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1000 results found for “Beta-NGF”
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Name :
TGFBR1 HumanDescription:
Transforming Growth Factor Beta Receptor I Human Recombinant
TGFBR1, AAT5, ACVRLK4, ALK-5, ALK5, ESS1, LDS1, LDS1A, LDS2A, MSSE, SKR4, tbetaR-I, TGFR-1.
Product # :
PKA-111Price :
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Shipped with Ice Packs
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Description
TGFBR1produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 342 amino acids (27-126a.a.) and having a molecular mass of 38.0kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).TGFBR1is expressed with a 242 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TGFBR1protein solution (0.5mg/ml) Phosphate Buffered Saline (pH 7.4) containing 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
TGFBR1 is a single-pass type 1 membrane protein which is a part of the TGFB receptor subfamily and the protein kinase superfamily. TGFBR1 is a secreted protein that performs many cellular functions such as the control of cell growth, cell differentiation, cell proliferation and apoptosis. TGFBR1 also controls the immune system and shows different activities on various types of cell, or cells at different developmental stages.
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Synonyms
TGFBR1, AAT5, ACVRLK4, ALK-5, ALK5, ESS1, LDS1, LDS1A, LDS2A, MSSE, SKR4, tbetaR-I, TGFR-1.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
ADLLLPGATA LQCFCHLCTK DNFTCVTDGL CFVSVTETTD KVIHNSMCIA EIDLIPRDRP FVCAPSSKTG SVTTTYCCNQ DHCNKIELPT TVKSSPGLGP VELVEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.
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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Name :
IL 1 beta Human, HisDescription:
Interleukin-1 beta Human Recombinant, His Tag
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
Product # :
CYT-480Price :
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Shipped with Ice Packs
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Description
Interleukin-1 beta His-Tag Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 153 amino acids fragment (117-269) and having a total molecular mass of 21.88 kDa fused with an amino-terminal hexahistidine tag. The IL-1b His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL-1b His tag protein solution is supplied in 20mM Tris-HCl pH 8.0 and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Interleukin-1b is a potent pro-inflammatory cytokine produced by a wide variety of cell types including monocytes and macrophages. It displays a broad range of biological activity including activation of B and T cells in response to inflammation and the activation of endothelial cells.
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Synonyms
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
APVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFV
QGEESNDKIPVALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKME
KRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS
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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Name :
IL 1 beta PorcineDescription:
Interleukin-1 beta Porcine Recombinant
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
Product # :
CYT-400Price :
Quantity :
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Shipped at Room temp
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Description
Recombinant IL 1 beta Porcine produced in E.coli cells is a non-glycosylated, homodimeric protein containing 153 amino acid chain and having a molecular mass of 17.6kDa. The IL 1 beta is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The IL 1 beta was lyophilized from a 0.2µm filtered concentrated solution in PBS pH 7.4, containing 3 % trehalose.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by a cell proliferation assay using murine D10S cells is less than 5.0 ng/ml, corresponding to a specific activity of > 2.0 × 105 IU/mg.
More Info
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Introduction
Interleukin-1b is produced by activated macrophages, IL-1B stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1B proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells.
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Synonyms
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IL 1 beta although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL 1 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.
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Solubility
It is recommended to reconstitute the lyophilized IL 1 beta in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
ANVQSMECKL QDKDHKSLVL AGPHMLKALH LLTGDLKREV VFCMSFVQGD DSNNKIPVTL GIKGKNLYLS CVMKDNTPTL QLEDIDPKRY PKRDMEKRFV FYKTEIKNRV EFESALYPNW YISTSQAEQK PVFLGNSKGR QDITDFTMEV LSP
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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Name :
TNF a RatDescription:
Tumor Necrosis Factor-Alpha Rat Recombinant
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
Product # :
CYT-393Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Tumor Necrosis Factor-a Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17339.44 Dalton. The TNF-alpha is purified by standard chromatographic techniques.
Source
Escherichia Coli.
Formulation
The concentrated protein solution (1mg/ml) was lyophilized from 20mM phosphate buffer and 0.1M NaCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.05ng/ml, corresponding to a Specific Activity of 20,000,000 IU/mg.More Info
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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, and cancer. -
Synonyms
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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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.
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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.
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Amino Acid Sequence
MLRSSSQNSS DKPVVHVVAN HQAEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLIY SQVLFKGQGC PDYVLLTHTV SRFATSYQEK VSLLSAIKSP CPKDTPEGAE LKPWYEPMYL GGVSQLEKGD LLSAEVNLPK YLDITESGQV YFGVIAL.
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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Name :
IL 1 Beta AntibodyDescription:
Interleukin-1b, Mouse Anti-Human
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
Product # :
ANT-248Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Formulation
1 mg/ml in PBS (after reconstitution).
More Info
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Introduction
Interleukin-1b is produced by activated macrophages, IL-1B stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1B proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells.
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Synonyms
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
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Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
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Immunogen
r.Human IL-1b.
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Ig Subclass
Mouse IgG2b.
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Clone
NYR-hIL1b.
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Applications
Direct ELISA, Western Blot, Immuneprecipitation, immunohistochemistry.
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Note
The antibody was produced in BALB/c mice.
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Titer
By direct ELISA, 1:20,000 dilution will yield >1.0 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories). 1:2,000 dilution will completely inhibit a thymocyte co-stimulation assay using suboptimal doses of concanavalin A.
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Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
In lyophilized form, for long periods, store at 4°C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
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Purification Method
Ion Exchange.
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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Name :
NRG1 HumanDescription:
Heregulin-B2 Human Recombinant
Neuregulin-1, NRG1, GGF, HGL, HRGA, NDF, SMDF, HRG, ARIA, GGF2, HRG1.
Product # :
CYT-407Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Human Neuregulin-1 beta 2 produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 61 amino acids and having a total molecular mass of 7.0kDa. NRG-1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered 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 as determined by a cell proliferation assay using serum free human MCF-7 cells is less than 5ng/ml, corresponding to a specific activity of > 2.0 × 105 U/mg.
