The a1-antichymotrypsin (ACT) protein has a molar mass of 55-66kDa. It has a serpin structure with three ß sheets, 8 a helices and a reactive centre loop containing the active site. The gene is mapped to human chromosome 14q32.1.
Synonyms: Anti-alpha-1-antichymotrypsin; Anti-Aact; Anti-Act; Anti-Serpin peptidase inhibitor, clade a (alpha-1 antiproteinase, antitrypsin), member 3
MDL Number: MFCD00162119
Storage: -20C
Application: All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project (www.proteinatlas.org)and as a result, are supported by the most extensive characterization in the industry. The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Biochem Physiol Actions: a1-antichymotrypsin (ACT) is an a-globulin glycoprotein that is a member of the serpin superfamily and is encoded by the SERPINA3 gene in humans. Its expression is higher in prostate cancer than in benign prostatic hyperplasia. The serine protease has been found to be associated with several diseases such as chronic obstructive pulmonary disease (COPD), Parkinson's disease (PD), Alzheimer's disease (AD), stroke, cystic fibrosis, cerebral haemorrhage and multiple system atrophy. The encoded protein forms a complex with toxic ß-amyloid (Aß). The gene expression is induced by cytokines. ACT inhibits serine proteases, such as pancreatic chymotrypsin, leukocyte cathepsin G, mast cell chymases, human glandular kallikrein 2, kallikrein 3, and pancreatic cationic elastase. The levels of circulating ACT increases with inflammation. It also has the ability to bind to DNA unlike other serpins.
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