes proteolytic cleavage to generate the biologically active form. TGF-β1 exerts its effects by binding to specific cell surface receptors, leading to the activation of downstream signaling cascades. These signaling pathways involve Smad-dependent and Smad-independent mechanisms, which ultimately regulate gene expression and cellular responses.
Biological Functions:

TGF-β1 regulates cell proliferation by exerting both stimulatory and inhibitory effects, depending on the cellular context. It plays a crucial role in tissue development, wound healing, and tissue repair by promoting extracellular matrix synthesis and modulating the immune response. TGF-β1 also has immunomodulatory functions, influencing the differentiation and function of immune cells. However, dysregulation of TGF-β1 signaling is associated with various pathologies, including cancer progression, fibrosis, and autoimmune disorders.
Role in Cancer:

TGF-β1 acts as a tumor suppressor in early stages of cancer by inhibiting cell proliferation and inducing apoptosis. However, in advanced stages, it promotes tumor progression by enhancing tumor cell migration, invasion, and angiogenesis. The dual role of TGF-β1 in cancer highlights its complex involvement in tumorigenesis.
Therapeutic Implications:

Given the significant role of TGF-β1 in various diseases, targeting its signaling pathways has emerged as a potential therapeutic strategy. Several approaches, including small molecule inhibitors, antibodies, and gene therapies, are being explored to modulate TGF-β1 activity in a controlled manner. These interventions hold promise in the treatment of cancer, fibrosis, and other TGF-β1-related disorders.
Conclusion:

Transforming Growth Factor-Beta 1 is a versatile cytokine with diverse functions in cellular regulation. Its role in physiological processes and disease pathogenesis underscores its importance as a therapeutic target. Further investigations into the precise mechanisms and downstream effects of TGF-β1 signaling will contribute to the development of novel therapies for various human disorders.

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:

Tumor Necrosis Factor-Alpha Mouse Recombinant

TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

Product # :

CYT-252

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Description

Tumor Necrosis Factor-a Mouse Recombinant produced in E. coli is a single, non glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17301.32 Dalton. The TNF-alpha is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.

Purity

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

Biological Activity

The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.1ng/ml, corresponding to a Specific Activity of 10,000,000Units/mg.

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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.
Synonyms
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Tumor Necrosis Factor-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-a 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 Tumor Necrosis Factor-alpha in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MLRSSSQNSS DKPVAHVVAN HQVEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLVY SQVLFKGQGC PDYVLLTHTV SRFAISYQEK VNLLSAVKSP CPKDTPEGAE LKPWYEPIYL GGVFQLEKGD QLSAEVNLPK YLDFAESGQV YFGVIAL
Background
Tumor Necrosis Factor-alpha (TNF-α) is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. It is primarily produced by activated macrophages, but can also be secreted by other immune cells, such as T cells, natural killer cells, and mast cells. TNF-α is involved in a wide range of physiological and pathological processes, including the defense against infections, the development of autoimmune diseases, and the progression of cancer.
TNF-α exerts its effects by binding to two distinct cell surface receptors, TNF receptor 1 (TNFR1) and TNF receptor 2 (TNFR2). Upon binding to its receptors, TNF-α activates multiple signaling pathways, including the nuclear factor-kappa B (NF-κB) pathway, the mitogen-activated protein kinase (MAPK) pathway, and the apoptotic pathway. These signaling pathways regulate various cellular processes, such as inflammation, cell proliferation, differentiation, and apoptosis.
In the context of infections, TNF-α plays a crucial role in the body's defense against pathogens. It promotes the recruitment and activation of immune cells, enhances the production of other pro-inflammatory cytokines, and stimulates the expression of adhesion molecules on endothelial cells, facilitating the migration of immune cells to the site of infection. TNF-α also helps to induce fever, which is an important component of the body's immune response to infections.
However, excessive or prolonged production of TNF-α can contribute to the development of chronic inflammatory diseases, such as rheumatoid arthritis, inflammatory bowel disease, and psoriasis. In these conditions, elevated levels of TNF-α promote the infiltration of immune cells into the affected tissues, leading to tissue damage and the perpetuation of inflammation. The central role of TNF-α in the pathogenesis of these diseases has led to the development of anti-TNF-α therapies, which have revolutionized the treatment of chronic inflammatory diseases. These therapies include monoclonal antibodies, such as infliximab and adalimumab, and soluble TNF receptor fusion proteins, such as etanercept. Anti-TNF-α therapies have been shown to be effective in reducing inflammation, improving symptoms, and slowing disease progression in patients with chronic inflammatory diseases.
In the context of cancer, TNF-α has complex and context-dependent effects on tumor development and progression. On one hand, TNF-α can promote anti-tumor immunity by activating immune cells and stimulating the production of other pro-inflammatory cytokines. On the other hand, chronic inflammation driven by TNF-α can promote tumor growth, angiogenesis, and metastasis. Therefore, the role of TNF-α in cancer is still an area of active research, and the development of TNF-α-targeted therapies for cancer remains a challenge.
In conclusion, TNF-α is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. Its involvement in various physiological and pathological processes has made it an important target for the development of therapies for chronic inflammatory diseases and cancer. Anti-TNF-α therapies have revolutionized the treatment of chronic inflammatory diseases, but the complex role of TNF-α in cancer remains an area of ongoing research. Understanding the precise mechanisms by which TNF-α contributes to disease pathogenesis will be crucial for the development of more effective and targeted therapies.
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.24 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 TNF-a 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:

Kruppel-Like Factor 6 Human Recombinant

Krueppel-like factor 6, B-cell-derived protein 1, Core promoter element-binding protein, GC-rich sites-binding factor GBF, Proto-oncogene BCD1, Suppressor of tumorigenicity 12 protein, Transcription factor Zf9, KLF6, BCD1, COPEB, CPBP, ST12.

