The antibody was purified by affinity chromatography and conjugated with APC under optimal conditions. The solution is free of unconjugated APC and unconjugated antibody.
anticorps ADAM10, anticorps Adam10, anticorps adam10, anticorps wu:fc03d12, anticorps ad10, anticorps cd156c, anticorps kuz, anticorps kuzbanian, anticorps madm, anticorps xadam10, anticorps ADAM-10, anticorps ADAM 10, anticorps AD10, anticorps CD156c, anticorps HsT18717, anticorps MADM, anticorps 1700031C13Rik, anticorps LOC100219653, anticorps zgc:64203, anticorps ADAM metallopeptidase domain 10, anticorps ADAM metallopeptidase domain 10a, anticorps ADAM metallopeptidase domain 10 S homeolog, anticorps a disintegrin and metallopeptidase domain 10, anticorps ADAM metallopeptidase domain 10b, anticorps ADAM10, anticorps Adam10, anticorps adam10a, anticorps adam10.S, anticorps adam10b
Sujet
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.