|Application ||WB, IHC-P, IP|
|Reactivity||Human, Monkey, Dog|
|Calculated MW||46737 Da|
|Dilution||IHC-P (10 µg/ml), WB (1:500 - 1:1000),|
|Other Names||SERPINA1, A1A, A1AT, AAT, Alpha 1 Antitrypsin, Alpha-1 protease inhibitor, Alpha-1-antiproteinase, Alpha-1-antitrypsin, Alpha1AT, PRO2275, Alpha-1-antitrypsin null, PI1, Serpin A1|
|Target/Specificity||Human SERPINA1 / Alpha 1 Antitrypsin|
|Reconstitution & Storage||PBS, pH 7.3, 1% BSA, 50% glycerol, 0.02% sodium azide. Store at -20°C. Minimize freezing and thawing.|
|Precautions||SERPINA1 / Alpha 1 Antitrypsin Antibody (clone 15H10) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin.|
|Cellular Location||Secreted. Endoplasmic reticulum. Note=The S and Z allele are not secreted effectively and accumulate intracellularly in the endoplasmic reticulum|
|Tissue Location||Ubiquitous. Expressed in leukocytes and plasma.|
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Provided below are standard protocols that you may find useful for product applications.
Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin.
Bollen A.,et al.DNA 2:255-264(1983).
Long G.L.,et al.Biochemistry 23:4828-4837(1984).
Rosenberg S.,et al.Nature 312:77-80(1984).
Ciliberto G.,et al.Cell 41:531-540(1985).
Nukiwa T.,et al.J. Biol. Chem. 261:15989-15994(1986).
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