A1AT – Alpha 1 Antitrypsin Antibodies

Affinity Biologicals, Inc. manufactures a broad range of A1AT – Alpha 1 Antitrypsin Antibodies which can be found in the listing below.   Further information about each individual A1AT – Alpha 1 Antitrypsin Antibody is available by following the associated links.  Our A1AT – Alpha 1 Antitrypsin Antibodies are excellent for use in immunoassays where high sensitivity is required and are frequently the preferred reagent for immunopreciptaion techniques and activity neutralization assays.  These antibodies have proven to be extremely useful in the preparation of immune-adsorbent resins for use in immuno-depletion of specific proteins from plasma as well as immuno-affinity purification of proteins.  Affinity’s A1AT – Alpha 1 Antitrypsin Antibodies are manufactured for use in research applications.

Listing of A1AT – Alpha 1 Antitrypsin Antibodies

Description of Alpha 1-Antitrypsin

Alpha 1Antitrypsin (A1AT), also known as Alpha 1Proteinase inhibitor (A1PI), 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 A1AT 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. A1AT 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 A1AT is believed to be neutrophil elastase1,2, but A1AT is a broad-spectrum inhibitor for many serine proteinases and the main role of A1AT in vivo is likely that of a “backup” inhibitor and proteinase scavenger in fluids and tissues. Although the association rates of A1AT 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 A1AT occurs through proteolytic cleavage between Met358 and Ser359, which induces a conformational change in A1AT locking the enzyme into a stable, inactive 1:1 enzyme-inhibitor complex.

References and Reveiws

  1. Johnson D, Travis J; Oxidative Inactivation of Human α-1-Proteinase Inhibitor; JBC 254, pp4022-4026, 1979.
  2. Travis J, Johnson D; Human α-1-Proteinase Inhibitor; Methods in Enzymology, 80, pp 754-765, 1981.
  3. Heeb MJ, Griffin JH; Physiologic Inhibition of Human Activated Protein C by α-1-Trypsin Inhibitor; JBC 263, pp11613-11616, 1988.
  4. 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.