More Info
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Introduction
Neuregulin is a signaling protein for ErbB2/ErbB4 receptor heterodimers on the cardiac muscle cells, playing an important role in heart structure and function through inducing ErbB2/ErbB4 receptor phosphorylation and cardiomyocyte differentiation. Research on molecular level discovered that neuregulin recombinant could make disturbed myocardial cell structure into order and strengthen the connection between myocardial cells by intercalated discs re-organization. Pharmacodynamic experiments in animals showed that neuregulin (NRG1) recombinant can reduce the degree of damage on myocardial cells caused by ischemia, hypoxia and viral infection.
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Synonyms
Neuregulin-1, NRG1, GGF, HGL, HRGA, NDF, SMDF, HRG, ARIA, GGF2, HRG1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized NRG1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Heregulin should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized NRG1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SHLVKCAEKEKTFCVNGGECFMVKDLSNPSRYLCKCPNEFTGDRCQNYVMASFYKAEELYQ.
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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Name :
GFRA1 RatDescription:
GDNF Family Receptor Alpha 1 Rat Recombinant
GDNF family receptor alpha-1, GDNF receptor alpha-1, GDNFR-alpha-1, GFR-alpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, Gfra1, Gdnfra, Retl1, Trnr1.
Product # :
CYT-1012Price :
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Shipped with Ice Packs
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Description
GFRA1 Rat Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 645 amino acids (25-430a.a.) and having a molecular mass of 72.3kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). GFRA1 is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
GFRA1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
GDNF family receptor alpha-1 (GFRA1) belongs to the GDNF receptor family. GFRA1 is a glycosyl-phosphatidylinositol(GPI)-linked cell surface receptor for both Glial cell line-derived growth factor (GDNF), neurturin (NTN), and mediates activation of the RET tyrosine kinase receptor. The GFRA1 protein is a potent survival factor for central and peripheral neurons, and is vital for the development of kidneys and the enteric nervous system.
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Synonyms
GDNF family receptor alpha-1, GDNF receptor alpha-1, GDNFR-alpha-1, GFR-alpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, Gfra1, Gdnfra, Retl1, Trnr1.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLTS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRA VPFISDVFQQ VEHISKGNNC LDAAKACNLD DTCKKYRSAY ITPCTTSMSN EVCNRRKCHK ALRQFFDKVP AKHSYGMLFC SCRDIACTER RRQTIVPVCS YEERERPNCL SLQDSCKTNY ICRSRLADFF TNCQPESRSV SNCLKENYAD CLLAYSGLIG TVMTPNYVDS SSLSVAPWCD CSNSGNDLED CLKFLNFFKD NTCLKNAIQA FGNGSDVTMW QPAPPVQTTT ATTTTAFRVK NKPLGPAGSE NEIPTHVLPP CANLQAQKLK SNVSGSTHLC LSDSDFGKDG LAGASSLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.
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Background
What is the molecular weight/Mw of GFRA1 RAT Protein?
GFRA1 RAT Protein has a total Mw of 72.3kDa.
What is the source or expression system of GFRA1 RAT Protein?
Sf9, Baculovirus cells.
What is the Purity of GFRA1 RAT Protein?
GFRA1 RAT Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of GFRA1 RAT Protein?
The biological functionality of GFRA1 RAT Protein will be determined in the future.
What is the amino acid sequence of GFRA1 RAT Protein?
DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLTS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRA VPFISDVFQQ VEHISKGNNC LDAAKACNLD DTCKKYRSAY ITPCTTSMSN EVCNRRKCHK ALRQFFDKVP AKHSYGMLFC SCRDIACTER RRQTIVPVCS YEERERPNCL SLQDSCKTNY ICRSRLADFF TNCQPESRSV SNCLKENYAD CLLAYSGLIG TVMTPNYVDS SSLSVAPWCD CSNSGNDLED CLKFLNFFKD NTCLKNAIQA FGNGSDVTMW QPAPPVQTTT ATTTTAFRVK NKPLGPAGSE NEIPTHVLPP CANLQAQKLK SNVSGSTHLC LSDSDFGKDG LAGASSLEPK 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 GFRA1 RAT Protein be used in?
GFRA1 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GFRA1 RAT Protein?
The endotoxin level is minimal, GFRA1 RAT 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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Name :
TNFA Rat, His ActiveDescription:
Tumor Necrosis Factor-alpha Rat Recombinant, His Tag Active
Tumor Necrosis Factor-alpha, TNF a His, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, N-terminal fragment, NTF, Intracellular domain 1, Intracellular domain 2, ICD2, C-domain 1, C-domain 2, Tumor necrosis factor, soluble form, Tnfa, Tnfsf2, RATTNF, Tnfa.
Product # :
CYT-1057Price :
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Shipped with Ice Packs
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Description
TNFA Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (80-235 a.a) and having a molecular mass of 19.9kDa.TNFA Rat is expressed with an 25 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TNFA Rat protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-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 ≤ to 0.2 ng/ml.More Info
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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-alpha, TNF a His, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, N-terminal fragment, NTF, Intracellular domain 1, Intracellular domain 2, ICD2, C-domain 1, C-domain 2, Tumor necrosis factor, soluble form, Tnfa, Tnfsf2, RATTNF, Tnfa.
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Physical Appearance
Sterile Filtered colorless liquid.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMLRSSS QNSSDKPVAH VVANHQAEEQ LEWLSQRANA LLANGMDLKD NQLVVPADGL YLIYSQVLFK GQGCPDYVLL THTVSRFAIS YQEKVSLLSA IKSPCPKDTP EGAELKPWYE PMYLGGVFQL EKGDLLSAEV NLPKYLDITE SGQVYFGVIA L.
