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C533

Recombinant Human Serpin A1/a1-Antitrypsin

10ug

1200

1080

现货

国产

C533

Recombinant Human Serpin A1/a1-Antitrypsin

50ug

3520

3168

现货

国产

C533

Recombinant Human Serpin A1/a1-Antitrypsin

500ug

12320

11088

现货

国产

C533

Recombinant Human Serpin A1/a1-Antitrypsin

1mg

17600

15840

现货

国产

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  • Catalog# C533
    Source Human Cells
    Description Recombinant Human Serpin A1 produced by transfected human cells is a secreted protein with sequence (Glu25-Lys418) of Human SERPIN A1 fused with a polyhistidine tag at the C-terminus.
    Names Alpha-1-Antitrypsin, Alpha-1 Protease Inhibitor, Alpha-1-Antiproteinase, Serpin A1, SERPINA1, AAT, PI
    Accession # P01009
    Formulation Lyophilized from a 0.2 μm filtered solution of 20mM TrisHCl, 150mM NaCl, 2mM CaCl2, pH 7.5
    Shipping The product is shipped at ambient temperature.
    Reconstitution Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
    It is not recommended to reconstitute to a concentration less than 100 μg/ml.
    Dissolve the lyophilized protein in 1X PBS.
    Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
    Storage Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks.
    Reconstituted protein solution can be stored at 4-7°C for 2-7 days.
    Aliquots of reconstituted samples are stable at < -20°C for 3 months.
    Purity Greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE.
    Endotoxin Less than 0.1 ng/µg (1 IEU/µg).
    Amino Acid Sequence
    EDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLS LGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKF LEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWE RPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKL QHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEA PLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIDQNTKSPLFMGKVVN PTQKVDHHHHHH
    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.