|Detection of Human Serpin A1/ alpha 1‑Antitrypsin by Western Blot. Western blot shows human plasma and lysates of human lung tissue and human kidney tissue. PVDF membrane was probed with 1 µg/mL of Mouse Anti-Human Serpin A1/ alpha 1‑Antitrypsin Monoclonal Antibody (Catalog # MAB1268) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF018). Specific bands were detected for Serpin A1/ alpha 1‑Antitrypsin at approximately 50-60 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
Serpin A1/ alpha 1‑Antitrypsin in HepG2 Human Cell Line. |
Serpin A1/ alpha 1‑Antitrypsin was detected in immersion fixed HepG2 human hepatocellular carcinoma cell line using Mouse Anti-Human Serpin A1/
Detection of Human Serpin A1/ alpha 1‑Antitrypsin by Simple WesternTM. Simple Western lane view shows lysates of human plasma, loaded at 0.2 mg/mL. A specific band was detected for Serpin A1/ alpha 1‑Antitrypsin at approximately 65 kDa (as indicated) using 10 µg/mL of Mouse Anti-Human Serpin A1/ alpha 1‑Antitrypsin Monoclonal Antibody (Catalog # MAB1268). This experiment was conducted under reducing conditions and using the|
12-230 kDa separation system.
Serpin A1 is the archetypal member of the Serpin superfamily of the serine protease inhibitors (1). As one of the most abundant proteinase inhibitors in the circulation, it is synthesized in the liver and secreted into the bloodstream with the major function to protect tissues against neutrophil elastase. A severe Serpin A1 deficiency leads to several clinical complications such as pulmonary emphysema, juvenile hepatitis, cirrhosis, and hepatocellular carcinoma (2). The deficiency is caused by point mutations in naturally occurring Serpin A1 variants (over 70 are known). For example, the Z variant (Glu342 to Lys) forms intracellular inclusion bodies, is not secreted, and leads to a severe Serpin A1 deficiency (3).
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