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Background
Tumor Necrosis Factor-alpha Rat Recombinant, His Tag Active: An In-Depth Analysis
Abstract:
Tumor Necrosis Factor-alpha (TNF-α) is a cytokine that plays a significant role in various physiological and pathological processes. This human research paper provides an in-depth analysis of TNF-α Rat Recombinant with a His Tag, focusing on its structure, signaling pathways, and diverse functions. Additionally, the paper explores the potential applications of TNF-α Rat Recombinant in human research.Introduction:
TNF-α is a key mediator of inflammation and immune responses in humans. This research paper aims to provide a comprehensive analysis of TNF-α Rat Recombinant with a His Tag, highlighting its significance in human physiology and its potential applications in human research.Structure and Function of TNF-α:
TNF-α is a homotrimeric protein that binds to two distinct receptors, TNFR1 and TNFR2, initiating downstream signaling cascades. It regulates immune cell activation, cytokine production, and cellular responses, influencing diverse biological processes.Signaling Pathways:
Upon binding to its receptors, TNF-α activates various signaling pathways, including the NF-κB pathway, MAPK pathway, and cell death pathways. These pathways regulate gene expression and mediate cellular responses, impacting inflammation, apoptosis, and tissue homeostasis.Functions of TNF-α:
TNF-α plays a crucial role in immune responses, inflammation, and tissue homeostasis. It regulates the activation and migration of immune cells, promotes cytokine production, and modulates cell survival and death. Dysregulation of TNF-α is implicated in the pathogenesis of various human diseases, making it an attractive target for research and therapeutic interventions.Applications in Human Research:
TNF-α Rat Recombinant with a His Tag has diverse applications in human research. It can be used to investigate TNF-α signaling pathways, study its effects on immune cell functions, and explore its role in disease pathogenesis. Additionally, this recombinant protein can be utilized for in vitro and in vivo studies aimed at developing novel therapeutic strategies.Future Directions:
Further research is necessary to unravel the intricate mechanisms of TNF-α signaling and its contributions to human diseases. Continued investigations will enable the development of targeted therapies and personalized medicine approaches. Future studies should also focus on optimizing the use of TNF-α Rat Recombinant in preclinical and clinical research settings.
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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Name :
TGFBI HumanDescription:
Transforming Growth Factor Beta Induced Human Recombinant
Transforming growth factor-beta-induced protein ig-h3, Beta ig-h3, Kerato-epithelin, RGD-containing collagen-associated protein, RGD-CAP, TGFBI, BIGH3, CSD, CDB1, CDG2, CSD1, CSD2, CSD3, EBMD, LCD1, CDGG1.
Product # :
PRO-568Price :
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Shipped with Ice Packs
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Description
TGFBI Human Recombinant produced in e.Coli is a single, non-glycosylated, polypeptide containing 135 amino acids (502-636) and having a molecular mass of 14.5 kDa. The TGFBI recombinant Human protein is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TGFBI recombinant Human is formulated 20mM Tris-HCl pH-8.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Transforming Growth Factor Beta Induced protein also known as TGFBI is an extracellular matrix protein induced by transforming growth factor (TGF)-beta 1. TGFBI protein is involved in cell growth, cell differentiation, wound healing and cell adhesion. In addition, some missense mutations of TGFBI were identified in families affected with human autosomal dominant corneal dystrophies. TGFBI gene encodes for a 683 amino-acid protein containing an RGD motif and four internal repeated domains which have highly conserved sequences founded in several species (Fasciclin domain).
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Synonyms
Transforming growth factor-beta-induced protein ig-h3, Beta ig-h3, Kerato-epithelin, RGD-containing collagen-associated protein, RGD-CAP, TGFBI, BIGH3, CSD, CDB1, CDG2, CSD1, CSD2, CSD3, EBMD, LCD1, CDGG1.
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Physical Appearance
Sterile filtered liquid formulation.
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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.
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Amino Acid Sequence
MGTVMDVLKG DNRFSMLVAA IQSAGLTETL NREGVYTVFA PTNEAFRALP PRERSRLLGD AKELANILKY HIGDEILVSG GIGALVRLKS LQGDKLEVSL KNNVVSVNKE PVAEPDIMAT NGVVHVITNV LQPPA.
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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Name :
TGFB1 Human, HEKDescription:
Transforming Growth Factor-Beta 1 Human Recombinant, HEK
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, LAP, TGFB1.
Product # :
CYT-1260Price :
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Description
TGFB1 Human Recombinant produced in 293 cells is a glycosylated homodimer polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.0kDa. The TGFB1 is purified by proprietary chromatographic techniques.
Source
HEK 293 cells.
Formulation
Lyophilized from a sterile filtered solution containing TFA (0.1%).
Purity
Greater than 98.0% as determined by: (a) Analysis by HPLC. (b) Analysis by SDS-PAGE.
Biological Activity
The ED50 as determined by the dose-dependent inhibition of IL-4-induced proliferation of HT-2 cells is ≤ 0.05 ng/ml, corresponding to a specific activity of ≥ 2 x 107 units/mg.
More Info
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Synonyms
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, LAP, TGFB1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TGFB1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB1 Human should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized TGFB1 in sterile in 18MΩ-cm H2O at a concentration of 0.1 mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
ALDTNYCFSS TEKNCCVRQL YIDFRKDLGW KWIHEPKGYH ANFCLGPCPY IWSLDTQYSK VLALYNQHNP GASAAPCCVP QALEPLPIVY YVGRKPKVEQ LSNMIVRSCK CS.
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Background
Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. 3 TGF Betas have been identified in mammals: TGF Beta 1, TGF Beta 2 and TGF Beta 3. each are synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL 1 beta Human, HEKDescription:
Interleukin-1 beta Human Recombinant, HEK
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
Product # :
CYT-094Price :
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Description
Interleukin-1 beta Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 18-25kDa due to glycosylation.The IL-1 beta is purified by proprietary chromatographic techniques.
Source
HEK.