Product # :

PRO-1864

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Description

KLF6 Human Recombinant produced in E. coli is. a single polypeptide chain containing 306 amino acids (1-283) and having a molecular mass of 34.3kDa. KLF6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The KLF6 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Kruppel-Like Factor 6 (KLF6) is a nuclear protein which has 3 zinc fingers. The zinc fingers of KLF6 are accountable for the specific DNA binding with the guanine-rich core promoter factors. The central region is involved in activation or posttranslational regulatory pathways, and the acidic N terminal domain takes part in the process of transcriptional activation.
Synonyms
Krueppel-like factor 6, B-cell-derived protein 1, Core promoter element-binding protein, GC-rich sites-binding factor GBF, Proto-oncogene BCD1, Suppressor of tumorigenicity 12 protein, Transcription factor Zf9, KLF6, BCD1, COPEB, CPBP, ST12.
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 MGSMDVLPMC SIFQELQIVH ETGYFSALPS LEEYWQQTCL ELERYLQSEP CYVSASEIKF DSQEDLWTKI ILAREKKEES ELKISSSPPE DTLISPSFCY NLETNSLNSD VSSESSDSSE ELSPTAKFTS DPIGEVLVSS GKLSSSVTST PPSSPELSRE PSQLWGCVPG ELPSPGKVRS GTSGKPGDKG NGDASPDGRR RVHRCHFNGC RKVYTKSSHL KAHQRTHTGE KPYRCSWEGC EWRFARSDEL TRHFRKHTGA KPFKCSHCDR CFSRSDHLAL HMKRHL.

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:

Tumor Necrosis Factor Receptor 13B Human Recombinant, Sf9

Tumor Necrosis Factor Receptor Superfamily Member 13B, Tumor Necrosis Factor Receptor Superfamily, Member 13B, Transmembrane Activator And CAML Interactor ,TACI , Tumor Necrosis Factor Receptor 13B, CD267 Antigen, TNFRSF14B, CD267, CVID2, IGAD2, CVID, RYZN.

Product # :

CYT-982

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Description

TACI produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 407 amino acids (1-165a.a.) and having a molecular mass of 45.8kDa (Molecular size on SDS-PAGE will appear at approximately 25-50kDa). TACI is expressed with a 242 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

TACI a protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4), 30% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
TNFRSF13B (TACI) is a transmembrane receptor protein found predominantly on the surface of B cells (a significant part of the immune system). TACI was at first discovered owing to its ability to interact with calcium-modulator and cyclophilin ligand (CAML). Later on, it was found that TACI plays a key role in humoral immunity by interacting with two members of the TNF family. Also, TACI controls T cell-independent B cell antibody responses, isotype switching, and B cell homeostasis.
Synonyms
Tumor Necrosis Factor Receptor Superfamily Member 13B, Tumor Necrosis Factor Receptor Superfamily, Member 13B, Transmembrane Activator And CAML Interactor ,TACI , Tumor Necrosis Factor Receptor 13B, CD267 Antigen, TNFRSF14B, CD267, CVID2, IGAD2, CVID, RYZN.
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
ADLMSGLGRS RRGGRSRVDQ EERFPQGLWT GVAMRSCPEE QYWDPLLGTC MSCKTICNHQ SQRTCAAFCR SLSCRKEQGK FYDHLLRDCI SCASICGQHP KQCAYFCENK LRSPVNLPPE LRRQRSGEVE NNSDNSGRYQ GLEHRGSEAS PALPGLKLSA DQVALVYSLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.

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:

Placental Growth Factor Human Recombinant, His Tag

PIGF, PGF, PLGF-1.

Product # :

CYT-1031

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Description

PLGF1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 19-131) containing 123 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 13.8kDa (calculated).

Source

Escherichia Coli.

Formulation

PLGF1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in PBS and 5% w/v trehalose, pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
PLGF is a growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration. It binds to receptor vegfr-1/flt1.
Synonyms
PIGF, PGF, PLGF-1.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein 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. PLGF1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHAS LPAVPPQQWA LSAGNGSSEV EVVPFQEVWG RSYCRALERL VDVVSEYPSE VEHMFSPSCV SLLRCTGCCG DENLHCVPVE TANVTMQLLK IRSGDRPSYV ELTFSQHVRC ECR.

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:

Keratinocyte Growth Factor-2 Human Recombinant

FGFA, FGF10, FGF-10, KGF-2, Fibroblast growth factor 10.

Product # :

CYT-303

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Description

Keratinocyte Growth Factor-2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 170 amino acids (40-208) and having a molecular mass of 19300 Dalton. Keratinocyte Growth Factor 2 is highly related to KGF-1(FGF-7), it binds to the same receptor as KGF-1 and shares 57% sequence homology. The FGF10 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2um filtered concentrated (1mg/ml) solution in 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, calculated by the dose-dependant stimulation of FGF receptors by BaF3 indicator cells (measured by ³H-thymidine uptake) is < 0.5 ng/ml, corresponding to a specific activity of 2x10⁶units/mg.

