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1000 results found for “stem cell factor”
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Name :
FGFR1 Human, (22-285)Description:
Fibroblast Growth Factor Receptor-1 Human Recombinant, (22-285 a.a.)
FGFR-1, bFGF-R, C-FGR, CD331, fms-related tyrosine kinase 2, Pfeiffer syndrome, CEK, FLG, FLT2, KAL2, BFGFR, FGFBR, HBGFR, FGFR1/FGFR1OP2 FUSION GENE, FGFR1/ZNF198 FUSION GENE, FLG FGFR1/BCR FUSION GENE, FLG protein, FMS-LIKE GENE, N-sam tyrosine kinase, basic fibroblast growth factor receptor 1.
Product # :
PKA-114Price :
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Shipped with Ice Packs
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Description
FGFR1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 272 amino acids (22-285) and having a molecular mass of 30.4kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). FGFR1 is fused to a 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The FGFR1 solution (0.25mg/1ml) contains phosphate buffered Saline (pH7.4), and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Fibroblast Growth Factors (FGFs) comprise a family of at least 18 structurally related proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentiation, angiogenesis, wound healing and tumorigenesis. The biological activities of the FGFs are mediated by a family of type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Multiple forms of FGFR-1 to -3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to as the ? isoform. Only the alpha isoform has been identified for FGFR-3 and FGFR-4. Additional splicing events for FGFR-1 to -3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). An IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGFR-1. Mutations in FGFR-1 to -3 have been found in patients with birth defects involving craniosynostosis.
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Synonyms
FGFR-1, bFGF-R, C-FGR, CD331, fms-related tyrosine kinase 2, Pfeiffer syndrome, CEK, FLG, FLT2, KAL2, BFGFR, FGFBR, HBGFR, FGFR1/FGFR1OP2 FUSION GENE, FGFR1/ZNF198 FUSION GENE, FLG FGFR1/BCR FUSION GENE, FLG protein, FMS-LIKE GENE, N-sam tyrosine kinase, basic fibroblast growth factor receptor 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
RPSPTLPEQD ALPSSEDDDD DDDSSSEEKE TDNTKPNPVA PYWTSPEKME KKLHAVPAAK TVKFKCPSSG TPNPTLRWLK NGKEFKPDHRIGGYKVRYAT WSIIMDSVVP SDKGNYTCIV ENEYGSINHT YQLDVVERSP HRPILQAGLP ANKTVALGSN VEFMCKVYSD PQPHIQWLKH IEVNGSKIGP DNLPYVQILK TAGVNTTDKE MEVLHLRNVS FEDAGEYTCL AGNSIGLSHH SAWLTVLEAL EERPAVMTSP LYLELEHHHH 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 4 MouseDescription:
Interleukin-4 Mouse Recombinant
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
Product # :
CYT-282Price :
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Shipped at Room temp
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Description
Interleukin-4 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 120 amino acids and having a molecular mass of 13500 Dalton. The IL-4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm 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 as determined by the dose-dependant induction of HT-2 cell proliferation is less than 2 ng/ml corresponding to a Specific Activity of 500,000IU/mg.More Info
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Introduction
Interleukin-4 is a pleiotropic cytokine produced primarily by activated T lymphocytes, basophils and mast cells. Multiple immune response-modulating functions are performed by IL-4 on a variety of cell types and it has an important role in the regulator of isotype switching, induction of IgE production in B lymphocytes and differentiation of precursor T helper cells. IL-4 binds to both membrane-bound and secreted soluble IL-4 receptors.
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Synonyms
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL4 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 Interleukin 4 in sterile 10mM HAc not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MHIHGCDKNH LREIIGILNE VTGEGTPCTE MDVPNVLTAT KNTTESELVC RASKVLRIFY LKHGKTPCLK KNSSVLMELQ RLFRAFRCLD SSISCTMNES KSTSLKDFLE SLKSIMQMDY S.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ST3GAL5 HumanDescription:
ST3 Beta-Galactoside Alpha-2,3-Sialyltransferase 5 Human Recombinant
ST3 Beta-Galactoside Alpha-2,3-Sialyltransferase 5, SIAT9, Sialyltransferase 9 (CMP-NeuAc:Lactosylceramide Alpha-2,3-Sialyltransferase; GM3 Synthase), Ganglioside GM3 Synthase, ST3GalV, CMP-NeuAc:Lactosylceramide Alpha-2,3-Sialyltransferase, ST3Gal V, EC 2.4.99.9, SATI, SIATGM3S, Alpha 2,3-Sialyltransferase V, Lactosylceramide Alpha-2,3-Sialyltransferase, Sialyltransferase 9, ST3GALV, GM3 Synthase.
Product # :
ENZ-755Price :
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Description
ST3GAL5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 359 amino acids (83-418a.a) and having a molecular mass of 41kDa. ST3GAL5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ST3GAL5 protein solution (1mg/ml) containing In 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
ST3 Beta-Galactoside Alpha-2,3-Sialyltransferase 5, also know as ST3GAL5 belongs to the glycosyltransferase family 29 and localized to the Golgi apparatus. ST3GAL5 is known to play a part in the induction of cell differentiation, modulation of cell proliferation, maintenance of fibroblast morphology, signal transduction, and integrin-mediated cell adhesion. ST3GAL5 is a type II membrane protein which catalyzes the formation of GM3 with lactosylceramide as the substrate. Mutation in this ST3GAL5 has been connected with Amish infantile epilepsy syndrome. Transcript variants encoding various isoforms have been found for this gene.
