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> SerpinA1 Protein & Antibody SerpinA1 Protein & Antibody
Serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1
SerpinA1 Products
SerpinA1 Protein, Recombinant
| Molecule | Species | Description //For Detailed Info. and Price------CLICK! | Cat. No |
| SerpinA1 | Human | SerpinA1 Protein, Recombinant  |
10306-H08H |
SerpinA1 Antibody
| Molecule | Application | Description //For Detailed Info. and Price------CLICK! | Cat. No |
| Human SerpinA1 | ELISA | SerpinA1 Antibody | 10306-R204 |
| Human SerpinA1 | WB, ELISA | SerpinA1 Antibody | 10306-RP01 |
| Human SerpinA1 | WB, ELISA | SerpinA1 Antibody (Antigen Affinity Purified) | 10306-RP02 |
SerpinA1 cDNA Clone
| Molecule | Species | Description //For Detailed Info. and Price------CLICK! | Cat. No |
| SerpinA1 | Human | Homo sapiens SerpinA1 transcript variant 1 cDNA Clone(NM_000295.4) | HG10306-M |
SerpinA1 Related Areas
Enzyme>>Protease & Regulator>>Serine Protease & Regulator>>Serpin Superfamily>>SerpinA1
Immunology>>Innate Immunity>>Acute Phase Proteins>>SerpinA1
SerpinA1 Alternative Names
SERPINA1, A1A, A1AT, AAT, MGC23330, MGC9222, PI, PI1, PRO2275 [Homo sapiens]
Serpina1, Aat, Pre, Pre-1, Spi-1, Spi1, [a]1-PI [Mus musculus]
SerpinA1 Related Products
Protein Products
Antibody Products
cDNA Clone Products
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. It 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 a 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 Related Studies
- Köhnlein 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.
SerpinA1 related areas, pathways, and other information