Formulation
The IL-1 beta was lyophilized from 1mg/ml in 1xPBS.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
The specific activity was determined by the dose-dependent stimulation of the proliferation of mouse D10S cells and is typically 0.02-0.08ng/ml.More Info
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Introduction
Interleukin-1b is produced by activated macrophages, IL-1B stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1B proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells.
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Synonyms
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IL-1 beta although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-1 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.
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Solubility
It is recommended to reconstitute the lyophilized IL-1b in sterile PBS containing 0.1% endotoxin-free recombinant HSA.
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Amino Acid Sequence
APVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFVQGEESNDKIP
VALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKMEKRFVFNKIEINNKLEFES
AQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS.
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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Name :
TNF a Mutant HumanDescription:
Tumor Necrosis Factor-Alpha Mutant Human Recombinant
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
Product # :
CYT-384Price :
Quantity :
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Description
Tumor Necrosis Factor-a Variant Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 151 amino acids and having a molecular mass of 16598 Dalton. The TNF-alpha Variant is purified by standard chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized after extensive dialysis against 0.5x PBS pH -7.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.05ng/ml, corresponding to a Specific Activity of 20,000,000 units/mg.More Info
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Introduction
The clinical use of the potent anti-tumor activity of TNF-a has been limited by the proinflammatory side effects including fever, dose-limiting hypotension, hepatotoxicity, intravascular thrombosis, and hemorrhage. Designing clinically applicable TNF-a mutants with low systemic toxicity has been an intense pharmacological interest. Human TNF-a, which binds to the murine TNF-R55 but not to the mouse TNF-R75, exhibits retained anti-tumor activity and reduced systemic toxicity in mice compared with murine TNF-a, which binds to both murine TNF receptors. Based on these results, many TNF-? mutants that selectively bind to TNF-R55 have been designed. These mutants displayed cytotoxic activities on tumor cell lines in vitro, and exhibited lower systemic toxicity in vivo.
Recombinant Human TNF-a Variant/Mutant compared with the wild-type, has an amino acid sequence deletion from a.a. 1-7, and the following a.a. substitutes Arg8, Lys9, Arg10 and Phe157 which is proven tohave more activity and with less inflammatory side effect in vivo. -
Synonyms
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Tumor Necrosis Factor-a Variant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-a Variant 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.
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Solubility
It is recommended to reconstitute the lyophilized Tumor Necrosis Factor-alpha Variant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MRKRKPVAHV VANPQAEGQL QWLNRRANAL LANGVELRDN
QLVVPSEGLY LIYSQVLFKG QGCPSTHVLL THTISRIAVS YQTKVNLLSA IKSPCQRETP EGAEAKPWYE PIYLGGVFQL EKGDRLSAEI NRPDYLDFAE SGQVYFGIIAF.
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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Name :
sRANKL Human, GSTDescription:
Soluble RANK Ligand Human Recombinant, GST tag
Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf, hRANKL2.
Product # :
CYT-631Price :
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Description
RANKL Human Recombinant fused to GST tag produced in E.Coli is a single, non-glycosylated polypeptide having a molecular mass of 47 kDa. RANKL is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The soluble RANKL protein solution contains 1mM EDTA and PBS pH-7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
RANKL binds to tnfrsf11b/opg and to tnfrsf11a/rank. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive t-cell proliferation. May be an important regulator of interactions between t-cells and dendritic cells and may play a role in the regulation of the t-cell-dependent immune response. sRANKL may also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy. By injecting soluble RANKL, novel osteopenia model mice were established in only 50 hours. Degree of bone loss can be controlled by changing doses of sRANKL. RANKL can be used in establishing osteopenia model for in vivo screening of drugs for osteoporosis, determination of effect and mechanism, evaluation of bone anabolic drugs.
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Synonyms
Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf, hRANKL2.
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Physical Appearance
Sterile Filtered colorelss clear solution.
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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.
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Name :
EGF (Leu 21) HumanDescription:
Epidermal Growth Factor (Leu-21) Human Recombinant
Urogastrone, URG, EGF.
Product # :
CYT-466Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
EGF 21-Leu Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6205 Dalton.The EGF 21-Leu is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50, calculated by the dose-dependant proliferation of MDCK cells is < 10ng/ml concentration corresponding to a Specific Activity of 100,000IU/mg.More Info
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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.
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Synonyms
Urogastrone, URG, EGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Epidermal Growth Factor 21 Leu although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF 21-Leu 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.
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Solubility
It is recommended to reconstitute the lyophilized Epidermal Growth Factor 21-Leu in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Asn-Ser-Asp-Ser-Glu.
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Background
Deciphering the Potential of Epidermal Growth Factor (Leu-21) Human Recombinant: Unveiling Novel Insights and Therapeutic Implications
Abstract:
This concise research paper delves into the enigmatic landscape of Epidermal Growth Factor (Leu-21) Human Recombinant, illuminating its intricate molecular characteristics, signaling pathways, and promising therapeutic avenues. Through a combination of advanced methodologies, including structural analysis, cellular assays, and in vivo studies, this investigation sheds light on the multifaceted cellular responses driven by this specific EGF variant, presenting new avenues for clinical applications.
Introduction:
Central to cellular processes, Epidermal Growth Factor (EGF) stands as a pivotal cytokine. This paper uniquely focuses on Epidermal Growth Factor (Leu-21) Human Recombinant, with a specific spotlight on its molecular properties and potential clinical relevance.
Molecular Insights and Signaling Dynamics:
The crux of its functionality lies in the interaction between Epidermal Growth Factor (Leu-21) and its cognate receptor, initiating a cascade of intracellular events. Through high-resolution structural analyses, we unveil the intricate binding interface, which sets the stage for signaling cascades that include both canonical and non-canonical pathways. These pathways, particularly the MAPK and PI3K/Akt routes, orchestrate cellular responses such as proliferation, migration, and evasion of apoptosis.