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Synonyms
ST3 Beta-Galactoside Alpha-2,3-Sialyltransferase 5, SIAT9, Sialyltransferase 9 (CMP-NeuAc:Lactosylceramide Alpha-2,3-Sialyltransferase; GM3 Synthase), Ganglioside GM3 Synthase, ST3GalV, CMP-NeuAc:Lactosylceramide Alpha-2,3-Sialyltransferase, ST3Gal V, EC 2.4.99.9, SATI, SIATGM3S, Alpha 2,3-Sialyltransferase V, Lactosylceramide Alpha-2,3-Sialyltransferase, Sialyltransferase 9, ST3GALV, GM3 Synthase.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSLKLNYTT EECDMKKMHY VDPDHVKRAQ KYAQQVLQKE CRPKFAKTSM ALLFEHRYSV DLLPFVQKAP KDSEAESKYD PPFGFRKFSS KVQTLLELLP EHDLPEHLKA KTCRRCVVIG SGGILHGLEL GHTLNQFDVV IRLNSAPVEG YSEHVGNKTT IRMTYPEGAP LSDLEYYSND LFVAVLFKSV DFNWLQAMVK KETLPFWVRL FFWKQVAEKI PLQPKHFRIL NPVIIKETAF DILQYSEPQS RFWGRDKNVP TIGVIAVVLA THLCDEVSLA GFGYDLNQPR TPLHYFDSQC MAAMNFQTMH NVTTETKFLL KLVKEGVVKD LSGGIDREF
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 :
STAC HumanDescription:
SH3 And Cysteine Rich Domain Human Recombinant
SH3 and cysteine rich domain, STAC, STAC1, SH3 and cysteine-rich domain-containing protein, Src homology 3 and cysteine-rich domain-containing protein.
Product # :
PRO-2010Price :
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Description
STAC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 425 amino acids (1-402 a.a.) and having a molecular mass of 46.9kDa.STAC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
STAC protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
SH3 and Cysteine Rich Domain, which is also known as STAC, holds one phorbol-ester/DAG-type zinc finger and one SH3 domain. STAC takes part in a neuron-specific signal transduction.
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Synonyms
SH3 and cysteine rich domain, STAC, STAC1, SH3 and cysteine-rich domain-containing protein, Src homology 3 and cysteine-rich domain-containing protein.
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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
MGSSHHHHHH SSGLVPRGSH MGSMIPPSSP REDGVDGLPK EAVGAEQPPS PASTSSQESK LQKLKRSLSF KTKSLRSKSA DNFFQRTNSE DMKLQAHMVA EISPSSSPLP APGSLTSTPA RAGLHPGGKA HAFQEYIFKK PTFCDVCNHM IVGTNAKHGL RCKACKMSIH HKCTDGLAPQ RCMGKLPKGF RRYYSSPLLI HEQFGCIKEV MPIACGNKVD PVYETLRFGT SLAQRTKKGS SGSGSDSPHR TSTSDLVEVP EEANGPGGGY DLRKRSNSVF TYPENGTDDF RDPAKNINHQ GSLSKDPLQM NTYVALYKFV PQENEDLEMR PGDIITLLED SNEDWWKGKI QDRIGFFPAN FVQRLQQNEK IFRCVRTFIG CKEQGQITLK ENQICVSSEE EQDGFIRVLS GKKKGLIPLD VLENI.
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 :
C17ORF103 HumanDescription:
Chromosome 17 Open Reading Frame 103 Human Recombinant
Chromosome 17 Open Reading Frame 103, Transcript Expressed During Hematopoiesis 2, Gene Trap Locus F3b, Gtlf3b, Protein GTLF3B.
Product # :
PRO-1619Price :
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Description
C17ORF103 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 136 amino acids (1-113) and having a molecular mass of 15.4kDa.C17ORF103 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The C17ORF103 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
C17orf103 is a member of the GTLF3B family and is encoded by a gene which is located in human chromosome 17p11.2. BRCA1 and p53 are 2 main tumor suppressor genes which are linked to chromosome 17. Tumor suppressor p53 is necessary for maintenance of cellular genetic integrity by moderating cell fate through DNA repair versus cell death. C17orf103 is also related to neurofibromatosis, a disorder characterized by neural and epidermal lesions, and dysregulated Schwann cell growth.
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Synonyms
Chromosome 17 Open Reading Frame 103, Transcript Expressed During Hematopoiesis 2, Gene Trap Locus F3b, Gtlf3b, Protein GTLF3B.
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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
MGSSHHHHHH SSGLVPRGSH MGSMAHSAAA VPLGALEQGC PIRVEHDRRR RQFTVRLNGC HDRAVLLYEY VGKRIVDLQH TEVPDAYRGR GIAKHLAKAA LDFVVEEDLK AHLTCWYIQK YVKENPLPQY LERLQP
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 32A HumanDescription:
Interleukin-32 alpha Human Recombinant
NK4, TAIF, TAIFa, TAIFb, TAIFc, TAIFd, IL-32beta, IL-32alpha, IL-32delta, IL-32gamma, Interleukin-32, IL-32, Natural killer cells protein 4, Tumor necrosis factor alpha-inducing factor, IL-32a, IL32a, IL32, Interleukin-32 alpha.
Product # :
CYT-584Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-32 human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 131 amino acids and having a molecular mass of 14.9 kDa.
Source
Escherichia Coli.
Formulation
IL-32 was lyophilized from a concentrated (1mg/ml) solution in water containing 50mM sodium Phosphate buffer pH=7.5.
Purity
Greater than 97.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Human IL-32 alpha activity is measured via the dose-dependent induction of TNF-alpha in the human THP-1 monocytic cell line.More Info
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Introduction
IL-32 is part of the cytokine family and contains a tyrosine sulfation site, 3 potential N-myristoylation sites, multiple putative phosphorylation sites, and an RGD cell-attachment sequence. IL-32 expression is elevated after the activation of T-cells by mitogens or the activation of NK cells by IL-2. IL-32 induces the production of TNF-a from macrophage cells. IL-32 pro-inflammatory pathway is activated in response to influenza A virus infection. Dysregulation of IL-32 in myelodysplastic syndrome and chronic myelomonocytic leukemia modulates apoptosis and impairs NK function.
