Recombinant Mouse Serpin A1c/alpha-1-Antitrypsin Protein, CF

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. Severe Serpin A1 deficiency leads to several clinical complications such as pulmonary emphysema, juvenile hepatitis, cirrhosis, and hepatocellular carcinoma (2). In contrast to a single Serpin A1 gene in the human genome, there is a cluster of five Serpin A1 genes in the mouse genome with high overall sequence identity but markedly divergent residues in the reactive center loop (3, 4). The purified rmSerpin A1c inhibits trypsin and chymotrypsin, but does not inhibit neutrophil elastase.