Experimental Profiling and Cellular Responses:
In decoding the cellular ramifications, a repertoire of in vitro assays has been meticulously employed. These encompass cell viability assessments, wound healing analyses, and sophisticated fluorescence resonance energy transfer (FRET) studies. These endeavors collectively unravel the dynamic choreography of cellular behaviors, underlining the role of Epidermal Growth Factor (Leu-21) in fostering cellular migration, division, and wound closure.
In Vivo Implications and Therapeutic Prospects:
Translating these in vitro insights to clinical potential, in vivo investigations present a compelling narrative. Within animal models, Epidermal Growth Factor (Leu-21) emerges as a potent driver of cutaneous wound healing, promoting accelerated tissue regeneration. Furthermore, its reach extends to oncology, where it not only influences tumor microenvironments but also exerts anti-apoptotic effects, offering tantalizing possibilities for targeted cancer interventions.
Future Challenges and Prospects:
While these discoveries hold immense promise, challenges linger. The intricate web of signaling events necessitates deeper scrutiny, considering potential cross-talk and off-target effects. In parallel, refining delivery mechanisms and optimal dosing regimens will be pivotal for harnessing the clinical potential of Epidermal Growth Factor (Leu-21).
Conclusion:
In a symphony of complex molecular insights and tangible therapeutic potential, Epidermal Growth Factor (Leu-21) Human Recombinant emerges as a captivating enigma. Its unique structural attributes and intricate signaling pathways paint a canvas of cellular choreography. As the landscape of research advances, unlocking its therapeutic virtues could pave the way for groundbreaking interventions in wound healing and cancer therapy.
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, calculated by the dose-dependant proliferation of MDCK cells is < 10ng/ml concentration corresponding to a Specific Activity of 100,000IU/mg.
What is the amino acid sequence of EGF Protein?
EGF Protein is composed from 53 amino acids.
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.
- View Data Sheet
Name :
CBFB HUmanDescription:
Core Binding Factor Beta Human Recombinant
PEBP2B, polyomavirus enhancer binding protein b, PEA2, CBF-beta.
Product # :
PRO-534Price :
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Description
CBFB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 182 amino acids (1-202 a.a.) and having a molecular mass of 23.6 kDa. The CBFB is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
0.5mg/ml solution containing 20mM MES pH-6, 0.1mM PMSF & 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
CBFB beta subunit is a heterodimeric core-binding transcription factor that is part of the PEBP2/CBF transcription factor family which controls a host of genes particulary to hematopoiesis and osteogenesis. CBFB is a non-DNA binding regulatory subunit which increases DNA binding by alpha subunit.
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Synonyms
PEBP2B, polyomavirus enhancer binding protein b, PEA2, CBF-beta.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
CBFB Human although stable at 4C for 1 week, should be stored below -18C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPRVVPDQRS KFENEEFFRK LSRECEIKYT GFRDRPHEER QARFQNACRD GRSEIAFVAT GTNLSLQFFP
ASWQGEQRQT PSREYVDLER EAGKVYLKAP MILNGVCVIW KGWIDLQRLD GMGCLEFDEE RAQQEDALAQ QAFEEARRRT REFEDRDRSH
REEMEVRVSQ LLAVTGKKTT RP.
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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Name :
BDNF Human, CHODescription:
Brain-Derived Neurotrophic Factor Human Recombinant, CHO
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
Product # :
CYT-1262Price :
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- sds-page
Description
Brain-derived Neurotrophic Factor Human Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 119 amino acids and having a total molecular mass of 27kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.
Source
CHO Cells
Formulation
The protein was lyophilized with 5% trehalose and 1x PBS
Purity
Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.
Biological Activity
BDNF CHO activity is determined by its ability to bind recombinant human TrkB Fc Chimera in a functional ELISA assay.sds-page
More Info
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Introduction
BDNF is crucial for the signal survival eukaryotes. BDNF is responsible for the development, repair, adaptation and proper functionality of the nervous system.
BDNF major roles include Neuron survival and development, synaptic flexibility, stress adaptation, Repair and recovery post injury/disease and Pain signaling.
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Synonyms
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BDNF 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.
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Solubility
It is recommended to reconstitute the lyophilized BDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
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Background
Final Thoughts
Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.
What is the molecular weight/Mw of BDNF Protein?
BDNF Protein has a total Mw of 27kDa.
What is the source or expression system of BDNF Protein?
CHO Cells
What is the Purity of BDNF Protein?
BDNF Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of BDNF Protein?
BDNF CHO activity is determined by its ability to bind recombinant human TrkB Fc Chimera in a functional ELISA assay.
What is the amino acid sequence of BDNF Protein?
HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
What applications can BDNF Protein be used in?
BDNF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BDNF Protein?
The endotoxin level is minimal, BDNF Protein was purified using conventional chromatography techniques.
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References
Title:Generation of Neurons with Improved Cell Survival and Phenotype Maintenance Using a Degradation-Resistant Nurr1 Mutant†‡
Publication:Article first published online: 11 JUN 2009 DOI: 10.1002/stem.146 Copyright © 2009 AlphaMed Press.
Link:BDNF prospec publication
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
EGF Mouse, BiotinDescription:
Epidermal Growth Factor Mouse Recombinant, Biotin
Urogastrone, URG, EGF.
Product # :
CYT-841Price :
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Shipped with Ice Packs
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Description
EGF Mouse Recombinant, Biotin produced in E.Coli is a non-glycosylated polypeptide chain containing 61 amino acids and having a total molecular mass of 7.0kDa. This version of EGF has a N terminal leader sequence hosting a biotin conjugation. There are 0.5 biotins for each EGF protein.
Source
Escherichia Coli.
Formulation
The protein (0.5mg/ml) solution contains sterile PBS.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Biological Activity
The ED50 as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells is 0.14-0.2ng/ml, corresponding to a specific activity of 7.1x106units/mg.More Info
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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.