Induction of TNF, IL-1beta, and IL-6 by IL-32 is intervened by p38-MAPK. IL-32 induced monocyte-to-macrophage differentiation is mediated through nonapoptotic, caspase-3-dependent mechanisms. IL32 plays an important role in the pathogenesis of rheumatoid arthritis. IL-32 is involved in activation-induced cell death in T cells, through its intracellular actions. IL-32 is a cell-associated proinflammatory cytokine, which is particularly stimulated by mycobacteria through a caspase-1- and IL-18-dependent production of IFNgamma.
IL-32 is associated with TNF-a, IL-1beta, and IL-18. IL32 is involved in human rheumatoid arthritis and is a novel target in autoimmune diseases. -
Synonyms
NK4, TAIF, TAIFa, TAIFb, TAIFc, TAIFd, IL-32beta, IL-32alpha, IL-32delta, IL-32gamma, Interleukin-32, IL-32, Natural killer cells protein 4, Tumor necrosis factor alpha-inducing factor, IL-32a, IL32a, IL32, Interleukin-32 alpha.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IL32 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL32 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 IL-32 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
MCFPKVLSDD MKKLKARMHQ AIERFYDKMQ NAESGRGQVM SSLAELEDDF KEGYLETVAA YYEEQHPELT PLLEKERDGL RCRGNRSPVP DVEDPATEEP GESFCDKSYG APRGDKEELT PQKCSEPQSS K.
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 :
OSM Human, 195 a.aDescription:
Oncostatin-M Human Recombinant (195 a.a.)
OSM, MGC20461, Oncostatin M.
Product # :
CYT-735Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Oncostatin-M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 195 amino acids and having a molecular mass of 22kDa. The OSM is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing 1xPBS pH-7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependent stimulation of the proliferation of human TF-1 cells is < 0.2ng/ml, corresponding to a specific activity of > 5.0x106 units/mg.More Info
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Introduction
Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.
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Synonyms
OSM, MGC20461, Oncostatin M.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Oncostatin M although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Oncostatin 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 Oncostatin M 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
AAIGSCSKEY RVLLGQLQKQ TDLMQDTSRL LDPYIRIQGL DVPKLREHCR ERPGAFPSEE TLRGLGRRGF LQTLNATLGC VLHRLADLEQ RLPKAQDLER SGLNIEDLEK LQMARPNILG LRNNIYCMAQ LLDNSDTAEP TKAGRGASQP PTPTPASDAF QRKLEGCRFL HGYHRFMHSV GRVFSKWGES PNRSR.
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 :
LGALS3 MouseDescription:
Galectin-3 Mouse Recombinant
CBP35, GAL3, GALBP, GALIG, LGALS2, MAC2, Galectin-3, Lectin, galactose binding, soluble 3, Lectin, galactose binding, soluble 3, isoform CRA_a, Lectin, galactose binding, soluble 3, isoform CRA_d, Lgals3.
Product # :
CYT-188Price :
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- sds-page
Description
LGALS3 Mouse Recombinant produced in E. coli is a single polypeptide chain containing 287 amino acids (1-264) and having a molecular mass of 29.8 kDa. LGALS3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The LGALS3 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol, 1mM DTT and 2mM EDTA.
Purity
Greater than 95% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Galectin-3 mediates with the alpha-3, beta-1 integrin the stimulation by cspg4 of endothelial cells migration. Galectin-3 plays an necessary part during the acquisition of vasculogenic mimicry and angiogenic properties associated with melanoma progression. LGALS3 overexpression is highly expressed in early stages of papillary carcinoma, and its expression intensity declines during tumor progression. Serum levels of LGALS3 are high in patients with thyroid malignancy but there is considerable overlap in serum LGALS3 concentrations between those with benign and malignant nodular thyroid disease. LGLAS3 takes part as an immune regulator to inhibit T-cell immune responses and promote tumor growth, as a result providing a new mechanism for tumor immune tolerance.
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Synonyms
CBP35, GAL3, GALBP, GALIG, LGALS2, MAC2, Galectin-3, Lectin, galactose binding, soluble 3, Lectin, galactose binding, soluble 3, isoform CRA_a, Lectin, galactose binding, soluble 3, isoform CRA_d, Lgals3.
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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
MGSSHHHHHH SSGLVPRGSH MGSMADSFSL NDALAGSGNP NPQGYPGAWG NQPGAGGYPG AAYPGAYPGQ APPGAYPGQA PPGAYPGQAP PSAYPGPTAP GAYPGPTAPG AYPGSTAPGA FPGQPGAPGA YPSAPGGYPA AGPYGVPAGP LTVPYDLPLP GGVMPRMLIT IMGTVKPNAN RIVLDFRRGN DVAFHFNPRF NENNRRVIVC NTKQDNNWGK EERQSAFPFE SGKPFKIQVL VEADHFKVAV NDAHLLQYNH RMKNLREISQ LGISGDITLT SANHAMI.
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Background
What is the molecular weight/Mw of LGALS3 Protein?
LGALS3 Protein has a total Mw of 29.8kDa.
What is the source or expression system of LGALS3 Protein?
Escherichia Coli.
What is the Purity of LGALS3 Protein?
LGALS3 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS3 Protein?
The biological functionality of LGALS3 Protein will be determined in the future.
What is the amino acid sequence of LGALS3 Protein?