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Introduction
KGF-2 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-10 exhibits mitogenic activity for keratinizing epidermal cells, but essentially no activity for fibroblasts, which is similar to the biological activity of FGF7. Studies of the mouse homolog of suggested that this gene is required for embryonic epidermal morphogenesis including brain development, lung morphogenesis, and initiation of lim bud formation. This gene is also implicated to be a primary factor in the process of wound healing.
Synonyms
FGFA, FGF10, FGF-10, KGF-2, Fibroblast growth factor 10.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Keratinocyte Growth Factor-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF10 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 FGF-10 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MLGQDMVSPE ATNSSSSSFS SPSSAGRHVR SYNHLQGDVR WRKLFSFTKY FLKIEKNGKV SGTKKENCPY SILEITSVEI GVVAVKAINS NYYLAMNKKG KLYGSKEFNN DCKLKERIEE NGYNTYASFN WQHNGRQMYV ALNGKGAPRR GQKTRRKNTS AHFLPMVVHS.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.79 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-10 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:

LIGHT Human Recombinant

Tumor necrosis factor ligand superfamily member 14, CD258, Tnfsf14, Light

Product # :

CYT-1202

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Description

Recombinant Human LIGHT (74-240 aa) having a Mw of 23kDa was purified from E. coli.The Recombinant Human LIGHT is purified by proprietary chromatographic technique.

Source

Escherichia Coli.

Formulation

TNFSF14 solution contains PBS & 25mM K2CO3.

Purity

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

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Introduction
TNFRSF14, a member of the TNF receptor superfamily, is a type I transmembrane protein. TNFRSF14 is expressed in peripheral blood T cells, B cells, monocytes and in various tissues enriched in lymphoid cells. TNFRSF14 operates as a co-stimulatory factor for the activation of lymphoid cells and as a deterrent to infection by herpesvirus. Additionally, TNFRSF14 encourages the proliferation of T cells, and triggers apoptosis of various tumor cells.
Synonyms
Tumor necrosis factor ligand superfamily member 14, CD258, Tnfsf14, Light
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
DGPAGSWEQL IQERRSHEVN PAAHLTGANS SLTGSGGPLL WETQLGLAFL RGLSYHDGAL VVTKAGYYYI YSKVQLGGVG CPLGLASTIT HGLYKRTPRY PEELELLVSQ QSPCGRATSS SRVWWDSSFL GGVVHLEAGE KVVVRVLDER LVRLRDGTRS YFGAFMV

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-Acidic Human Recombinant, Sf9

HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.

Product # :

CYT-364

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Description

Fibroblast Growth Factor-1 Human Recombinant (FGF-1) produced in Sf9 insect cells is a single, glycosylated, polypeptide chain containing 140 amino acids and having a molecular mass of 15803 Dalton. The FGF-a is purified by proprietary chromatographic techniques.

Source

Baculovirus.

Formulation

The sterile protein solution (1.8mg/ml) contains 20mM Tris HCl pH=7.9, 100mM KCl, 0.2mM DTT and 20% glycerol.

Purity

Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <10 ng/ml, corresponding to a specific activity of 100,000IU/mg.

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Introduction
Acidic fibroblast growth factor 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. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. 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
HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.
Physical Appearance
Sterile Filtered liquid formulation.
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
The sequence of the first five N-terminal amino acids as determined and was found to be Met-Phe-Asn-Leu-Pro.
Background
What is the molecular weight/Mw of FGF 1 Protein?
FGF 1 Protein has a total Mw of 15.8kDa.

What is the source or expression system of FGF 1 Protein?
Baculovirus.

What is the Purity of FGF 1 Protein?
FGF 1 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF 1 Protein?
The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <10 ng/ml, corresponding to a specific activity of 100,000IU/mg.

What is the amino acid sequence of FGF 1 Protein?
FGF 1 Protein is composed from 140 amino acids.

What applications can FGF 1 Protein be used in?
FGF 1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF 1 Protein?
The endotoxin level is minimal, FGF 1 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:

General Transcription Factor IIA, 1 Human Recombinant

General transcription factor IIA, 1, 19/37kDa, TF2A1, TFIIA, TFIIA-42, TFIIAL, Transcription initiation factor IIA subunit 1, Transcription initiation factor TFIIA 42 kDa subunit, GTF2A1.

Product # :

PRO-1808

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Description

GTF2A1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 297 amino acids (1-274) and having a molecular mass of 32.2kDa. GTF2A1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GTF2A1 solution (0.5mg/ml) contains 20mM Tris-HCl(pH8.0), 20% glycerol, 0.15M NaCl and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
General Transcription Factor IIA, 1 (GTF2A1) in a complex along with TBP mediates transcriptional activity. GTF2A1 is a part of the transcription machinery of RNA polymerase II and is also participates in transcriptional activation.
Synonyms
General transcription factor IIA, 1, 19/37kDa, TF2A1, TFIIA, TFIIA-42, TFIIAL, Transcription initiation factor IIA subunit 1, Transcription initiation factor TFIIA 42 kDa subunit, GTF2A1.
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 MGSMANSANT NTVPKLYRSV IEDVINDVRD IFLDDGVDEQ VLMELKTLWE NKLMQSRAVD GFHSEEQQLL LQVQQQHQPQ QQQHHHHHHH QQAQPQQTVP QQAQTQQVLI PASQQATAPQ VIVPDSKLIQ HMNASNMSAA ATAATLALPA GVTPVQQILT NSGQLLQVVR AANGAQYIFQ PQQSVVLQQQ VIPQMQPGGV QAPVIQQVLA PLPGGISPQT GVIIQPQQIL FTGNKTQVIP TTVAAPTPAQ AQITATGQQQ PQAQPAQTQA PLVLQVD.