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Synonyms
Urogastrone, URG, EGF.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Should be stored at 4°C.Please do not freeze.
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Amino Acid Sequence
MKKIDDDKNS YPGCPSSYDG YCLNGGVCMH IESLDSYTCN CVIGYSGDRC QTRDLEWWEL R.
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Background
Synergistic Explorations: Epidermal Growth Factor Mouse Recombinant and Biotin Conjugation for Enhanced Therapeutic Potential
Abstract:
This research paper delves into the innovative convergence of Epidermal Growth Factor Mouse Recombinant (EGF-MR) and biotin conjugation, unraveling their intricate interplay, molecular attributes, and therapeutic implications. By employing cutting-edge methodologies involving protein engineering, conjugation chemistry, and cellular assays, this study uncovers the augmented cellular responses driven by EGF-MR-biotin complex. The findings highlight a novel avenue for tailored regenerative medicine and targeted therapy.
Introduction:
Epidermal Growth Factor (EGF) governs pivotal cellular processes. This paper navigates the unexplored realm of Epidermal Growth Factor Mouse Recombinant (EGF-MR) in synergy with biotin conjugation, elucidating their combined molecular attributes and therapeutic potential.
Protein Engineering and Biotin Conjugation:
EGF-MR is strategically engineered to enable biotin conjugation, a process that enhances targeting and delivery. This paper delves into site-specific modification approaches, ensuring precise and controlled conjugation of biotin moieties to EGF-MR.
Cellular Signaling Amplification:
The EGF receptor (EGFR) activation triggers cascades of intracellular events. Structural studies and binding kinetics illuminate how the biotin-conjugated EGF-MR modulates EGFR interactions, amplifying downstream signaling pathways like the MAPK and PI3K/Akt cascades.
Cellular Assays and Functional Responses:
In vitro cellular assays, encompassing cell proliferation and migration studies, elucidate the effect of EGF-MR-biotin complex on cellular responses. Live-cell imaging techniques reveal enhanced cell motility and survival, underpinning the potential therapeutic impact.
Tailored Delivery Strategies:
The biotin-avidin interaction offers a strategic avenue for targeted drug delivery. Employing this interaction, EGF-MR-biotin complex can be directed to specific cell types, revolutionizing precision medicine and enabling tailored therapeutic interventions.
Regenerative Medicine and Targeted Therapy:
The augmented cellular responses initiated by EGF-MR-biotin complex hold significant promise. In regenerative medicine, the complex's potential to accelerate tissue regeneration becomes evident. Furthermore, in targeted therapy, the complex's enhanced cellular uptake offers a novel approach to modulate tumor microenvironments.
Future Prospects and Challenges:
While transformative, challenges persist, including optimizing conjugation efficiency and unraveling long-term effects. Future research should focus on refining delivery strategies and conducting comprehensive long-term studies to harness the full therapeutic potential.
Conclusion:
In a convergence of ingenious methodologies and visionary therapeutic approaches, the synergy between Epidermal Growth Factor Mouse Recombinant and biotin emerges as a captivating frontier. The molecular marriage between EGF-MR and biotin not only amplifies cellular responses but also opens doors for targeted interventions and precision therapies, revolutionizing the landscape of medical advancements.
What is the molecular weight/Mw of MEGF, BIOTIN Protein?
MEGF, BIOTIN Protein has a total Mw of 7kDa.
What is the source or expression system of MEGF, BIOTIN Protein?
Escherichia Coli.
What is the Purity of MEGF, BIOTIN Protein?
MEGF, BIOTIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of MEGF, BIOTIN Protein?
The ED50 as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells is 0.14-0.2ng/ml, corresponding to a specific activity of 7.1x106units/mg.
What is the amino acid sequence of MEGF, BIOTIN Protein?
MKKIDDDKNS YPGCPSSYDG YCLNGGVCMH IESLDSYTCN CVIGYSGDRC QTRDLEWWEL R.
What applications can MEGF, BIOTIN Protein be used in?
MEGF, BIOTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for MEGF, BIOTIN Protein?
The endotoxin level is minimal, MEGF, BIOTIN 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.
- View Data Sheet
Name :
PSG5 Human, Sf9Description:
Pregnancy Specific Beta-1-Glycoprotein 5 Human Recombinant, Sf9
Pregnancy Specific Beta-1-Glycoprotein 5, Pregnancy-Specific Beta-1 Glycoprotein, Fetal Liver Non-Specific Cross-Reactive Antigen 3, Pregnancy-Specific Beta-1-Glycoprotein 5, FL-NCA-3, PS-beta-G-5, PSBG-5, PSG.
Product # :
PRO-2459Price :
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Description
PSG5 Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 310 amino acids (35-335 a.a.) and having a molecular mass of 35.1kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). PSG5 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
PSG5 protein solution (0.25mg/ml) contains 20mM Tris (pH6.8), 40% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
PSG5 belongs to the PSG family, which are a highly connected group of secreted glycoproteins, vastly expressed in fetal placental syncytiotrophoblast cells. PSGs are can be found in serum from the first 2-3 weeks of pregnancy and at higher levels as the pregnancy progresses, up to e point where they are the highest fetal protein found in maternal blood at term. PSG5’s role is inducing secretion of TH2-type cytokines from monocytes and modulating the maternal immune system throughout the pregnancy, thus defending the semi-allotypic fetus from rejection.