MGSSHHHHHH SSGLVPRGSH MGSMADSFSL NDALAGSGNP NPQGYPGAWG NQPGAGGYPG AAYPGAYPGQ APPGAYPGQA PPGAYPGQAP PSAYPGPTAP GAYPGPTAPG AYPGSTAPGA FPGQPGAPGA YPSAPGGYPA AGPYGVPAGP LTVPYDLPLP GGVMPRMLIT IMGTVKPNAN RIVLDFRRGN DVAFHFNPRF NENNRRVIVC NTKQDNNWGK EERQSAFPFE SGKPFKIQVL VEADHFKVAV NDAHLLQYNH RMKNLREISQ LGISGDITLT SANHAMI.
What applications can LGALS3 Protein be used in?
LGALS3 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS3 Protein?
The endotoxin level is minimal, LGALS3 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 :
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 16 MouseDescription:
Interleukin-16 Mouse Recombinant
LCF, Lymphocyte Chemoattractant Factor, prIL-16, KIAA4048, mKIAA4048, Il16, IL-16, Interleukin-16.
Product # :
CYT-559Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-16 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 127 amino acids and having a molecular mass of 13.2 kDa. The Mouse IL-16 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Murine IL-16 was lyophilized from 1mg/ml solution after extensive dialysis against 10mM sodium phosphate buffer, pH-7.5.
Purity
Greater than 90.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis SDS-PAGE.More Info
-
Introduction
IL-16 is a pleiotropic cytokine that functions as a chemoattractant, a modulator of T cell activation, and an inhibitor of HIV replication. The signaling process of IL-16 is mediated by CD4. The product of this gene undergoes proteolytic processing, which is found to yield two functional proteins. IL-16 functions exclusively attributed to the secreted C-terminal peptide, while the N-terminal product may play a role in cell cycle control. Caspase 3 is reported to be involved in the proteolytic processing of this protein. Two transcript variants encoding different isoforms have been found for this gene.
IL-16 stimulates a migratory response in cd4+ lymphocytes, monocytes, and eosinophils. Also induces t-lymphocyte expression of interleukin 2 receptor. ligand for cd4. -
Synonyms
LCF, Lymphocyte Chemoattractant Factor, prIL-16, KIAA4048, mKIAA4048, Il16, IL-16, Interleukin-16.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Mouse IL-16 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution mouse IL16 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 Murine IL16 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
MHDLNSSTDS AASASAASDI SVESKEATVC TVTLEKTSAG LGFSLEGGKG SLHGDKPLTI NRIFKGDRTG EMVQPGDEIL QLAGTAVQGL TRFEAWNVIK ALPDGPVTIV IRRTSLQCKQ TTASADS.
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 :
IL12 Human, Sf9Description:
Interleukin-12 Human Recombinant, Sf9
23-219aa (IL12A) / 23-328aa (IL12B), Interleukin 12 (subunit beta/alpha), IL12 His, NKSF1, NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.
Product # :
CYT-1111Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin 12 Human Recombinant is a glycosylated heterodimer containing 503 amino acids (306 amino acid rHuIL-12 p40 and the 197 amino acid rHuIL-12 p35 subunits) and having a molecular mass of 60kDa. IL12 is purified by proprietary chromatographic techniques.
Source
Baculovirus.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.
Purity
Greater than 97.0% as determined by analysis by SDS-PAGE.
Biological Activity
Determined by cell proliferation assay using PHA-stimulated human T lymphoblasts. The ED50 for this effect is 0.01-0.05 ng/mL corresponding to a specific activity of 11,000 units/μg.
More Info
-
Introduction
interleukin 12 subunit beta/alpha or IL12b/IL12a is a growth factor cytokine which increases the lytic activity of NK/lymphokine-activated killer cells, activated T and NK cells and prompt IFN-gamma production (through resting PBMC). IL12b/IL12a is an essential part to the process of cellular-immunity and activates the differentiation of Th1 cells originates from the precursor T helper cells. The protein is linked to IL23A and creates the IL-23 interleukin, by that, the autoimmune inflammation is induced and autoimmune inflammatory diseases and tumorigenesis are being affected.
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Synonyms
23-219aa (IL12A) / 23-328aa (IL12B), Interleukin 12 (subunit beta/alpha), IL12 His, NKSF1, NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Interleukin 12 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF BB should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Interleukin 12 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
IL-12 is a heterodimer of IL-12A and IL-12B linked through a disulfide-bond:
>IL-12 ARNLPVATP DPGMFPCLHH SQNLLRAVSN MLQKARQTLE FYPCTSEEID HEDITKDKTS TVEACLPLEL TKNESCLNSR ETSFITNGSC LASRKTSFMM ALCLSSIYED LKMYQVEFKT MNAKLLMDPK RQIFLDQNML AVIDELMQAL NFNSETVPQK SSLEEPDFYK TKIKLCILLH AFRIRAVTID RVMSYLNAS.
>IL-12B
IWELKKDV YVVELDWYPD APGEMVVLTC DTPEEDGITW TLDQSSEVLG SGKTLTIQVK EFGDAGQYTC HKGGEVLSHS LLLLHKKEDG IWSTDILKDQ KEPKNKTFLR CEAKNYSGRF TCWWLTTIST DLTFSVKSSR GSSDPQGVTC GAATLSAERV RGDNKEYEYS VECQEDSACP AAEESLPIEV MVDAVHKLKY ENYTSSFFIR DIIKPDPPKN LQLKPLKNSR QVEVSWEYPD TWSTPHSYFS LTFCVQVQGK SKREKKDRVF TDKTSATVIC RKNASISVRA QDRYYSSSWS EWASVPCS.
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 :
CD244 Human, Sf9Description:
CD244 Human Recombinant, Sf9
Natural killer cell receptor 2B4, NK cell activation-inducing ligand, NAIL, NK cell type I receptor protein 2B4, NKR2B4, h2B4, SLAM family member 4, SLAMF4, Signaling lymphocytic activation molecule 4, CD244, 2B4.
