VCAM-1/CD106 Extracellular Domain (human, recombinant)

Vascular cell adhesion molecule 1 (VCAM-1), also known as CD106, is a member of the immunoglobulin (Ig) superfamily that is involved in the adhesion and migration of leukocytes and angiogenesis. It is composed of an extracellular domain, which may contain seven or six Ig-like repeats depending on the splice variant, a transmembrane domain, and a C-terminal domain. VCAM-1 is constitutively expressed in dendritic cells, monocyte-derived cells, and epithelial cells and in endothelium when induced by cytokines. It can be cleaved by disintegrin and metalloproteinase domain-containing protein 17 (ADAM17) and other metalloproteinases to release soluble VCAM-1 (sVCAM-1), which is a process known as shedding, and is induced by TNF-alpha, IL-1beta, and other cytokines. Increased circulating levels of sVCAM-1 is associated with several diseases, including cancer, diabetes, sepsis, cardiovascular diseases, and preeclampsia, as well as parasitic infections. Cayman's VCAM-1/CD106 Extracellular Domain (human, recombinant) protein can be used for cell-based adhesion assays. This protein is a disulfide-linked homodimer. The reduced monomer, composed of VCAM-1 (amino acids 25-697) fused to human IgG1 Fc at its C-terminus, consists of 911 amino acids, has a calculated molecular weight of 100. kDa, and a predicted N-terminus of Phe25 after signal peptide cleavage. As a result of glycosylation, the monomer migrates at approximately 116. kDa by SDS-PAGE under reducing conditions.