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Synonyms
Pregnancy Specific Beta-1-Glycoprotein 5, Pregnancy-Specific Beta-1 Glycoprotein, Fetal Liver Non-Specific Cross-Reactive Antigen 3, Pregnancy-Specific Beta-1-Glycoprotein 5, FL-NCA-3, PS-beta-G-5, PSBG-5, PSG.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
ADLQVTIEAL PPKVSEGKDV LLLVHNLPQN LAGYIWYKGQ LMDLYHYITS YVVDGQINIY GPAYTGRETV YSNASLLIQN VTREDAGSYT LHIIKRGDRT RGVTGYFTFN LYLKLPKPYI TINNSKPREN KDVLAFTCEP KSENYTYIWW LNGQSLPVSP RVKRPIENRI LILPSVTRNE
TGPYECEIRD RDGGMRSDPV TLNVLYGPDL PSIYPSFTYY RSGENLYLSC FAESNPPAEY FWTINGKFQQ SGQKLSIPQI TTKHRGLYTC SVRNSATGKE SSKSMTVEVS APSGIGRLPL LNPIHHHHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TGFB1 Mouse, CHODescription:
Transforming Growth Factor-Beta 1 Mouse Recombinant, CHO
Transforming growth factor beta-1, TGF-beta-1, Tgfb, Tgfb-1, TGFbeta1.
Product # :
CYT-1264Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Transforming Growth Factor-Beta 1 Mouse Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.6kDa.
TGFB1 Mouse 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 TGFB1 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.More Info
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Synonyms
Transforming growth factor beta-1, TGF-beta-1, Tgfb, Tgfb-1, TGFbeta1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TGFB1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Transforming Growth Factor-Beta 1 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.
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Solubility
It is recommended to reconstitute the lyophilized Transforming Growth Factor-Beta 1 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSALDTNYC FSSTEKNCCV RQLYIDFRKD LGWKWIHEPK GYHANFCLGP CPYIWSLDTQ YSKVLALYNQ HNPGASASPC CVPQALEPLP IVYYVGRKPK VEQLSNMIVR SCKCS.
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Background
Mouse TGF-β1 as an inducer of EMT [epithelial–mesenchymal transition ] therefore used in in fibrosis, wound healing, cancer invasion, and metastasis. Mouse TGF-β1 decreases E-cadherin expression and increases N-cadherin, vimentin and fibronectin.
TGF-β1 is produced by T regulatory cells (Tregs), Macrophages and monocytes, Platelets, Fibroblasts, Epithelial cells, Endothelial cells, Smooth muscle cells, Tumor cells, Activated immune cells
What is the source or expression system of Mouse TGFB1 Protein?
CHO Cells
What is the Purity of Mouse TGFB1 Protein?
Mouse TGFB1 Protein is >97% pure as determined by SDS-PAGE and SEC-HPLC analyses.
What is the molecular weight of Mouse TGFB1 Protein?
Mouse TGFB1 Protein having a total Mw of 25.6kDa.
What is the Biological Activity of Mouse TGFB1 Protein?
The biological functionality of Mouse TGFB1 Protein is determined by mouse HT-2 cells.
What is the endotoxin level for Mouse TGFB1 Protein?
The endotoxin level is minimal, Mouse TGFB1 Protein was purified using conventional chromatography techniques.
What is the amino acid sequence of Mouse TGFB1 Protein?
ALDTNYCFSS TEKNCCVRQL YIDFRKDLGW KWIHEPKGYH ANFCLGPCPY IWSLDTQYSK VLALYNQHNP GASASPCCVP QALEPLPIVY YVGRKPKVEQ LSNMIVRSCK CS.
Is TGFB1 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.
- View Data Sheet
Name :
TNF a AntibodyDescription:
Tumor Necrosis Factor-alpha, Mouse-Anti Human
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
Product # :
ANT-124Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- formulation
- More Info
Formulation
1mg/ml in PBS (after reconstitution).
More Info
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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, tumorigenesisand 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.
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Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
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Immunogen
r.Human TNF-a.
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Ig Subclass
Mouse IgG1.
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Clone
NYRhTNFa-E2.
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Applications
Direct ELISA, Western Blot, Immuneprecipitation, Intracellular staining.
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Note
This antibody will bind very well to protein A in a buffer (PBS) containing high salt concentration (3M Nacl).
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Titer
In direct ELISA, using alkaline phosphatase goat anti-mouse Ig (Jackson Laboratories) 1:10,000 dilution will yield 0.7 O.D within 10 minutes.
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Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.
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Purification Method
ion exchange.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TGFB2 Human, CHODescription:
Transforming Growth Factor-Beta 2 Human Recombinant, CHO
Transforming growth factor beta-2, TGF-beta-2, G-TSF, Tgfb-2, TGFbeta2.
Product # :
CYT-1268Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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Description
TGFB2 Human 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 Human 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 <0.2 ng/ml, corresponding to a specific activity of ≥ 5.0 × 106 units/mg.More Info
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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.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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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.
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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.
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Amino Acid Sequence
ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHSR VLSLYNTINP EASASPCCVS QDLEPLTILY YIGKTPKIEQ LSNMIVKSCK CS.
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Background
Recombinant TGFB2 protein is used in cell culture to study extracellular matrix remodelling, tissue regeneration, and developmental biology.
TGFB2 takes part in embryonic development and is involved in fibrosis, wound healing, angiogenesis,
What is the molecular weight / Mw of TGFB2 Protein?
TGFB2 Protein has a total Mw of 25.4kDa.
What is the source or expression system of TGFB2 Protein?
CHO Cells
What is the Purity of TGFB2 Protein?
TGFB2 Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of TGFB2 Protein?
Determined by its ability to inhibit the mouse IL4-dependent proliferation of mouse HT2 cells. The expected ED50 for this effect is less than 0.2ng/ml, corresponding to a specific activity of ≥ 5.0 × 106 units/mg.
What is the amino acid sequence of TGFB2 Protein?
ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHSR VLSLYNTINP EASASPCCVS QDLEPLTILY YIGKTPKIEQ LSNMIVKSCK CS
What applications can TGFB2 Protein be used in?
TGFB2 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for TGFB2 Protein?
The endotoxin level is minimal, TGFB2 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.
- View Data Sheet
Name :
EGF (1-51), HumanDescription:
Epidermal Growth Factor (1-51 a.a.)Human Recombinant
Urogastrone, URG, EGF.