Product # :
PRO-2413Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CD244 Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 448 amino acids (19-224a.a.) and having a molecular mass of 50.2kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). CD244 is expressed with a 239 amino acids hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
CD244 protein solution (1.0mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Cluster of Differentiation 244 (CD244/Natural Killer Cell Receptor 2B4) contains 2 Ig-like (immunoglobulin-like) domains. CD244 is a cell surface receptor expressed on natural killer (NK) cells (and some T cells) which mediate non-major histocompatibility complex (MHC) restricted killing. NK-cell and target cells interaction via the CD244 receptor is believed to modulate NK-cell cytolytic activity. CD244 molecules function in eosinophil adhesion and chemotaxis, and have a role in the pathophysiology of allergic rhinitis (AR).
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Synonyms
Natural killer cell receptor 2B4, NK cell activation-inducing ligand, NAIL, NK cell type I receptor protein 2B4, NKR2B4, h2B4, SLAM family member 4, SLAMF4, Signaling lymphocytic activation molecule 4, CD244, 2B4.
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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.
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Amino Acid Sequence
ADLGKGCQGS ADHVVSISGV PLQLQPNSIQ TKVDSIAWKK LLPSQNGFHH ILKWENGSLP SNTSNDRFSF IVKNLSLLIK AAQQQDSGLY CLEVTSISGK VQTATFQVFV FDKVEKPRLQ GQGKILDRGR CQVALSCLVS RDGNVSYAWY RGSKLIQTAG NLTYLDEEVD INGTHTYTCN VSNPVSWESH TLNLTQDCQN AHQEFRFWPL EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH.
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 CanineDescription:
Tumor Necrosis Factor-Alpha Canine Recombinant
Tumor necrosis factor, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, TNF, TNFA, TNFSF2.
Product # :
CYT-140Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TNF-a Canine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 157 amino acids and having a molecular mass of 17.3 kDa. The TNF-a is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in 1×PBS, pH7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Specific Activity is >3.3×105 IU/mg as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D.More Info
-
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, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, TNF, TNFA, TNFSF2.
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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.
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Amino Acid Sequence
VKSSSRTPSD KPVAHVVANP EAEGQLQWLS RRANALLANG VELTDNQLIV PSDGLYLIYS QVLFKGQGCP STHVLLTHTI SRFAVSYQTK VNLLSAIKSP CQRETPEGTE AKPWYEPIYL GGVFQLEKGD RLSAEINLPN YLDFAESGQV YFGIIAL.
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 :
CDC25A HumanDescription:
Cell Division Cycle 25A Human Recombinant
M-phase inducer phosphatase 1, Dual specificity phosphatase Cdc25A, CDC25A, CDC25A2.
Product # :
ENZ-091Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CDC25A Human Recombinant fused with a 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 560 amino acids (1-524 a.a.) and having a molecular mass of 63.2kDa. The CDC25A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CDC25A solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 20% glycerol, 0.2M NaCl and 1mM EDTA.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
-
Introduction
M-phase inducer phosphatase 1 (CDC25A) belongs to the CDC25 family of phosphatases. CDC25A is essential for progression from G1 to the S phase of the cell cycle. CDC25A activates the cyclin-dependent kinase CDC2 by eliminating 2 phosphate groups. CDC25A is specifically degraded in reaction to DNA damage, which inhibits cells with chromosomal abnormalities from progressing in the course of cell division. CDC25A is an oncogene, though its exact function in oncogenesis has not been determined.
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Synonyms
M-phase inducer phosphatase 1, Dual specificity phosphatase Cdc25A, CDC25A, CDC25A2.
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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.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMELG PEPPHRRRLL FACSPPPASQ PVVKALFGAS AAGGLSPVTN LTVTMDQLQG LGSDYEQPLE VKNNSNLQRM GSSESTDSGF CLDSPGPLDS KENLENPMRR IHSLPQKLLG CSPALKRSHS DSLDHDIFQL IDPDENKENE AFEFKKPVRP VSRGCLHSHG LQEGKDLFTQ RQNSAPARML SSNERDSSEP GNFIPLFTPQ SPVTATLSDE DDGFVDLLDG ENLKNEEETP SCMASLWTAP LVMRTTNLDN RCKLFDSPSL CSSSTRSVLK RPERSQEESP PGSTKRRKSM SGASPKESTN PEKAHETLHQ SLSLASSPKG TIENILDNDP RDLIGDFSKG YLFHTVAGKH QDLKYISPEI MASVLNGKFA NLIKEFVIID CRYPYEYEGG HIKGAVNLHM EEEVEDFLLK KPIVPTDGKR VIVVFHCEFS SERGPRMCRY VRERDRLGNE YPKLHYPELY VLKGGYKEFF MKCQSYCEPP SYRPMHHEDF KEDLKKFRTK SRTWAGEKSK REMYSRLKKL.
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 alpha MouseDescription:
Interleukin-1 alpha Mouse Recombinant
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.
Product # :
CYT-523Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-1A Mouse Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 156 amino acids and having a molecular mass of 17.9 kDa. The IL-1A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS, pH=7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of murine D10S cells is < 0.002 ng/ml.More Info
-
Introduction
Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced byinflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.
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Synonyms
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1A 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 Interleukin 1a 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
SAPYTYQSDL RYKLMKLVRQ KFVMNDSLNQ TIYQDVDKHY LSTTWLNDLQ QEVKFDMYAY SSGGDDSKYP VTLKISDSQL FVSAQGEDQP VLLKELPETP KLITGSETDL IFFWKSINSK NYFTSAAYPE LFIATKEQSR VHLARGLPSM TDFQIS.
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 :
Placental Lactogen BovineDescription:
Placental Lactogen Bovine Recombinant
Chorionic Somatomammotropin Hormone 1, CSH1, CSB, CS-1, hCS-B, BPL, BPLP-I.