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:

Growth and Differentiation Factor 15 Human Recombinant

GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.

Product # :

CYT-335

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Description

GDF15 Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated, Polypeptide chain containing 2x113 amino acids and having a molecular mass of 24.8 kDa. The GDF15 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GDF15 is lyophilized from a sterile filtered solution containing 0.1% Trifluoroacetic Acid (TFA).

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
GDF15 is part of the TGF-Beta superfamily that is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.
Synonyms
GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GDF15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF15 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 GDF15 in sterile 18M-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MARNGDHCPL GPGRCCRLHT VRASLEDLGW ADWVLSPREV QVTMCIGACP SQFRAANMHA QIKTSLHRLK PDTVPAPCCV PASYNPMVLI QKTDTGVSLQ TYDDLLAKDC HCI.
Background
What is the molecular weight/Mw of GDF15 HUMAN Protein?
GDF15 HUMAN Protein has a total Mw of 24.8kDa.

What is the source or expression system of GDF15 HUMAN Protein?
Escherichia Coli.

What is the Purity of GDF15 HUMAN Protein?
GDF15 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF15 HUMAN Protein?
The biological functionality of GDF15 HUMAN Protein will be determined in the future.

What is the amino acid sequence of GDF15 HUMAN Protein?
MARNGDHCPL GPGRCCRLHT VRASLEDLGW ADWVLSPREV QVTMCIGACP SQFRAANMHA QIKTSLHRLK PDTVPAPCCV PASYNPMVLI QKTDTGVSLQ TYDDLLAKDC HCI.

What applications can GDF15 HUMAN Protein be used in?
GDF15 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDF15 HUMAN Protein?
The endotoxin level is minimal, GDF15 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:

Platelet-Derived Growth Factor B Human Recombinant

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-492

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Description

PDGF-B Human Recombinant mature chain produced in E.Coli is a non-glycosylated, polypeptide chain containing 109 amino acids fragment (82-190) and having a molecular mass of 16.75 kDa. The PDGF-B is fused with an amino-terminal hexahistidine tag and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Platelet-Derived Growth Factor-B is supplied in 25mM Na-Acetate pH 4.8, 1mM EDTA and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
The term ‘PDGF’ refers to a family of disulphide bond-linked dimeric isoforms that act as autocrine and paracrine growth factors and are produced by a variety of cell types other than platelets.
They act as potent mitogens for almost all mesenchymally-derived cells. Aberrant expression is involved in certain cancers, fibroproliferative disorders and atherosclerosis. The protein also contributes to wound healing and neural regeneration. There are four members of the PDGF family – PDGF A, PDGF B, PDGF C and PDGF D. Two distinct types of PDGF-A exist – a short form that is soluble and a long form that is retained by the extracellular matrix.
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 clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.

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:

Tumor Necrosis Factor-alpha Human Recombinant, Sf9

Tumor Necrosis Factor, TNFA, Tumor Necrosis Factor Ligand Superfamily Member 2, Cachectin, TNF-Alpha, TNFSF2, TNF-A, Tumor Necrosis Factor (TNF Superfamily, Member 2), Tumor Necrosis Factor-Alpha, TNF, Macrophage-Derived, TNF, Monocyte-Derived, TNF Superfamily, APC1 Protein, Member 2, DIF, Tumor necrosis factor.

Product # :

CYT-903

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Description

TNF a produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 163 amino acids (77-233a.a.) and having a molecular mass of 18.1kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). TNF a is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 90.0% as determined bySDS-PAGE.

Biological Activity

Measured in a cytotoxicity assay using L929 mouse fibrosarcoma cells in the presence of the metabolic inhibitor actinomycin D.

The ED50 for this effect is ≤ 0.2 ng/ml.

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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.
Synonyms
Tumor Necrosis Factor, TNFA, Tumor Necrosis Factor Ligand Superfamily Member 2, Cachectin, TNF-Alpha, TNFSF2, TNF-A, Tumor Necrosis Factor (TNF Superfamily, Member 2), Tumor Necrosis Factor-Alpha, TNF, Macrophage-Derived, TNF, Monocyte-Derived, TNF Superfamily, APC1 Protein, Member 2, DIF, Tumor necrosis 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
VRSSSRTPSD KPVAHVVANP QAEGQLQWLN RRANALLANG VELRDNQLVV PSEGLYLIYS QVLFKGQGCP STHVLLTHTI SRIAVSYQTK VNLLSAIKSP CQRETPEGAE AKPWYEPIYL GGVFQLEKGD RLSAEINRPD YLDFAESGQV YFGIIALHHH HHH.

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:

Growth and Differentiation Factor 15 D-Variant Human Recombinant

GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.

Product # :

CYT-314

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Description

GDF15 D-variant (His substitutes Asp at position 7) Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated, Polypeptide chain containing 2x113 amino acids and having a molecular mass of 24.5kDa. The GDF15 D-variant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GDF15 D-variant is lyophilized without additives.

