| Product Name | Serpina9, 26-418aa, Mouse, Baculovirus |
|---|---|
| Description | Serpina9, also known as serpin A9, is a member of the Serpin superfamily of serine protease inhibitors. Serpins are the most broadly distributed superfamily of protease inhibitors that use a conformational change to inhibit target enzymes. They are known to inhibit serine proteases and some are known to inhibit caspases and papain-like cysteine proteases. Serpins are conformational labile and many of the disease-linked mutations of serpins result in misfolding or in pathogenic, inactive polymers. This protein shows inhibition towards trypsin, thrombin, and plasmin and binds DNA and heparin. Recombinant mouse Serpina9, fused to His-tag at C-terminus, was expressed in insect cell and purified by using conventional chromatography techniques. |
| Synonyms | Serpin A9, Serpin A9, 2310014L03Rik, AW049635, Centerin |
| Host | Virus |
| Molecular Weight |
59.9kDa (527aa) 35-70kDa (SDS-PAGE under reducing conditions) |
| Amino Acid Sequence | NPYNQESSHL PSMKKNPASQ VSPSNTRFSF LLYQRLAQEN PGQNILFSPV SISTSLAMLS LGARSATKTQ ILRTLGFNFT WVSEPTIHMG FEYLVRSLNK CHQGRELRMG SVLFIRKELQ LQATFLDRVK KLYGAKVFSE DFSNAATAQA QINSYVEKET KGKVVDVIQD LDSQTAMVLV NHIFFKANWT QPFSTANTNK SFPFLLSKGT TVHVPMMHQT ESFAFGVDKE LGCSILQMDY RGDAVAFFVL PGKGKMRQLE KSLSARRLRK WSRSLQKRWI KVFIPKFSIS ASYNLETILP KMGIRDAFNS NADFSGITKT HFLQVSKAAH KAVLDVSEEG TEAAAATTTK LIVRSRDTPS SIIAFKEPFL ILLLDKNTES VLFLGKVENP RKMLEHHHHH H |
| Tag | His-tag |
| Form | Liquid, in Phosphate Buffered Saline (pH 7.4) containing 10% glycerol. |
| Concentration | 0.25mg/ml (determined by Absorbance at 280nm) |
| Purity | > 85% by SDS-PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles. |
| References | Law RH., et al. (2006) Genome Biol. 7:216. Paterson MA., et al. (2007) Biochem J. 405:489-494. |
| Background | Serpina9, also known as serpin A9, is a member of the Serpin superfamily of serine protease inhibitors. Serpins are the most broadly distributed superfamily of protease inhibitors that use a conformational change to inhibit target enzymes. They are known to inhibit serine proteases and some are known to inhibit caspases and papain-like cysteine proteases. Serpins are conformational labile and many of the disease-linked mutations of serpins result in misfolding or in pathogenic, inactive polymers. This protein shows inhibition towards trypsin, thrombin, and plasmin and binds DNA and heparin. Recombinant mouse Serpina9, fused to His-tag at C-terminus, was expressed in insect cell and purified by using conventional chromatography techniques. |
| Supplier | ARP |
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