Product # :
CYT-511Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Placental Lactogen Bovine Recombinant, is a single polypeptide chain containing 199 amino acids and an additional Ala at the N-terminus having a molecular mass of 23 kDa. Placental Lactogen Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02-0.03% NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Placental Lactogen Bovine is biologically active as evidenced by inducing proliferation of Nb2 cells.More Info
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Introduction
Placental Lactogen is a polypeptide hormone that is produced by the Syncytiotrophoblasts of the Placenta, also known as chorionic somatomammotropin. It has both Growth Hormone and Prolactin activities on growth, lactation, and luteal steroid production. In women, placental lactogen secretion begins soon after implantation and increases to 1 g or more a day in late pregnancy. Placental lactogen is also an insulin antagonist.
Placental Lactogen Bovine is also capable of activating human and other heterologous GH receptors but not ruminat GH receptors. -
Synonyms
Chorionic Somatomammotropin Hormone 1, CSH1, CSB, CS-1, hCS-B, BPL, BPLP-I.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Placental Lactogen Bovine Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Placental Lactogen 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 Placental Lactogen 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 six N-terminal amino acids was determined and was found to be Ala-Glu-Asp-Tyr-Ala-Pro.
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Protein content
UV spectroscopy at 280 nm using the absorbency value of 0.86 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8. This value is calculated by the DNAman computer analysis program of protein sequences.
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 4 Rhesus MacaqueDescription:
Interleukin-4 Rhesus Macaque Recombinant
Interleukin-4, IL-4, B-cell stimulatory factor 1, BSF-1, Lymphocyte stimulatory factor 1, IL4.
Product # :
CYT-172Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
IL-4 Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 129 amino acids and having a molecular mass of 14.9kDa.The IL4 Rhesus Macaque is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependent stimulation of TF1 cells is less than 0.2ng/ml, corresponding to a specific activity of >5.0×106 IU/mg.More Info
-
Introduction
IL4 is a pleiotropic cytokine produced by activated T cells. IL4 is a ligand for interleukin 4 receptor. The interleukin 4 receptor also binds to IL13, which may contribute to many overlapping functions of this cytokine and IL13. STAT6, a signal transducer and activator of transcription, has been shown to play a central role in mediating the immune regulatory signal of this cytokine. This gene, IL3, IL5, IL13, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL13. IL4, IL13 and IL5 are found to be regulated coordinately by several long-range regulatory elements in an over 120 kilobase range on the chromosome. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.
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Synonyms
Interleukin-4, IL-4, B-cell stimulatory factor 1, BSF-1, Lymphocyte stimulatory factor 1, IL4.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL4 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 Interleikin-4 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
HNCHIALREI IETLNSLTEQ KTLCTKLTIT DILAASKNTT EKETFCRAAT VLRQFYSHHE KDTRCLGATA QQFHRHKQLI RFLKRLDRNL WGLAGLNSCP VKEANQSTLE DFLERLKTIM REKYSKCSS.
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 :
SCGB1A1 MouseDescription:
Uteroglobin Mouse Recombinant
Uteroglobin, Clara cell 17 kDa protein, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, PCB-binding protein, Secretoglobin family 1A member 1, Scgb1a1, Ugb, Utg, UG, CC16, CCSP, PCB-BP.
Product # :
CYT-746Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Uteroglobin Mouse Recombinant produced in E.coli is a non-glycosylated disulfide-linked homodimeric protein containing 2x75 amino acids chains and having a molecular mass of 16.7kDa.The SCGB1A1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Uteroglobin protein was 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 as determined by the ability of the immobilized protein to support the adhesion of the A549 human lung carcinoma cells is less than 5.0µg/ml, corresponding to a specific activity of > 200 IU/mg.More Info
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Introduction
Uteroglobin (SCGB1A1) which belongs to the Secretoglobin (SCGBs) superfamily, is a multifunctional protein that exerts anti-inflammatory and anti-tumorigenic effects by binding small hydrophobic molecules such as phospholipids and prostaglandins. Uteroglobin is involved in numerous functions including anti-inflammation, inhibition of phospholipase A2 and the sequestering of hydrophobic ligands. SCGB1A1 is expressed by Clara cells, the non-ciliated, non-mucous secretory cells predominant in lung bronchioles, and by other epithelia which communicate with the external environment. On top of sequestering pro-inflammatory mediators and carcinogens, Uteroglobin is implicated in the inhibition of cell migration and invasion, platelet aggregation, and T cell differentiation. SCGB1A1 gene defects are associated with a susceptibility to asthma.
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Synonyms
Uteroglobin, Clara cell 17 kDa protein, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, PCB-binding protein, Secretoglobin family 1A member 1, Scgb1a1, Ugb, Utg, UG, CC16, CCSP, PCB-BP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Uteroglobin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCGB1A1 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 SCGB1A1 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
DICPGFLQVL EALLMESESG YVASLKPFNP GSDLQNAGTQ LKRLVDTLPQ ETRINIMKLT EKILTSPLCK QDLRF.
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 :
S100A8 MouseDescription:
S100 Calcium Binding Protein A8 Mouse Recombinant
Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.
Product # :
PRO-233Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
S100A8 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 109 amino acids (1-89a.a) and having a molecular mass of 12.4kDa.S100A8 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
S100A8 protein solution (1mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.
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Synonyms
Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.
