| Description | Human IgG2-kappa, Recombinant (IB2), Isotype Control, could be used for Flow Cytometry | Inquire | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： 100B, previously called S100 beta, belongs to the S100 family within the EF-hand superfamily of Ca2+ binding proteins. S100 proteins contain two EF-hand motifs that differ in affinity, separated by a hingePurity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： 100B, previously called S100 beta, belongs to the S100 family within the EF-hand superfamily of Ca2+ binding proteins. S100 proteins contain two EF-hand motifs that differ in affinity, separated by a hinge region with a hydrophobic cleft that is exposed upon Ca2+ binding. S100B is a 91 amino acid (aa) protein, after removal of the initial methionine, and is found as homodimers of 10.4 kDa monomers. Human S100B shares 99%, 98%, 100%, 99% and 97% aa sequence identity with mouse, rat, rabbit, equine and bovine S100B, respectively. Within the S100 family, human S100B shows the highest aa identity (59%) with S100A1. S100B is expressed primarily by astrocytes and oligodendrocytes in the central nervous system, and by Schwann cells in the peripheral nervous system. Ca2+-bound S100B interacts in vitro with at least 20 cytoplasmic proteins, including several structural molecules such as tubulin and GFAP. It can inhibit the phosphorylation of these kinase substrates and others such as tau and neuromodulin. Astrocytes can secrete S100B, which then acts in a cytokine-like manner. Nanomolar concentrations of S100B are secreted constitutively, promote proliferation, and are neurotrophic and anti-apoptotic. Blood levels of S100B reflect extracellular concentrations within the nervous system, and are elevated in Down’s syndrome, Alzheimer’s disease and Tourette’s syndrome, metabolic stress, acute brain injury and brain tumors. Micromolar concentrations of S100B can be destructive and pro-apoptotic; they induce the expression of iNOS, COX-2, IL-1, IL‑6 and TNF-alpha by microglia, astrocytes or neurons. Most extracellular actions of S100B can be mediated by RAGE (receptor for advanced glycation end products), which is also a receptor for other S100 proteins... Read More | As the most abundant protein in human plasma, human serum albumin (HSA) is the transporter of hormones, lipids and other substances. Its main physiological function is to regulate plasma pH and maintain plasma osmotic pressure.Osrhsa (recombinant human serum albumin from Oryza sativa) is a As the most abundant protein in human plasma, human serum albumin (HSA) is the transporter of hormones, lipids and other substances. Its main physiological function is to regulate plasma pH and maintain plasma osmotic pressure.Osrhsa (recombinant human serum albumin from Oryza sativa) is a recombinant human serum albumin developed by using rice endosperm cell expression platform (oryzhiexp) and purification platform (oryzpur). It does not contain animal derived ingredients and can eliminate the risk of blood derived virus infection. Compared with fetal bovine serum (FBS), plasma derived albumin (pHSA) and bovine serum albumin (BSA), osrhsa has higher purity and better batch stability. It can be used in various research fields, including biopharmaceutical, cell therapy and cell culture of gene therapy. It can replace serum and promote cell growth. At the same time, osrhsa is also widely used in biomedical production as drug carrier, vaccine protector, cell cryoprotectant and medical device embedding agent.ApplicationBiopharmaceuticals, human vaccines, cell culture, cell storage, chemical drug molecular carriers, medical devices, in vitro diagnosis, etc.Comparison of physical and chemical properties between OsrHSA and natural human white pHSAphysicochemical propertiespHSAOsrHSAamino acid sequenceagreementN-terminal amino acidsDAHKSEVDAHKSEVC-terminal amino acidsKLVAASQAALGLKLVAASQAALGLGlycoside modificationnothingmolecular weight (MALDl)66.554 (kDa)66.550 ( a)Isoelectric point (pl)4.84.8Drug binding activityclosethermal stabilitymp 65℃mp 65℃esterase activityidenticalcrystal structureidenticalRestrictions on use:The above products are only suitable for scientific research, laboratory and production use, and cannot be directly used in human body... 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 |