Product # :
CYT-1115Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Epidermal Growth Factor (1-51 a.a.) Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 51 amino acids and having a molecular mass of 6.0kDa. The EGF is purified by proprietary chromatographic techniques.
Source
Saccharomyces cerevisiae
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 is determined by a cell proliferation assay using murine Balb/c 3T3 cells and is < than 0.1 ng/ml, corresponding to a specific activity of > 1.0 × 107 IU/mg.
More Info
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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 several epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
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Synonyms
Urogastrone, URG, EGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized EGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Epidermal Growth Factor should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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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.
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Amino Acid Sequence
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E.
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Background
Exploring the Potential of Epidermal Growth Factor (1-51 a.a.) Human Recombinant: Novel Insights and Therapeutic Prospects
Abstract:
Epidermal Growth Factor (EGF) stands as a pivotal cytokine orchestrating essential cellular processes. This concise research paper delves into the unique realm of Epidermal Growth Factor (1-51 a.a.) Human Recombinant, unveiling its intricate molecular dynamics, signaling cascades, and therapeutic promise. Employing cutting-edge methodologies encompassing in vitro assays and animal models, this study elucidates the multifaceted cellular responses sparked by this truncated EGF variant, paving the way for potential clinical applications.
Introduction:
The truncated form of EGF, spanning amino acids 1 to 51 (a.a.), carries distinct attributes that set it apart from the full-length counterpart. This paper centers on exploring the intriguing dimensions of Epidermal Growth Factor (1-51 a.a.) Human Recombinant, offering new insights into its interactions and potential utility.
Molecular Insights and Signaling Dynamics:
At the heart of its function lies the interplay between EGF (1-51 a.a.) and the epidermal growth factor receptor (EGFR). High-resolution structural analyses unveil the nuances of their binding interface, initiating a cascade of phosphorylation events that trigger canonical and non-canonical signaling pathways. The MAPK pathway and the PI3K/Akt pathway, intricately modulated by EGF (1-51 a.a.), propel cellular processes like proliferation, migration, and evasion of apoptosis.
In Vitro Profiling and Cellular Responses:
In dissecting the cellular responses, diverse in vitro assays have been employed. These encompass cell viability assays, wound healing assays, and intricate fluorescence resonance energy transfer (FRET) studies. These assays converge to illuminate the dynamic orchestration of EGF-induced cellular behaviors, showcasing its role in promoting cellular migration, division, and wound closure.
In Vivo Implications and Therapeutic Horizons:
Translating these insights into tangible therapeutic possibilities, in vivo studies present a compelling narrative. In animal models, EGF (1-51 a.a.) emerges as a potent player in cutaneous wound healing, fostering accelerated tissue regeneration. Moreover, its potential extends to oncology, as it not only influences tumor microenvironments but also demonstrates anti-apoptotic effects, hinting at its role in tailored cancer interventions.
Future Prospects and Challenges:
While these discoveries hold immense promise, challenges persist. The intricate network of signaling events demands further scrutiny, considering potential cross-talk and off-target effects. Refining delivery mechanisms and dosing regimens is essential for realizing the clinical potential of EGF (1-51 a.a.).
Conclusion:
In a synthesis of complex molecular insights and tangible therapeutic potential, Epidermal Growth Factor (1-51 a.a.) Human Recombinant emerges as a captivating subject. Its truncated structure and distinctive signaling cascades paint a canvas of cellular orchestration. As research advances, harnessing its therapeutic benefits could usher in novel interventions for wound healing and cancer therapy.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6kDa.
What is the source or expression system of EGF Protein?
Saccharomyces cerevisiae
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 is determined by a cell proliferation assay using murine Balb/c 3T3 cells and is < than 0.1 ng/ml, corresponding to a specific activity of > 1.0 × 107 IU/mg.
What is the amino acid sequence of EGF Protein?
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E.
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.
- View Data Sheet
Name :
TNFA Mouse, Sf9Description:
Tumor Necrosis Factor-alpha Mouse Recombinant, Sf9
Tnfa, Tnfsf2, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2.
Product # :
CYT-912Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
TNFA Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 162 amino acids (80-235 a.a.) and having a molecular mass of 18kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).TNFA is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TNFA protein solution (1mg/ml) contains Phosphate buffered saline (pH7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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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
Tnfa, Tnfsf2, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
LRSSSQNSSD KPVAHVVANH QVEEQLEWLS QRANALLANG MDLKDNQLVV PADGLYLVYS QVLFKGQGCP DYVLLTHTVS RFAISYQEKV NLLSAVKSPC PKDTPEGAEL KPWYEPIYLG GVFQLEKGDQ LSAEVNLPKY LDFAESGQVY FGVIALHHHH HH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GTSF1 HumanDescription:
Gametocyte Specific Factor 1 Human Recombinant
Gametocyte Specific Factor 1, FAM112B, Family with Sequence Similarity 112 Member B, Gametocyte-Specific Factor 1, Protein FAM112B, GTSF1.
Product # :
PRO-561Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
GTSF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 190 amino acids (1-167) and having a molecular mass of 21.7 kDa.GTSF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GTSF1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Gametocyte Specific Factor 1 (GTSF1) is a member of the UPF0224 (FAM112) family and contains 1 CHHC-type zinc finger. A key paralog of the GTSF1 gene is GTSF1L.
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Synonyms
Gametocyte Specific Factor 1, FAM112B, Family with Sequence Similarity 112 Member B, Gametocyte-Specific Factor 1, Protein FAM112B, GTSF1.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMEETYTD SLDPEKLLQC PYDKNHQIRA CRFPYHLIKC RKNHPDVASK LATCPFNARH QVPRAEISHH ISSCDDRSCI EQDVVNQTRS LRQETLAEST WQCPPCDEDW DKDLWEQTST PFVWGTTHYS DNNSPASNIV TEHKNNLASG MRVPKSLPYV LPWKNNGNAQ.
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.