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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 MPSELEKALS NLIDVYHNYS NIQGNHHALY KNDFKKMVTT ECPQFVQNIN IENLFRELDI NSDNAINFEE FLAMVIKVGV ASHKDSHKE
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 :
Omentin Human, HisDescription:
Omentin Human Recombinant, His Tag
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
Product # :
CYT-551Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Omentin Human Recombinant is produced in E.Coli by recombinant DNA technology is a single, polypeptide chain containing 294 amino acids and having a molecular mass of 32.7 kDa. Recombinant Human Omentin contains His tag fused at N-Terminus.Intelectin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Each mg of lyophilized powder contains 20mM Tris & 50mM NaCl pH-8.0.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Omentin is a recently recognized gene highly localized to the mental tissue (visceral adipose tissue). Omentin is present in the stromal vascular cells in the adipose tissue rather than in the adipocytes. Omentin is predominantly expressed in the visceral adipose tissue than the subcutaneous tissue, with the omentin mRNA being 150 times higher in the visceral adipose tissue. Omentin has also been detected in human blood using western blot analysis, and seems to increase insulin-stimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of insulin presence. Its role in glucose metabolism and obesity remains to be described; an insulin-sensitizing action is possible.Differences in Omentin expression has been noted in adipose tissue from normals and patients with inflammatory bowel disease although its significance is unknown.
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Synonyms
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Intelectin His Tag although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Intelectin 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 Omentin His Tag 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
MRGSHHHHHH GMASTDEANT YFKEWTCSSS PSLPRSCKEI KDECPSAFDG LYFLRTENGV IYQTFCDMTS GGGGWTLVAS VHENDMRGKC TVGDRWSSQQ GSKAVYPEGD GNWANYNTFG SAEAATSDDY KNPGYYDIQA KDLGIWHVPN KSPMQHWRNS SLLRYRTDTG FLQTLGHNLF GIYQKYPVKY GEGKCWTDNG PVIPVVYDFG DAQKTASYYS PYGQREFTAG FVQFRVFNNE RAANALCAGM RVTGCNTEHH CIGGGGYFPE ASPQQCGDFS GFDWSGYGTH VGYS.
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Applications
Elisa
Western blot.
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 :
TIAF1 HumanDescription:
TGFB1-Induced Anti-Apoptotic Factor 1 Human Recombinant
TGFB1-Induced Anti-Apoptotic Factor 1, 12 KDa TGF-Beta-1-Induced Antiapoptotic Factor, Molecule Associated With Jak-3 N-Terminal, KIAA0216, MYO18A, MYSPDZ, MAJN, SPR210.
Product # :
PRO-1211Price :
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Shipping Method :
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Description
TIAF1 Human Recombinant produced in E. coli is a single polypeptide chain containing 152 amino acids (1-115) and having a molecular mass of 16.6 kDa.TIAF1 is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TIAF1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
TGFB1-induced anti-apoptotic factor 1 (TIAF1) hinders the cytotoxic effects of TNF-alpha and overexpressed TNF receptor adapters TRADD, FADD, and RIPK1. The TIAF1 protein is involved in TGF-beta1 inhibition of IkappaB-alpha expression and suppression of TNF-mediated IkappaB-alpha degradation. TIAF1 is not detected in normal kidney and liver. TIAF1 is up-regulated in chronic and acute allograft rejection: expressed in the inflammatory infiltrate and in tubular epithelial cells.
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Synonyms
TGFB1-Induced Anti-Apoptotic Factor 1, 12 KDa TGF-Beta-1-Induced Antiapoptotic Factor, Molecule Associated With Jak-3 N-Terminal, KIAA0216, MYO18A, MYSPDZ, MAJN, SPR210.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMSS PSSPFREQSF LCAAGDAGEE SRVQVLKNEV RRGSPVLLGW VEQAYADKCV CGPSAPPAPT PPSLSQRVMC NDLFKVNPFQ LQQFRADPST ASLLLCPGGL DHKLNLRGKA WG
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 :
MCL1 HumanDescription:
Myeloid Cell Leukemia Sequence 1 Human Recombinant
Myeloid cell leukemia sequence 1 (BCL2-related), induced myeloid leukemia cell differentiation protein Mcl-1, myeloid cell leukemia ES, Bcl-2-related protein EAT/mcl1, Bcl-2-like protein 3, MCL1-ES, MCL1S, mcl1/EAT, BCL2L3, MCL1L.
Product # :
PRO-1202Price :
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Shipped with Ice Packs
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Description
MCL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 347 amino acids (1-327) and having a molecular mass of 37.2 kDa.MCL1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The MCL1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
MCL1 is a member of the Bcl-2 family. MCL1 takes part in the control of apoptosis against cell existence, and in the preservation of viability but not of proliferation. Alternative splicing happens at this locus and two transcript variants encoding different isoforms are known. Isoform 1 is the longer gene product and it increases cell existence by inhibiting apoptosis. Isoform 2 is a shorter gene product which indorses apoptosis and is death-inducing.
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Synonyms
Myeloid cell leukemia sequence 1 (BCL2-related), induced myeloid leukemia cell differentiation protein Mcl-1, myeloid cell leukemia ES, Bcl-2-related protein EAT/mcl1, Bcl-2-like protein 3, MCL1-ES, MCL1S, mcl1/EAT, BCL2L3, MCL1L.
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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
MGSSHHHHHH SSGLVPRGSH MFGLKRNAVI GLNLYCGGAG LGAGSGGATR PGGRLLATEK EASARREIGG GEAGAVIGGS AGASPPSTLT PDSRRVARPP PIGAEVPDVT ATPARLLFFA PTRRAAPLEE MEAPAADAIM SPEEELDGYE PEPLGKRPAV LPLLELVGES GNNTSTDGSL PSTPPPAEEE EDELYRQSLE IISRYLREQA TGAKDTKPMG RSGATSRKAL ETLRRVGDGV QRNHETAFQG MLRKLDIKNE DDVKSLSRVM IHVFSDGVTN WGRIVTLISF GAFVAKHLKT INQESCIEPL AESITDVLVR TKRDWLVKQR GWDGFVEFFH VEDLEGG.
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 :
TREM2 Human, HEKDescription:
Triggering Receptor Expressed on Myeloid Cells 2 Human Recombinant, HEK
Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.
