Recombinant Human Serpin A1/alpha-1-Antitrypsin

Instruction Manual!

Product name:	Recombinant Human Serpin A1/alpha-1-Antitrypsin
Source:	Human Cells
Purity:	Greater than 95% as determined by reducing SDS-PAGE.
Buffer Formulation:	Lyophilized from a 0.2 μm filtered solution of 20mM TrisHCl, 150mM NaCl, 2mM CaCl2, pH 7.5.
Applications:	Applications:SDS-PAGE; WB; ELISA; IP.
Storage:	Avoid repeated freeze/thaw cycles. Store at 2-8 oC for one month. Aliquot and store at -80 oC for 12 months.
UOM:	100ug/50ug/200ug/1mg/1g

Source	Human Cells
Description	Recombinant Human Serpin 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.
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 ddH2O. 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 reducing SDS-PAGE.
Endotoxin	Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.
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.