Description
Alpha-1-Antitrypsin A1AT Polylconal Antibody
Affinity’s Alpha-1-Antitrypsin A1AT Polyclonal Antibody is the base level of our A1AT antibody family. The purity of IgG is typically 90% and is provided in a solution of HEPES buffered saline containing 50% glycerol (v/v). The titre is essentially the same as the starting antiserum and each vial typically contains the amount of IgG recovered from one milliliter of antiserum. This Alpha-1-Antitrypsin A1AT Polyclonal Antibody is generally intended for use in applications such as immuno-precipitation, immuno-electrophoresis, immuno-depletion and activity neutralization assays.
Product Code: SA1AT-IG
Retail Product Size: 10 mg vial
Host Animal: Sheep anti-human Alpha-1-Antitrypsin Polyclonal Antibody
Species Cross Reactivity: View Chart
Product Datasheet: A1AT Alpha-1-antitrypsin Polyclonal Antibody, purified anti-human sheep IgG
Description of Alpha 1-Antitrypsin
Alpha 1Antitrypsin (α1AT), also known as Alpha 1Proteinase inhibitor (α1PI), is the most abundant protease inhibitor in blood and a member of the SERPIN family of proteinase inhibitors. Serum levels are typically 1.3 mg/ml (25 μM) but α1AT is an acute phase protein and concentrations can rise four-fold during inflammatory episodes or tissue injury. Low levels in circulation have been associated with pulmonary disease such as emphysema. α1AT is a single chain molecule with a mass of 52,000 daltons that is produced primarily in the liver and to a lesser extent by blood monocytes and intestinal epithelium. Based on association rates, the primary target enzyme for α1AT is believed to be neutrophil elastase1,2, but α1AT is a broad-spectrum inhibitor for many serine proteinases and the main role of α1AT in vivo is likely that of a “backup” inhibitor and proteinase scavenger in fluids and tissues. Although the association rates of α1AT with other enzymes are lower, the high concentration in plasma makes it an important inhibitor of activated Protein C, activated FXI, thrombin and plasmin1-4. Enzyme inhibition by α1AT occurs through proteolytic cleavage between Met358 and Ser359, which induces a conformational change in α1AT locking the enzyme into a stable, inactive 1:1 enzyme-inhibitor complex.
References and Reviews
- Johnson D, Travis J; Oxidative Inactivation of Human α-1-Proteinase Inhibitor; JBC 254, pp4022-4026, 1979.
- Travis J, Johnson D; Human α-1-Proteinase Inhibitor; Methods in Enzymology, 80, pp 754-765, 1981.
- Heeb MJ, Griffin JH; Physiologic Inhibition of Human Activated Protein C by α-1-Trypsin Inhibitor; JBC 263, pp11613-11616, 1988.
- Scott CF, Schapira M, James HL, Cohen AB, Colman RW; The Inactivation of Factor XIa by plasma protease inhibitors: Predominant role of α1protease inhibitor and protective effect of high molecular weight kininogen. J Clin Invest 69, pp 844, 1982.
