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Serpin A1 Protein, Human, Recombinant (aa 25-418, His)

Catalog No. TMPJ-00505
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

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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Serpin A1 Protein, Human, Recombinant (aa 25-418, His)
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
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Biological Description
Technical Params
Product Properties
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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Keywords

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

 

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