Recombinant Mouse Serpin A1a
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Documents del producto
Product specifications
| Category | Proteins and Peptides |
| Host | Mammalian Cells |
| Reactivity | Mouse |
| Observed MW | 50-60 kDa |
| Expression | Glu25-Lys413 |
| Purity | Greater than 95% as determined by SDS-PAGE. |
| Size 1 | 10μg |
| Size 2 | 50μg |
| Size 3 | 500μg |
| Size 4 | 1mg |
| Form | Liquid |
| Tested Applications | Western Blot, ELISA |
| Buffer | 0.2 μm filtered solution of 20 mM Tris, 150 mM NaCl, pH 8.0. |
| Availability | 7 days |
| Storage | The protein solution is stable at -80°C for 6 months after receipt, and for 3 months under sterile conditions after opening. Avoid repeated freeze/thaw cycle. |
| UniProt ID | AAH11040.1 |
| Alias | PI,A1A,AAT; PI1,A1AT,nNIF,PRO2275,alpha1AT,Alpha-1-antitrypsin,Alpha-1 protease inhibitor,Alpha-1-antiproteinase,Serpin A1 |
| Background | Protein SERPINA1 |
| Status | RUO |
| Note | Endotoxin: < 1 EU/µg as determined by LAL test. Tag : C-terminal His Tag |
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SERPINA1 antibody
The protein encoded by this gene is secreted and is a serine protease inhibitor whose targets include elastase, plasmin, thrombin, trypsin, chymotrypsin, and plasminogen activator. Defects in this gene can cause emphysema or liver disease. Several transcript variants encoding the same protein have been found for this gene.
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SERPINA1 is the gene for a protein called alpha-1-antitrypsin(AAT), which is a serine protease inhibitor whose targets include elastase, plasmin, thrombin, trypsin, chymotrypsin, and plasminogen activator. AAT is a glycoprotein synthesized primarily by hepatocytes, with smaller amountssynthesized by intestinal epithelial cells, neutrophils, pulmonary alveolar cells and macrophages. AAT is the most abundant, endogenous serine protease inhibitor in blood circulation and it has been implicated in regulating vital fluid phase biological events such as blood coagulation, fibrinolysis, complement activation, apoptosis, reproduction, tumor progression and inflammatory response. The primary function of AAT is thought to be the inactivation of neutrophil elastase and other endogenous serine proteases. Defects in SERPINA1 can cause emphysema or liver disease.
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