The antibody was purified by affinity chromatography and conjugated with APC under optimal conditions. The solution is free of unconjugated APC and unconjugated antibody.
ADAM10 antikoerper, Adam10 antikoerper, adam10 antikoerper, wu:fc03d12 antikoerper, ad10 antikoerper, cd156c antikoerper, kuz antikoerper, kuzbanian antikoerper, madm antikoerper, xadam10 antikoerper, ADAM-10 antikoerper, ADAM 10 antikoerper, AD10 antikoerper, CD156c antikoerper, HsT18717 antikoerper, MADM antikoerper, 1700031C13Rik antikoerper, LOC100219653 antikoerper, zgc:64203 antikoerper, ADAM metallopeptidase domain 10 antikoerper, ADAM metallopeptidase domain 10a antikoerper, ADAM metallopeptidase domain 10 S homeolog antikoerper, a disintegrin and metallopeptidase domain 10 antikoerper, ADAM metallopeptidase domain 10b antikoerper, ADAM10 antikoerper, Adam10 antikoerper, adam10a antikoerper, adam10.S antikoerper, adam10b antikoerper
Hintergrund
CD156c, also known as a disintegrin and metalloproteinase domain-containing protein 10 (ADAM10), is a 748 amino acid type I membrane glycoprotein ubiquitously expressed on most cell types. It consists of multiple functional domains, including a N-terminal prodomain, catalytic domain, cysteine-rich domain, transmembranous domain, and cytoplasmic domain. It is secreted as a precursor protein and becomes as the activate/mature form through removing the ADAM10 prodomain by proprotein convertase 7 and furin. ADAM10 functions as metalloproteinase to cleave several molecules including Notch, pro-TNF-α, amyloid precursor protein, myelin basic protein, and type IV collagen. It mediates the release of several cell adhesion molecules such as vascular endothelial cadherin or L-selectin to regulate endothelial permeability and leukocyte transmigration. Dysregulation of ADAM activity may contribute to the pathogenesis of vascular diseases.