SerpinA1 Proteins, Antibodies, cDNA Clones, ELISA Kits Research Reagents

SERPINA1 (Serpin Family A Member 1) is a protein coding gene located on human chromosome 14q32.13. SERPINA1 is also known as PI, A1A, AAT, PI1, A1AT, nNIF, PRO2275 and alpha1AT. The human SERPINA1 gene encodes a 46737 Da protein containing 418 amino acids. The SERPINA1 protein is biasedly expressed in liver and small intestine. Among its related pathways are Response to elevated platelet cytosolic Ca2+ and Transport to the Golgi and subsequent modification. SERPINA1 is related to identical protein binding and protease binding. SERPINA3 is an important paralog of SERPINA1 gene. SERPINA1 is associated with some diseases, including Alpha-1-Antitrypsin Deficiency and Hemorrhagic Disease Due To Alpha-1-Antitrypsin Pittsburgh Mutation.

SerpinA1 Protein (2)

    SerpinA1 Antibody (11)

      SerpinA1 ELISA Kit & Match Antibody ELISA Pair Set (2)

      SerpinA1 cDNA Clone (26)


      SerpinA1 Lysate (2)

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        SerpinA1 Background

        SerpinA1, also known as Alpha-1 antitrypsin (AAT), is a prototype member of the Serpin superfamily of the serine protease inhibitors. This serine protease inhibitor blocks the protease, neutrophil elastase. Alpha-1 antitrypsin is mainly produced in the liver and acts as an antiprotease. Its principal function is to inactivate neutrophil elastase, preventing tissue damage. SerpinA1 (alpha1-antitrypsin), an acute phase protein and the classical neutrophil elastase inhibitor, is localized within lipid rafts in primary human monocytes in vitro. Its association with monocytes is inhibited by cholesterol depleting/efflux-stimulating agents (nystatin, filipin, MbetaCD (methyl-beta-cyclodextrin) and oxidized low-density lipoprotein (oxLDL) and conversely, enhanced by free cholesterol. Furthermore, SerpinA1/monocyte association per se depletes lipid raft cholesterol as characterized by the activation of extracellular signal-regulated kinase 2, formation of cytosolic lipid droplets, and complete inhibition of oxLDL uptake by monocytes. Previous population studies have suggested that heterozygote status for the AAT gene (SerpinA1) is a risk factor for chronic rhinosinusitis with nasal polyposis (CRSwNP). Alpha-1 antitrypsin deficiency is a recently identified genetic disease that occurs almost as frequently as cystic fibrosis. It is caused by various mutations in the SerpinA1 gene, and has numerous clinical implications. Alpha-1 antitrypsin deficiency is an inherited disease affecting the lung and liver. In the liver, alpha-1 antitrypsin deficiency may manifest as benign neonatal hepatitis syndrome; a small percentage of adults develop liver fibrosis, with progression to cirrhosis and hepatocellular carcinoma. Its most important physiologic functions are the protection of pulmonary tissue from aggressive proteolytic enzymes and regulation of pulmonary immune processes.

        SerpinA1 References

        • Khnlein T, et al. (2008) Alpha-1 antitrypsin deficiency: pathogenesis, clinical presentation, diagnosis, and treatment. Am J Med. 121(1): 3-9.
        • Camelier AA, et al. (2008) Alpha-1 antitrypsin deficiency: diagnosis and treatment. J Bras Pneumol. 34(7): 514-27.
        • Subramaniyam D, et al. (2010) Cholesterol rich lipid raft microdomains are gateway for acute phase protein, SERPINA1. Int J Biochem Cell Biol. 42(9): 1562-70.
        • Kilty SJ, et al. (2010) Polymorphisms in the SERPINA1 (Alpha-1-Antitrypsin) gene are associated with severe chronic rhinosinusitis unresponsive to medical therapy. Am J Rhinol Allergy. 24(1): e4-9.

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