Purity

Greater than 95.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

More Info

Introduction
GDF15 is part of the TGF-Beta superfamily that is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.
Synonyms
GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GDF15 D-variant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF15 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 GDF15 D-variant in sterile 5mM AcOH (acetic Acid) at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MARNGDDCPL GPGRCCRLHT VRASLEDLGW ADWVLSPREV QVTMCIGACP SQFRAANMHA QIKTSLHRLK PDTVPAPCCV PASYNPMVLI QKTDTGVSLQ TYDDLLAKDC HCI.
Background
What is the molecular weight/Mw of GDF15 D HUMAN Protein?
GDF15 D HUMAN Protein has a total Mw of 24.5kDa.

What is the source or expression system of GDF15 D HUMAN Protein?
Escherichia Coli.

What is the Purity of GDF15 D HUMAN Protein?
GDF15 D HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF15 D HUMAN Protein?
The biological functionality of GDF15 D HUMAN Protein will be determined in the future.

What is the amino acid sequence of GDF15 D HUMAN Protein?
MARNGDDCPL GPGRCCRLHT VRASLEDLGW ADWVLSPREV QVTMCIGACP SQFRAANMHA QIKTSLHRLK PDTVPAPCCV PASYNPMVLI QKTDTGVSLQ TYDDLLAKDC HCI.

What applications can GDF15 D HUMAN Protein be used in?
GDF15 D HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDF15 D HUMAN Protein?
The endotoxin level is minimal, GDF15 D 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:

Epidermal Growth Factor Human Recombinant

Urogastrone, URG, EGF.

Product # :

CYT-217

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Shipped at Room temp

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Description

Epidermal Growth Factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6.2kDa. The EGF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

EGF was lyophilized from a concentrated (1mg/ml) solution containing PBS pH-7.4.

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 0.1 ng/ml, corresponding to a specific activity of >1.0x10⁷ IU/mg.

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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF 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 Epidermal 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
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR.
Background
About EGF:
In the sphere of biomedical studies, epidermal boom factor (EGF) is a cornerstone that gives precious insights into the mechanisms underlying tissue healing, differentiation, and mobile proliferation. In this article we will explore the characteristics and uses of epidermal growth factor (EGF).
Description:
Epidermal growth factor (EGF) is a 6-kDa protein consisting of 53 amino acid residues and 3 intramolecular disulfide linkages. Human tissues, such as platelets, the parotid gland, and the submandibular gland, are rich in EGF. EGF, which was first discovered in human urine and the submaxillary glands of mice, functions as a major modulator of cell proliferation by attaching to its receptor, EGFR, which is found on the cell membrane. EGF triggers autophosphorylation of transmembrane protein tyrosine kinase EGFR upon binding, hence initiating downstream signaling cascades through pathways such as phosphatidylinositol and ras. Beyond the cell membrane, EGF has a variety of roles as it also initiates cytoplasmic processes such actin depolymerization and membrane ruffle formation. Studies indicate that EGF and its receptor might possibly be important components of the nucleus, highlighting the complexity of EGF-mediated cellular responses.
Function:
By attaching to the epidermal growth factor receptor (EGFR), EGF promotes the survival, differentiation, and multiplication of cells. This connection is essential for boosting many physiological processes and stimulating cell proliferation. The preservation of oro-esophageal and stomach tissue integrity is greatly supported by salivary EGF, which is regulated by dietary inorganic iodine. Its actions include the healing of gastric and oral ulcers, the inhibition of gastric acid secretion, the stimulation of DNA synthesis, and the protection of mucosal surfaces against harmful substances such as bile acids, gastric acid, and bacteria. Salivary EGF's role extends to repairing gastric tissue and addressing oro-esophagal issues, showcasing its healing ability in resolving oral and gastrointestinal ailments, including ulcers.
Mechanism:
EGF functions by forming a strong bond with the cell surface's epidermal growth factor receptor (EGFR), which triggers ligand- induced dimerization. This incident sets off the intrinsic protein-tyrosine kinase activity of EGFR, which in turn initiates a signal transduction cascade inside the cell. Numerous biochemical changes are brought about by this cascade, such as increased intracellular calcium levels, increased glycolysis and protein synthesis, and increased expression of particular genes, most notably the EGFR gene. These carefully planned alterations eventually promote DNA synthesis and cell division, illuminating the complex process by which EGF directs basic biological functions and modulates cellular responses.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6.2kDa.

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

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

What is the Biological Activity of EGF Protein?
The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 0.1 ng/ml, corresponding to a specific activity of >1.0x107 IU/mg.

What is the amino acid sequence of EGF Protein?
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR.

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

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

Vascular Endothelial Growth Factor Mouse Recombinant

Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

Product # :

CYT-336

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Shipped at Room temp

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Description

Vascular Endothelial Growth Factor Mouse Recombinant produced in E.Coli is a disulfide-linked homodimeric, double polypeptide chains containing 165 amino acids and having a molecular mass of 38.8kDa.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a 0.2µm filtered solution with PBS, pH 7.4.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The biological activity is determined by the dose-dependent stimulation of the proliferation of human umbilical vein endothelial cells (HUVEC) using a concentration range of 5.0 ng/ml corresponding to a specific activity of 200,000IU/mg.

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Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ). VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Vascular Endothelial Growth Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF 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 Vascular Endothelial 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
MAPTTEGEQK SHEVIKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCAGC CNDEALECVP TSESNITMQI MRIKPHQSQH IGEMSFLQHS RCECRPKKDR TKPEKHCEPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR.

