Human CellExp SERPINA1 /A1AT, human recombinant protein
SerpinA1, PI, A1A, AAT, PI1, A1AT, MGC9222, PRO2275, MGC23330，alpha1AT, SPAAT
|Calculated MW||The protein is fused with 6×His tag at the C-terminus, has a calculated MW of 45.1 kDa. The predicted N-terminus is Glu 25. DTT-reduced Protein migrates as 55-60 kDa due to glycosylation.|
|Other Names||SerpinA1, PI, A1A, AAT, PI1, A1AT, MGC9222, PRO2275, MGC23330，alpha1AT, SPAAT|
|Source||HEK 293 cells|
|Application Notes||Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 50 µg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 month. For extended storage, it is recommended to store at -20°C.|
|Storage||-20°C; Lyophilized from 0.22 µm filtered solution in PBS. Generally 5-8% Mannitol or trehalose is added as a protectant before lyophilization.|
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Provided below are standard protocols that you may find useful for product applications.
Serpin A1 also known as Alpha-1-antitrypsin (A1AT), serum trypsin inhibitor, alpha-1 proteinase inhibitor (A1PI), AAT, which belongs to the serpin family. Most serpins inactivate enzymes by binding to them covalently, requiring very high levels to perform their function. Like all serine protease inhibitors, A1AT has a characteristic secondary structure of beta sheets and alpha helices. Serpin A1 / A1AT is 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 of SerpinA1 inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin. Serpin A1 / A1AT protects tissues from enzymes of inflammatory cells, especially neutrophil elastase. Defects in SERPINA1 are the cause of alpha-1-antitrypsin deficiency (A1ATD).
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Nukiwa T.,et al.J. Biol. Chem. 261:15989-15994(1986).
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