|Detection of Mouse Serpin A8/Angiotensinogen by Western Blot. Western blot shows lysates of mouse liver tissue. PVDF membrane was probed with 0.5 µg/mL of Rat Anti-Mouse Serpin A8/Angiotensinogen Monoclonal Antibody (Catalog # MAB6966) followed by HRP-conjugated Anti-Rat IgG Secondary Antibody (Catalog # HAF005). Specific bands were detected for Serpin A8/Angiotensinogen at approximately 52-62 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
|Serpin A8/Angiotensinogen in Mouse Intestine. Serpin A8/Angiotensinogen was detected in perfusion fixed frozen sections of mouse intestine using Rat Anti-Mouse Serpin A8/Angiotensinogen Monoclonal Antibody (Catalog # MAB6966) at 5 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Rat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS017) and counterstained with hematoxylin (blue). Specific staining was localized to intestinal epithelial cells. View our protocol for Chromogenic IHC Staining of Frozen Tissue Sections.|
Serpin A8 (serine proteinase inhibitor-clade A #8; also angiotensinogen/ANGT) 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. Ang II induces vascoconstriction and aldosterone release. Mature human Serpin A8 is 452 aa in length (aa 34-485). It contains Ang I (aa 34-43) that is cleaved to create Ang II (aa 34-41). Serpin A8 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. Over aa 34-485, human Serpin A8 shares 61% aa identity with mouse Serpin A8.
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