Serpin A1 is a prototype member of the Serpin superfamily of the serine protease inhibitors. As one of the most abundant proteinase inhibitors in the circulation, it is synthesized in hepatocytes, and to a lesser extent, in macrophages as well as intestinal epithelial cell lines and secreted as the abundant proteinase inhibitor in the circulation whose targets include elastase, plasmin, thrombin, trypsin, chymotrypsin, and plasminogen activator. Point mutations in the native SerpinA1 variants result in Serpin A1 deficiency, and consequently lead to several clinical complications such as pulmonary emphysema, juvenile hepatitis, cirrhosis, and hepatocellular carcinoma. For example, the Z variants (Glu342 to Lys) forms intracellular inclusion bodies, is not secreted, and leads to a severe SerpinA1 deficiency. Accordingly, Serpin A1 deficiency in circulation is associated with emphysema or liver disease.
Pack Size | Availability | Price/USD | Quantity |
---|---|---|---|
10 μg | 5 days | $ 184.00 | |
50 μg | 5 days | $ 545.00 | |
500 μg | 5 days | $ 1,900.00 | |
1 mg | 5 days | $ 2,730.00 |
Description | Serpin A1 is a prototype member of the Serpin superfamily of the serine protease inhibitors. As one of the most abundant proteinase inhibitors in the circulation, it is synthesized in hepatocytes, and to a lesser extent, in macrophages as well as intestinal epithelial cell lines and secreted as the abundant proteinase inhibitor in the circulation whose targets include elastase, plasmin, thrombin, trypsin, chymotrypsin, and plasminogen activator. Point mutations in the native SerpinA1 variants result in Serpin A1 deficiency, and consequently lead to several clinical complications such as pulmonary emphysema, juvenile hepatitis, cirrhosis, and hepatocellular carcinoma. For example, the Z variants (Glu342 to Lys) forms intracellular inclusion bodies, is not secreted, and leads to a severe SerpinA1 deficiency. Accordingly, Serpin A1 deficiency in circulation is associated with emphysema or liver disease. |
Species | Human |
Expression System | Human Cells |
Tag | C-6His |
Accession Number | AAH11991.1 |
Synonyms | Alpha-1-Antiproteinase, α-1-Antiproteinase, SERPINA1, Serpin A1, AAT, Alpha-1 Protease Inhibitor, Alpha-1-Antitrypsin, PI, α-1-Antitrypsin, α-1 Protease Inhibitor |
Amino Acid | Glu25-Lys418 |
Construction | Recombinant Human Serine Protease Inhibitor-clade A1 is produced by our Mammalian expression system and the target gene encoding Glu25-Lys418 is expressed with a 6His tag at the C-terminus. |
Protein Purity | Greater than 95% as determined by reducing SDS-PAGE. (QC verified) |
Molecular Weight | 50-65 KDa, reducing conditions |
Endotoxin | Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test. |
Formulation | Lyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, 2mM CaCl<sub>2</sub>, pH 7.5. |
Reconstitution | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
Stability & Storage |
Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
Shipping |
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below. |
Research Background | Serpin A1 is a prototype member of the Serpin superfamily of the serine protease inhibitors. As one of the most abundant proteinase inhibitors in the circulation, it is synthesized in hepatocytes, and to a lesser extent, in macrophages as well as intestinal epithelial cell lines and secreted as the abundant proteinase inhibitor in the circulation whose targets include elastase, plasmin, thrombin, trypsin, chymotrypsin, and plasminogen activator. Point mutations in the native SerpinA1 variants result in Serpin A1 deficiency, and consequently lead to several clinical complications such as pulmonary emphysema, juvenile hepatitis, cirrhosis, and hepatocellular carcinoma. For example, the Z variants (Glu342 to Lys) forms intracellular inclusion bodies, is not secreted, and leads to a severe SerpinA1 deficiency. Accordingly, Serpin A1 deficiency in circulation is associated with emphysema or liver disease. |
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Please read the User Guide of Recombinant Proteins for more specific information.
Serpin A1 Protein, Human, Recombinant (aa 25-418, His) Alpha-1-Antiproteinase α-1-Antiproteinase SERPINA 1 a-1 Protease Inhibitor SERPINA1 Serpin A1 AAT Alpha-1 Protease Inhibitor Alpha-1-Antitrypsin PI α-1-Antitrypsin a-1-Antiproteinase SERPINA-1 a-1-Antitrypsin α-1 Protease Inhibitor recombinant recombinant-proteins proteins protein