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:

TRAIL Receptor-1 Human Recombinant

TNFRSF10A, TNF Receptor Superfamily Member 10a, Tumor Necrosis Factor Receptor Superfamily, Member 10a, TNF-Related Apoptosis-Inducing Ligand Receptor 1, Death Receptor 4, TRAIL Receptor 1, TRAIL-R1, TRAILR1, APO2, DR4, Tumor Necrosis Factor Receptor Superfamily Member 10a Variant 2, Tumor Necrosis Factor Receptor Superfamily Member 10A, Cytotoxic TRAIL Receptor, CD261 Antigen, TRAILR-1, CD261.

Product # :

CYT-1043

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Description

TNFRSF10A produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 224 amino acids (24-239a.a.) and having a molecular mass of 23.9kDa. TNFRSF10A is expressed with an 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TNFRSF10A protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Human TNFRSF10A is a type 1 transmembrane protein in the TNF R superfamily. TNFRSF10A is not expressed in rodents. The trimeric ligand Trail binds TNFRSF10A and induces apoptosis, and recombinant, soluble forms of the receptor inhibit Trail-induced apoptosis. TNFRSF10A is expressed generally in damaged, infected, and malignant cells. TNFRSF10A functions in immune surveillance, inducing apoptosis in cancer cells but not normal cells.
Synonyms
TNFRSF10A, TNF Receptor Superfamily Member 10a, Tumor Necrosis Factor Receptor Superfamily, Member 10a, TNF-Related Apoptosis-Inducing Ligand Receptor 1, Death Receptor 4, TRAIL Receptor 1, TRAIL-R1, TRAILR1, APO2, DR4, Tumor Necrosis Factor Receptor Superfamily Member 10a Variant 2, Tumor Necrosis Factor Receptor Superfamily Member 10A, Cytotoxic TRAIL Receptor, CD261 Antigen, TRAILR-1, CD261.
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
ASGTEAAAAT PSKVWGSSAG RIEPRGGGRG ALPTSMGQHG PSARARAGRA PGPRPAREAS PRLRVHKTFK FVVVGVLLQV VPSSAATIKL HDQSIGTQQW EHSPLGELCP PGSHRSEHPG ACNRCTEGVG YTNASNNLFA CLPCTACKSD EEERSPCTTT RNTACQCKPG TFRNDNSAEM CRKCSRGCPR GMVKVKDCTP WSDIECVHKE SGNGHNLEHH HHHH

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:

General Transcription Factor IIH Polypeptide 5 Human Recombinant

General transcription factor IIH subunit 5, bA120J8.2, C6orf175, TFB5, TFIIH, TGF2H5, TTD, TTD-A, TTDA, TFIIH basal transcription factor complex TTD-A subunit, TFB5 ortholog.

Product # :

PRO-2125

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Quantity :

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Shipped with Ice Packs

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Description

GTF2H5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 94 amino acids (1-71 a.a) and having a molecular mass of 10.4kDa.GTF2H5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GTF2H5 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
General Transcription Factor IIH Polypeptide 5 (GTF2H5) is a subunit of transcription/repair factor TFIIH, which serves in gene transcription and DNA repair. GTF2H5 protein stimulates ERCC3/XPB ATPase activity which triggers DNA opening during DNA repair, and is involved in the regulation of cellular levels of TFIIH. GTF2H5 gene mutations result in trichothiodystrophy, complementation group A.
Synonyms
General transcription factor IIH subunit 5, bA120J8.2, C6orf175, TFB5, TFIIH, TGF2H5, TTD, TTD-A, TTDA, TFIIH basal transcription factor complex TTD-A subunit, TFB5 ortholog.
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 MGSMVNVLKG VLIECDPAMK QFLLYLDESN ALGKKFIIQD IDDTHVFVIA ELVNVLQERV GELMDQNAFS LTQK.

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:

TRAIL Receptor-4 Human Recombinant

Tumor necrosis factor receptor superfamily member 10D, CD264, DCR2, TRAIL-R4, TRAILR4, TRUNDD, Decoy receptor 2, TNF-related apoptosis-inducing ligand receptor 4, TRAIL receptor 4, TRAIL receptor with a truncated death domain.

Product # :

CYT-1045

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Description

TNFRSF10D produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 395 amino acids (56-211a.a.) and having a molecular mass of 73.8kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).TNFRSF10D is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TNFRSF10D protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured in a neutralizing assay using Jurkat human T lymphocyte. The ED50 for this effect is less or equal to 10 ng/ml in the presence of 2ng/ml TRAIL.

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Introduction
TRAIL Receptor-4 Human Recombinant or TNFRSF10D, is part of the TNF-receptor superfamily. TNFRSF10D has atruncated cytoplasmic death domai , an extracellular TRAIL-binding domain and a transmembrane domain. The protein can prevent from TRAIL-mediated apoptosis on cells with TRAIL R1 and/or TRAIL R2.
Synonyms
Tumor necrosis factor receptor superfamily member 10D, CD264, DCR2, TRAIL-R4, TRAILR4, TRUNDD, Decoy receptor 2, TNF-related apoptosis-inducing ligand receptor 4, TRAIL receptor 4, TRAIL receptor with a truncated death domain.
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
ATIPRQDEVP QQTVAPQQQR RSLKEEECPA GSHRSEYTGA CNPCTEGVDY TIASNNLPSC LLCTVCKSGQ TNKSSCTTTR DTVCQCEKGS FQDKNSPEMC RTCRTGCPRG MVKVSNCTPR SDIKCKNESA ASSTGKTPAA EETVTTILGM LASPYHVEPK SCDKTHTCPP CPAPELLGGP
SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ
QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.

