|Calculated MW||35.2 kDa (313 aa, 1-289 aa + His Tag)|
|Other Names||Inorganic pyrophosphatase, IOPPP, PP, PP1, SID6-8061|
|Results||Specific activity is >28,000 pmoles/min/ µg|
|Sequence||MGSSHHHHHH SSGLVPRGSH MGSHMSGFST EERAAPFSLE YRVFLKNEKG QYISPFHDIP IYADKDVFHM VVEVPRWSNA KMEIATKDPL NPIKQDVKKG KLRYVANLFP YKGYIWNYGA IPQTWEDPGH NDKHTGCCGD NDPIDVCEIG SKVCARGEII GVKVLGILAM IDEGETDWKV IAINVDDPDA ANYNDINDVK RLKPGYLEAT VDWFRRYKVP DGKPENEFAF NAEFKDKDFA IDIIKSTHDH WKALVTKKTN GKGISCMNTT LSESPFKCDP DAARAIVDAL PPPCESACTV PTDVDKWFHH QKN|
|Storage||-20°C; 0.5 mg/ml solution in 20 mM Tris-HCl buffer (pH 8.0) containing 20% glycerol, 200 mM NaCl and 2 mM DTT|
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Provided below are standard protocols that you may find useful for product applications.
PPA1 (Pyrophosphatase) belongs to the PPase family. This protein is an enzyme that catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. The hydrolysis of inorganic pyrophosphate (PPi) to two phosphate ions is utilized in many biochemical pathways to render reactions effectively irreversible. Inorganic pyrophosphatase catalyzes this hydrolysis reaction in the early steps of lipid degradation, a prominent example of this phenomenon. By promoting the rapid hydrolysis of pyrophosphate (PPi), Inorganic pyrophosphatase provides the driving force for the activation of fatty acids destined for oxidation. Recombinant human PPA1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.
Fairchild T.A.,et al.Biochim. Biophys. Acta 1447:133-136(1999).
Saito T.,et al.Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
Kanni L.,et al.Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
Dai F.Y.,et al.Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
Hu R.-M.,et al.Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
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