Recombinant Human SerpinA1/A1AT Protein (His Tag)

Cat. No : CDRP-00553

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Target Information
Target Name	SerpinA1/A1AT
Synonyms	Alpha-1-Antitrypsin; Alpha-1 Protease Inhibitor; Alpha-1-Antiproteinase; Serpin A1; SERPINA1; AAT; PI; A1A; A1AT; AAT; alpha1AT; MGC23330; MGC9222; PI1; PRO2275
UniProt ID	P19438
Accession	AAH11991.1

Product Details
Expression Host	HEK293 Cells
Species	Human
Tag	C-6His
Molar Mass	45.4 kDa
Sequence	Gln 21-Pro 427

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.

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.

Properties
Purity	>90% as determined by reducing SDS-PAGE.
Formulation	Lyophilized from a 0.2 μm filtered solution of 20 mM Tris-HCl, 150 mM NaCl, 2 mM CaCl₂, pH7.5.
Reconstitution	Please refer to the printed manual for detailed information.
Shipping	This product is provided as lyophilized powder which is shipped with ice packs.
Storage	Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80 °C. Reconstituted protein solution can be stored at 4-8 °C for 2-7 days. Aliquots of reconstituted samples are stable at < -20 °C for 3 months.

! For research use only. Not intended for any clinical use.