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:

Leukemia Inhibitory Factor Rat Recombinant

Leukemia inhibitory factor, Cholinergic neuronal differentiation factor, Lif.

Product # :

CYT-731

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Description

Leukemia Inhibitory Factor (LIF) Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 19.8 kDa. The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

LIF Rat was lyophilized from 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

Purity

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

Biological Activity

The activity of rat LIF is determined by the ability to induce differentiation of M1 myeloid leukemic cells. The minimum detectable concentration of rat LIF in this assay is 0.5ng/mL.

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Introduction
Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.
Synonyms
Leukemia inhibitory factor, Cholinergic neuronal differentiation factor, Lif.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leukemia Inhibitory Factor (LIF) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leukemia Inhibitory Factor (LIF) 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 Leukemia Inhibitory Factor (LIF) in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SPLPITPVNA TCAIRHPCHG NLMNQIKSQL AQLNGSANAL FISYYTAQGE PFPNNVDKLC APNMTDFPPF HANGTEKTKL VELYRMVTYL GASLTNITWD QKNLNPTAVS LQIKLNATTD VMRGLLSSVL CRLCNKYHVG HVDVPCVPDN SSKEAFQRKK LGCQLLGTYK QVISVLAQAF .

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 Ligand Receptor Superfamily Member 10B Human Recombinant, Sf9

TNFRSF10B, CD262, DR5, KILLER, KILLER/DR5, TRAIL-R2, TRAILR2, TRICK2, TRICK2A, TRICK2B, TRICKB, ZTNFR9, Death receptor 5, TNF-related apoptosis-inducing ligand receptor 2.

Product # :

CYT-1055

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Description

TNFRSF10B produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 394 amino acids (56-210a.a.) and having a molecular mass of 43.9kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).TNFRSF10B is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

TNFRSF10B protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

Biological Activity

Measured by its ability to inhibit cytotoxicity assay using Jurkat human T lymphocyte. The ED50 for this effect ≤ to 5ng/ml with TRAIL

.

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Introduction
TRAIL Receptor-1 (DR4) and TRAIL Receptor-2(DR5) are members of the TNFR superfamily of transmembrane proteins and contain a cytoplasmic "death domain", which is capable of activating the cell's apoptotic machinery. These receptors are activated by binding to either membrane anchored or soluble TRAIL/Apo2L.
Synonyms
TNFRSF10B, CD262, DR5, KILLER, KILLER/DR5, TRAIL-R2, TRAILR2, TRICK2, TRICK2A, TRICK2B, TRICKB, ZTNFR9, Death receptor 5, TNF-related apoptosis-inducing ligand receptor 2.
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
ITQQDLAPQQ RAAPQQKRSS PSEGLCPPGH HISEDGRDCI SCKYGQDYST HWNDLLFCLR CTRCDSGEVE LSPCTTTRNT VCQCEEGTFR EEDSPEMCRK CRTGCPRGMV KVGDCTPWSD IECVHKESGT KHSGEVPAVE ETVTSSPGTP ASPCSLEPKS CDKTHTCPPC PAPELLGGPS
VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ
GNVFSCSVMH EALHNHYTQK SLSLSPGKHH HHHH.

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 AA Mouse Recombinant

Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, PDGF-AA, PDGF-1.

Product # :

CYT-590

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Description

PDGF-AA Mouse Recombinant is a disulfide linked homodimeric, non-glycosylated, polypeptide chain containing 2 x 126 amino acids and having a total molecular mass of 28.9 kDa. PDGF-AA is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized with no additives.

Purity

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

Biological Activity

Established by the dose-dependent stimulation of Balb/c 3T3 cells proliferation. The expected ED50 for this effect is 8-10 ng/ml corresponding to a specific activity of 100,000-125,000IU/mg.

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Introduction
PDGF-AA, PDGF-BB and PDGF-AB, are potent mitogens for a variety of cell types including smooth muscle cells, connective tissue cells, bone and cartilage cells, and some blood cells. The PDGF is stored in platelet alpha-granules and released upon platelet activation. The PDGF is involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. Two distinct signaling receptors used by PDGF have been identified and named PDGFR-alpha and PDGFR-beta. PDGFR-alpha is high-affinity receptor for each of the three PDGF forms. On the other hand, PDGFR-beta interacts with only PDGF-BB and PDGF-AB.
Synonyms
Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, PDGF-AA, PDGF-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PDGF-AA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF-AA 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 PDGF-AA in sterile 18MΩ-cm H2O at a concentration ranging between 0.1-0.5mg per 1ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSIEEAVPAV CKTRTVIYEI PRSQVDPTSA NFLIWPPCVE VKRCTGCCNT SSVKCQPSRV HHRSVKVAKV EYVRKKPKLK EVQVRLEEHL ECACATSNLN PDHREEETGR RRESGKNRKR KRLKPT.

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 Mouse Recombinant, Sf9

Fibroblast growth factor 21, FGF-21.

