|Calculated MW||53.3 kDa|
|Other Names||6PGD, PGD|
|Sequence||MGSSHHHHHH SSGLVPRGSH MAQADIALIG LAVMGQNLIL NMNDHGFVVC AFNRTVSKVD DFLANEAKGT KVVGAQSLKE MVSKLKKPRR IILLVKAGQA VDDFIEKLVP LLDTGDIIID GGNSEYRDTT RRCRDLKAKG ILFVGSGVSG GEEGARYGPS LMPGGNKEAW PHIKTIFQGI AAKVGTGEPC CDWVGDEGAG HFVKMVHNGI EYGDMQLICE AYHLMKDVLG MAQDEMAQAF EDWNKTELDS FLIEITANIL KFQDTDGKHL LPKIRDSAGQ KGTGKWTAIS ALEYGVPVTL IGEAVFARCL SSLKDERIQA SKKLKGPQKF QFDGDKKSFL EDIRKALYAS KIISYAQGFM LLRQAATEFG WTLNYGGIAL MWRGGCIIRS VFLGKIKDAF DRNPELQNLL LDDFFKSAVE NCQDSWRRAV STGVQAGIPM PCFTTALSFY DGYRHEMLPA SLIQAQRDYF GAHTYELLAK PGQFIHTNWT GHGGTVSSSS YNA|
|Storage||-20°C;In 20 mM Tris-HCl buffer (pH8.0) containing 1mM DTT, 0.1M Nacl, 10% glycerol|
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Provided below are standard protocols that you may find useful for product applications.
PGD (Phosphogluconate dehydrogenase), also known as 6PGD, is a 483 amino acid enzyme that is involved in the pentose phosphate shunt. Pentose is required for nucleic acid biosynthesis and the pentose phosphate cycle is a major source of NADPH. PGD deficiency increases the level of erythrocyte pyruvate kinase (PK) activity and reduces glutathione synthetase (GSH), resulting in hemolysis. Defects in PGD are generally asymptomatic and are inherited in an autosomal dominant fashion. Recombinant human PGD protein, fused to His tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques
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