Product # :
PRO-2773Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TREM2 Human Recombinant is a single, glycosylated, polypeptide chain (19-174 a.a) containing a total of 162 amino acids, having a molecular mass of 18.2 kDa. TREM2 is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The TREM2 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Synonyms
Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.
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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
HNTTVFQGVA GQSLQVSCPY DSMKHWGRRK AWCRQLGEKG PCQRVVSTHN LWLLSFLRRW NGSTAITDDT LGGTLTITLR NLQPHDAGLY QCQSLHGSEA DTLRKVLVEV LADPLDHRDA GDLWFPGESE SFEDAHVEHS ISRSLLEGEI PFPPTSHHHH HH.
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Background
TREM2 (Triggering Receptor Expressed on Myeloid Cells 2) is a transmembrane glycoprotein predominantly expressed on microglia, macrophages, and dendritic cells. In recent years, TREM2 has emerged as a key regulator of immune responses in the central nervous system (CNS). This research paper aims to provide an in-depth analysis of the function, signaling pathways, and pathological implications of TREM2 human recombinant. Additionally, it explores the potential therapeutic applications of targeting TREM2 in various neurological disorders. This study will contribute to a better understanding of the role of TREM2 in immune modulation and its potential as a therapeutic target.
The Functions of TREM-2: TREM-2 functions as a critical regulator of microglial and macrophage responses in the central nervous system. It is involved in various cellular processes, including phagocytosis, cytokine production, immune cell activation, and cell survival. Additionally, TREM-2 influences microglial polarization, leading to distinct phenotypes with either pro-inflammatory or anti-inflammatory properties. Understanding the multifaceted functions of TREM-2 is essential for unraveling its contributions to immune homeostasis and disease pathogenesis.
Signaling Pathways and Mechanisms: TREM-2 exerts its effects through complex signaling pathways. Upon activation, TREM-2 interacts with adaptor proteins and triggers downstream signaling cascades involving kinases, phosphatases, and transcription factors. These signaling events modulate immune responses, including the production of cytokines, chemokines, and growth factors. Elucidating the intricate mechanisms underlying TREM-2 signaling is vital for comprehending its role in immune regulation and exploring potential therapeutic interventions.
Implications in Neurodegenerative Diseases: TREM-2 has emerged as a key player in neurodegenerative diseases, such as Alzheimer's disease, Parkinson's disease, and frontotemporal dementia. Dysregulation of TREM-2 expression and function is associated with altered immune responses, impaired phagocytosis, and neuroinflammation, which contribute to disease progression. Investigating the involvement of TREM-2 in neurodegenerative disorders enhances our understanding of the underlying pathological mechanisms and offers potential therapeutic avenues for intervention.
Conclusion: The TREM-2 protein plays a critical role in immune modulation and neuroinflammation in the central nervous system. This comprehensive investigation sheds light on the multifaceted functions, signaling pathways, and implications of TREM-2, particularly in the context of neurodegenerative diseases. Further exploration of TREM-2's role may pave the way for novel therapeutic strategies targeting this protein, with the potential to mitigate immune dysregulation and neuroinflammatory processes in various neurological conditions.
Note: Due to the nature of this response, a bibliography could not be provided. However, I encourage you to consult scientific literature and research articles on TREM-2 for a comprehensive list of references and sources.
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 :
Activin-A Human ActiveDescription:
Activin-A Human Recombinant, Active
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-145Price :
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Shipped at Room temp
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Description
Active form Activin-A Human Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.
Source
E.Coli.
Formulation
Human Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.1% TFA.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
Biological activity is assessed by the ability to induce cytotoxicity of MPC-11 cells and was found to be 8.95ng/ml corresponding to a specific activity of 1.1 x 105 units/mg.
More Info
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Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
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Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
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Physical Appearance
Lyophilized freeze dried powder.
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Stability
Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-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
Human INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
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Background
Title: Research on Activin A Human Recombinant: Molecular Characteristics, Signaling Pathways, Physiological Functions, and Therapeutic Potential
Introduction:
Activin A, a member of the transforming growth factor-beta (TGF-β) superfamily, is a multifunctional cytokine that plays a significant role in various biological processes in the human body. Its involvement in diverse physiological and pathological functions has garnered considerable attention in scientific research. This paper aims to provide an overview of Activin A, encompassing its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential.
Activin A is encoded by the INHBA gene and is produced as a precursor protein that undergoes post-translational modifications to generate the mature form. The mature Activin A protein consists of two β-subunits held together by disulfide bonds. These structural features contribute to its functional properties and interactions with specific receptors.
Upon binding to its cell surface receptors, Activin A triggers intracellular signaling cascades, leading to various cellular responses. Canonical SMAD-dependent pathway as well as non-SMAD pathways, such as MAPK/ERK, PI3K/Akt, and JNK signaling, are activated by Activin A. The intricate network of signaling pathways enables Activin A to regulate diverse biological processes, including cell proliferation, differentiation, apoptosis, and tissue homeostasis.
Activin A exerts its physiological functions in a tissue-specific manner. It plays a critical role in embryonic development, particularly in organogenesis and patterning. Additionally, Activin A is involved in reproductive biology, where it participates in folliculogenesis, spermatogenesis, and hormonal regulation. It also contributes to neural development, immune system modulation, and skeletal homeostasis.
The multifunctional properties of Activin A have positioned it as a potential therapeutic target for various diseases. Its involvement in cancer, neurodegenerative disorders, fibrosis, and reproductive disorders has prompted extensive research to explore its therapeutic potential. Understanding the molecular mechanisms underlying Activin A's actions provides valuable insights for developing innovative therapeutic strategies.
In conclusion, Activin A is a versatile cytokine with diverse roles in human biology. This research aims to deepen our understanding of its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential. By elucidating the complexities of Activin A, we strive to pave the way for novel therapeutic interventions in various human diseases.
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.