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

カタログ番号 TMPJ-00505
別名: 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.

All products from TargetMol are for Research Use Only. Not for Human or Veterinary or Therapeutic Use.
Serpin A1 Protein, Human, Recombinant (aa 25-418, His)
パッケージサイズ 在庫状況 単価(税別)
10 μg 約5 days ¥ 42,500
50 μg 約5 days ¥ 125,000
500 μg 約5 days ¥ 436,000
1 mg 約5 days ¥ 626,500
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生物学的特性に関する説明
Technical Params
Product Properties
説明 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 Host HEK293 Cells
Tag C-6xHis
Accession Number AAH11991.1
別名 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 Glu25-Lys418
Protein Purity Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
分子量 50-65 KDa (reducing condition)
Endotoxin < 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Formulation Lyophilized from a solution filtered through a 0.22 μm filter, containing 20 mM Tris-HCl, 150 mM NaCl, 2 mM CaCl<sub>2</sub>, pH 7.5.
Reconstitution Reconstitute the lyophilized protein in distilled water. The product concentration should not be less than 100 μg/ml. Before opening, centrifuge the tube to collect powder at the bottom. After adding the reconstitution buffer, avoid vortexing or pipetting for mixing.
Stability & Storage

Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at-80℃. For reconstituted proteinsolutions, the solution can be stored at -20°c to -80'c for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.

Shipping

In general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry ice.

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.

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