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>   home   >   Products   >   Proteins   >   Human CellExp SERPINA1 /A1AT, human recombinant protein   

Human CellExp SERPINA1 /A1AT, human recombinant protein

SerpinA1, PI, A1A, AAT, PI1, A1AT, MGC9222, PRO2275, MGC23330,alpha1AT, SPAAT

     
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Product info
Primary Accession P01009
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.
Additional Info
Gene ID 5265
Gene Symbol SERPINA1
Other Names SerpinA1, PI, A1A, AAT, PI1, A1AT, MGC9222, PRO2275, MGC23330,alpha1AT, SPAAT
Gene Source Human
Source HEK 293 cells
Assay&Purity SDS-PAGE; ≥95%
Assay2&Purity2 HPLC;
Recombinant Yes
Target/Specificity SERPINA1
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.
Format Lyophilized powder
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.
Citations (0)
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Background

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).

References

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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Discontinued
Cat# PBV10865r-10
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