SERPINA1 antibody

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Description
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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Product specifications
Category | Primary Antibodies |
Immunogen Target | serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1 (SERPINA1) |
Host | Rabbit |
Reactivity | Human, Mouse, Rat |
Recommended Dilution | WB: 1:500 - 1:2000; IHC: 1:50 - 1:200 |
Clonality | polyclonal |
Conjugation | Unconjugated |
Isotype | IgG |
Observed MW | 45 kDa, 50 kDa |
Purity | ≥95% as determined by SDS-PAGE |
Purification | Immunogen affinity purified |
Size 1 | 100µg |
Form | liquid |
Tested Applications | ELISA, IHC, WB |
Storage | PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20℃ for 12 months (Avoid repeated freeze / thaw cycles.) |
UniProt ID | P01009 |
Gene ID | 5265 |
Alias | PI,A1A,AAT; PI1,A1AT,nNIF,PRO2275,alpha1AT,Alpha-1-antitrypsin,Alpha-1 protease inhibitor,Alpha-1-antiproteinase,Serpin A1 |
Background | Antibody anti-SERPINA1 |
Status | RUO |
Note | Mol. Weight 45 kDa, 50 kDa |
Descripción
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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 antibody
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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