|Detection of Serpin G1/C1 Inhibitor by Western Blot. Western blot shows lysates of human lung tissue and human ovary tissue. PVDF membrane was probed with 0.1 µg/mL of Goat Anti-Human Serpin G1/C1 Inhibitor Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2488) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). A specific band was detected for Serpin G1/C1 Inhibitor at approximately 100 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
|Detection of Human Serpin G1/C1 Inhibitor by Simple WesternTM. Simple Western lane view shows lysates of human lung tissue, loaded at 0.2 mg/mL. A specific band was detected for Serpin G1/C1 Inhibitor at approximately 162 kDa (as indicated) using 1 µg/mL of Goat Anti-Human Serpin G1/C1 Inhibitor Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2488) followed by 1:50 dilution of HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.|
As a member of the serpin superfamily of serine protease inhibitors, Serpin G1/C1 inhibitor is the physiological inhibitor of activated C1r and C1s, two serine proteases involved in the classical complement pathway. In addition, it inhibits plasma kallikrein and coagulation factor XIIa, two serine proteases involved in the processing of kininogen to release bradykinin. Therefore, it plays an important role in regulating activation of both the complement and contact systems (1). Serpin G1 deficiency results in hereditary angioedema, which is characterized by recurrent episodes of localized angioedema of the skin, gastrointestinal mucosa or upper respiratory mucosa (2). The deduced amino acid sequence of human Serpin G1 precursor consists of 500 residues with a signal peptide. The mature protein of 478 amino acid residues is heavily glycosylated (1).
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