Product # :

CYT-930

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sds-page

Description

FGF-21 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 190 amino acids (29-210a.a.) and having a molecular mass of 21.0kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). FGF21 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

FGF-21 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

sds-page

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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-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 colorless 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
AYPIPDSSPL LQFGGQVRQR YLYTDDDQDT EAHLEIREDG TVVGAAHRSP ESLLELKALK PGVIQILGVK ASRFLCQQPD GALYGSPHFD PEACSFRELL LEDGYNVYQS EAHGLPLRLP QKDSPNQDAT SWGPVRFLPM PGLLHEPQDQ AGFLPPEPPD VGSSDPLSMV EPLQGRSPSY ASLEHHHHHH.
Background
What is the molecular weight/Mw of FGF21 MOUSE,SF9 Protein?
FGF21 MOUSE,SF9 Protein has a total Mw of 21kDa.

What is the source or expression system of FGF21 MOUSE,SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of FGF21 MOUSE,SF9 Protein?
FGF21 MOUSE,SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF21 MOUSE,SF9 Protein?
The biological functionality of FGF21 MOUSE,SF9 Protein will be determined in the future.

What is the amino acid sequence of FGF21 MOUSE,SF9 Protein?
AYPIPDSSPL LQFGGQVRQR YLYTDDDQDT EAHLEIREDG TVVGAAHRSP ESLLELKALK PGVIQILGVK ASRFLCQQPD GALYGSPHFD PEACSFRELL LEDGYNVYQS EAHGLPLRLP QKDSPNQDAT SWGPVRFLPM PGLLHEPQDQ AGFLPPEPPD VGSSDPLSMV EPLQGRSPSY ASLEHHHHHH.

What applications can FGF21 MOUSE,SF9 Protein be used in?
FGF21 MOUSE,SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF21 MOUSE,SF9 Protein?
The endotoxin level is minimal, FGF21 MOUSE,SF9 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:

GDNF Family Receptor Alpha 3 Human Recombinant, Sf9

GDNF Family Receptor Alpha3, GDNFR-alpha-3, GFR-alpha-3, GDNF Receptor Alpha-3, GDNFR3, GDNF Family Receptor Alpha-3, Glial Cell Line-Derived Neurotrophic Factor Receptor Alpha-3, GPI-Linked Receptor, GFRA3.

Product # :

CYT-1013

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Description

GFRA3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 585 amino acids (32-374) and having a molecular mass of 65.5kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). GFRA3 is fused to a 239 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

GFRA3 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
GDNF Family Receptor Alpha 3 (GFRA3) belongs to the GDNF receptor family. GFRA3 creates a signaling receptor complex with RET tyrosine kinase receptor and binds the ligand, artemin (ARTN).
Synonyms
GDNF Family Receptor Alpha3, GDNFR-alpha-3, GFR-alpha-3, GDNF Receptor Alpha-3, GDNFR3, GDNF Family Receptor Alpha-3, Glial Cell Line-Derived Neurotrophic Factor Receptor Alpha-3, GPI-Linked Receptor, GFRA3.
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
ADPDPLPTES RLMNSCLQAR RKCQADPTCS AAYHHLDSCT SSISTPLPSE EPSVPADCLE AAQQLRNSSL IGCMCHRRMK NQVACLDIYW TVHRARSLGN YELDVSPYED TVTSKPWKMN LSKLNMLKPD SDLCLKFAML CTLNDKCDRL RKAYGEACSG PHCQRHVCLR QLLTFFEKAA EPHAQGLLLC PCAPNDRGCG ERRRNTIAPN CALPPVAPNC LELRRLCFSD PLCRSRLVDF QTHCHPMDIL GTCATEQSRC LRAYLGLIGT AMTPNFVSNV NTSVALSCTC RGSGNLQEEC EMLEGFFSHN PCLTEAIAAK MRFHSQLFSQ DWPHPTFAVM AHQNENLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.
Background
What is the molecular weight/Mw of GFRA3 HUMAN, SF9 Protein?
GFRA3 HUMAN, SF9 Protein has a total Mw of 65.5kDa.

What is the source or expression system of GFRA3 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.
What is the Purity of GFRA3 HUMAN, SF9 Protein?
GFRA3 HUMAN, SF9 Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of GFRA3 HUMAN, SF9 Protein?
The biological functionality of GFRA3 HUMAN, SF9 Protein will be determined in the future.

What is the amino acid sequence of GFRA3 HUMAN, SF9 Protein?
ADPDPLPTES RLMNSCLQAR RKCQADPTCS AAYHHLDSCT SSISTPLPSE EPSVPADCLE AAQQLRNSSL IGCMCHRRMK NQVACLDIYW TVHRARSLGN YELDVSPYED TVTSKPWKMN LSKLNMLKPD SDLCLKFAML CTLNDKCDRL RKAYGEACSG PHCQRHVCLR QLLTFFEKAA EPHAQGLLLC PCAPNDRGCG ERRRNTIAPN CALPPVAPNC LELRRLCFSD PLCRSRLVDF QTHCHPMDIL GTCATEQSRC LRAYLGLIGT AMTPNFVSNV NTSVALSCTC RGSGNLQEEC EMLEGFFSHN PCLTEAIAAK MRFHSQLFSQ DWPHPTFAVM AHQNENLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.

What applications can GFRA3 HUMAN, SF9 Protein be used in?
GFRA3 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GFRA3 HUMAN, SF9 Protein?
The endotoxin level is minimal, GFRA3 HUMAN, SF9 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.

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