Mouse Serpin A8/Angiotensinogen Antibody

Serpin A8 (serine proteinase inhibitor-clade A8; also angiotensinogen) is a secreted, 52-62 kDa glycoprotein member of the clade F-subfamily, serpin superfamily of protease inhibitors. It is expressed by neurons and hepatocytes, and undergoes extracellular cleavage by renin to create a ten amino acid (aa) peptide termed Ang/angiotensin I. This inactive peptide is further cleaved by ACE on the endothelial cell membrane to create bioactive Ang II and III. Ang II induces vascoconstriction and aldosterone release by acting on AT1 receptors, while Ang III drives aldosterone release. Ang I can be further processed by MME to generate Ang, a peptide that binds MAS1 on platelets, and promotes the release of NO, an antithrombotic agent. Mature mouse angiotensinogen is 453 aa in length (aa 25-477). It contains Ang I (aa 25-34) that is cleaved to create Ang II (aa 25-32), Ang III (aa 26-32) and Ang I (aa 25-31). Serpin A8/Angiotensinogen may circulate in a 200 kDa complex with major basic protein (MBP), or as part of a larger 300 kDa complex with MBP and complement C3dg. There is an alternative start site five aa upstream of the standard site. Over aa 25-477, mouse serpin A8 shares 86% and 61% aa identity with rat and human serpin A8, respectively.