| Description | Biochemical Test:SDS-PAGE (purity > 80%); Western blot with patient sample.Calculated Isoelectric Point:pH 5.62 | Inquire | Recombinant human basic fibroblast growth factor (also known as basic FGF, bFGF, FGF2, FGF-beta, or heparin-binding growth factor), is a biologically active protein suitable for cell culture applications. bFGF regulates diverse processes such as cell proliferation, differentiation, survival, Recombinant human basic fibroblast growth factor (also known as basic FGF, bFGF, FGF2, FGF-beta, or heparin-binding growth factor), is a biologically active protein suitable for cell culture applications. bFGF regulates diverse processes such as cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation, and wound recovery. bFGF can be used in studies of angiogenesis, fibroblast mitosis, axonal outgrowth in PC-12 cells, receptor binding, and tyrosine phosphorylation. This strain is expressed in recombinant Escherichia coli, and after multi-step separation and purification, it is dissolved in 10mM PBS, 0.15 M NaCl (pH7.2) solution, filtered through a 0.22 µm filter membrane, and then freeze-dried to make a lyophilized powder... Read More | Product IntroductionKGF keratinocyte growth factor (KGF), a cytokine identified by Rubin et al (1989) from the culture supernatant of embryonic lung fibroblasts, is an FGF family member, namely FGF-7.KGF is secreted by stromal cells and its receptor is distributed in epithelial cells, where it is a Product IntroductionKGF keratinocyte growth factor (KGF), a cytokine identified by Rubin et al (1989) from the culture supernatant of embryonic lung fibroblasts, is an FGF family member, namely FGF-7.KGF is secreted by stromal cells and its receptor is distributed in epithelial cells, where it is a potent epithelial cell specific growth factor, and its mitogenic activity is mainly expressed in keratinocytes, which can specifically promote epithelial cell proliferation, migration and differentiation, and is closely related to many aspects, such as organ development, wound repair, tumorigenesis and immune reconstitution.Osrhkgf was created using genetic recombination, expressed from rice endosperm cells and through a protein purification process.Specification parametersSource Oryza sativaAppearance white lyophilized powderActivity ≥1.0×105IU/mgpH 6.5-7.5Molecular weight 19.0 kDEndotoxin ≦0.1EU/ugCAS No 148348-15-6Matters needing attentionReconstitution: it is recommended to lyophilize the powder of osrhkgf to 100-200 UG/ml with sterile water to make further dilutions with other solvents.The dissolved osrhkgf could be stored for 2-7 days at 4 ◦ C and used up as soon as possible.To not use for short periods, store at - 20 ℃.Use as soon as possible after opening to avoid contamination.Limitations of useIt is suitable for research, laboratory and production use only and cannot be used directly in humans... Read More | Background：Tumor necrosis factor alpha (TNF-alpha ), also known as cachectin and TNFSF2, is the prototypic ligand of the TNF superfamily. It is a pleiotropic molecule that plays a central role in inflammation, immune system development, apoptosis, and lipid metabolism. Rat TNF-alpha consisitsBackground：Tumor necrosis factor alpha (TNF-alpha ), also known as cachectin and TNFSF2, is the prototypic ligand of the TNF superfamily. It is a pleiotropic molecule that plays a central role in inflammation, immune system development, apoptosis, and lipid metabolism. Rat TNF-alpha consisits of a 35 amino acid (aa) cytoplasmic domain, a 21 aa transmembrane segment, and a 179 aa extracellular domain (ECD). Within the ECD, rat TNF-alpha shares 94% aa sequence identity with mouse and 69%-76% with bovine, canine, cotton rat, equine, feline, human, porcine, and rhesus TNF-alpha. TNF-alpha is produced by a wide variety of immune, epithelial, endothelial, and tumor cells. TNF-alpha is assembled intracellularly to form a noncovalently linked homotrimer which is expressed on the cell surface. Cell surface TNF-alpha can induce the lysis of neighboring tumor cells and virus infected cells, and it can generate its own downstream cell signaling following ligation by soluble TNFR I. Shedding of membrane bound TNF-alpha by TACE/ADAM17 releases the bioactive cytokine, a 55 kDa soluble trimer of the TNF-alpha extracellular domain. TNF-alpha binds the ubiquitous 55-60 kDa TNF RI and the hematopoietic cell-restricted 80 kDa TNF RII, both of which are also expressed as homotrimers. Both type I and type II receptors bind TNF-alpha with comparable affinity, although only TNF RI contains a cytoplasmic death domain which triggers the activation of apoptosis. Soluble forms of both types of receptors are released and can neutralize the biological activity of TNF-alpha. Post-translational modificationsThe soluble form derives from the membrane form by proteolytic processing.The membrane form, but not the soluble form, is phosphorylated on serine residues.Dephosphorylation of the membrane form occurs by binding to soluble TNFRSF1A/TNFR1.O-glycosylated; glycans contain galactose, N-acetylgalactosamine and N-acetylneuraminic acid... Read More |