| Description | Used in the production of confectionary foods and artificial honey | Inquire | Purity>95% SDS-PAGE.FunctionProbable cell adhesion protein | Background:VCAM-1, also known as CD106, is an immunoglobulin (Ig)-like adhesion molecule that is mainly expressed in endothelial cells and other cell types including macrophages, dendritic cells, neurons, smooth muscle cells, fibroblasts, and oocytes. It plays a critical role in inflammation by Background:VCAM-1, also known as CD106, is an immunoglobulin (Ig)-like adhesion molecule that is mainly expressed in endothelial cells and other cell types including macrophages, dendritic cells, neurons, smooth muscle cells, fibroblasts, and oocytes. It plays a critical role in inflammation by recruiting leukocytes to acute and chronic inflammation sites. Alternatively-spliced forms are known to occur, but the most common form is a type I transmembrane protein with a 674 aa extracellular domain (ECD) that includes seven C2-type immunoglobulin domains, a 22 aa transmembrane segment, and a 19 amino acid (aa) cytoplasmic tail. Within the ECD, human VCAM-1 shares 75% and 76% aa sequence identity with the mouse and rat VCAM-1, respectively. VCAM-1 binds to leukocyte integrins alpha 4 beta 1 (VLA-4) and alpha 4 beta 7. During the inflammatory adhesion mechanism, activated integrins halt rolling leukocytes and attach them firmly to the vascular endothelium. The VCAM-1:VLA-4/ alpha 4 beta 7 interaction is also thought to be involved in the extravasation of white blood cells through the blood vessel wall to sites of inflammation. ELISA techniques have shown that detectable levels of soluble VCAM-1 are present in the biological fluids of apparently normal individuals, but elevated levels of serum VCAM-1 are indicative of future Atrial Fibrillation incident as well as liver disease. Tumor cells use overexpression of VCAM-1 as means of escaping immune surveillance.Post-translational modifications：Sialoglycoprotein.Function:Important in cell-cell recognition. Appears to function in leukocyte-endothelial cell adhesion. Interacts with the beta-1 integrin VLA4 on leukocytes, and mediates both adhesion and signal transduction. The VCAM1/VLA4 interaction may play a pathophysiologic role both in immune responses and in leukocyte emigration to sites of inflammation... 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 |