| Description | Human IgG3, Recombinant (IB3), Isotype Control, could be used for Flow Cytometry | Purity：>95%(SDS-PAGE) Function：Cooperates with MD-2 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS). Acts via MyD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Up-regulates cell surface Purity：>95%(SDS-PAGE) Function：Cooperates with MD-2 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS). Acts via MyD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Up-regulates cell surface molecules, including adhesion molecules.Background：CD14 is a 55 kDa cell surface glycoprotein that is preferentially expressed on monocytes/macrophages. The human CD14 cDNA encodes a 375 amino acid (aa) residue precursor protein with a 19 aa signal peptide and a C-terminal hydrophobic region characteristic for glycosylphosphatidyinositol (GPI)-anchored proteins. Human CD14 has four potential N-linked glycosylation sites and also bears O-linked carbohydrates. The amino acid sequence of human CD14 is approximately 65% identical with the mouse, rat, rabbit, and bovine proteins. CD14 is a pattern recognition receptor that binds lipopolysaccharides (LPS) and a variety of ligands derived from different microbial sources. The binding of CD14 with LPS is catalyzed by LPS-binding protein (LBP). The toll-like-receptors have also been implicated in the transduction of CD14-LPS signals. Similar to other GPI-anchored proteins, soluble CD14 can be released from the cell surface by phosphatidyinositol-specific phospholipase C. Soluble CD14 has been detected in serum and body fluids. High concentrations of soluble CD14 have been shown to inhibit LPS-mediated responses. However, soluble CD14 can also potentiate LPS response in cells that do not express cell surface CD14... Read More | Purity>95% SDS-PAGE. FunctionIGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Promotes cell migration | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：IL12 is a cytokine that acts on T and natural killer cells, and has a broad array of biological activities. It is a disulfide-linked heterodimer composed of the 40 kD cytokine receptor like subunit and a 35 Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：IL12 is a cytokine that acts on T and natural killer cells, and has a broad array of biological activities. It is a disulfide-linked heterodimer composed of the 40 kD cytokine receptor like subunit and a 35 kD subunit. This cytokine is expressed by activated macrophages that serve as an essential inducer of Th1 cells development. IL12 has been found to be important for sustaining a sufficient number of memory/effector Th1 cells to mediate long-term protection to an intracellular pathogen. Recombinant human IL12 protein, fused to His-tag at C-terminus, was expressed in insect cells using baculovirus expression system and purified by using conventional chromatography techniques... 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 |