|Calculated MW||31.4 kDa (284 aa, 1-260 aa + His Tag)|
|Other Names||Hydroxyacylglutathione hydrolase, GLO, GLX2, Glyoxalase II, HAGH1|
|Results||Specific activity is > 1.8 unit/ml|
|Sequence||MGSSHHHHHH SSGLVPRGSH MGSHMKVEVL PALTDNYMYL VIDDETKEAA IVDPVQPQKV VDAARKHGVK LTTVLTTHHH WDHAGGNEKL VKLESGLKVY GGDDRIGALT HKITHLSTLQ VGSLNVKCLA TPCHTSGHIC YFVSKPGGSE PPAVFTGDTL FVAGCGKFYE GTADEMCKAL LEVLGRLPPD TRVYCGHEYT INNLKFARHV EPGNAAIREK LAWAKEKYSI GEPTVPSTLA EEFTYNPFMR VREKTVQQHA GETDPVTTMR AVRREKDQFK MPRD|
|Storage||-20°C; 0.5 mg/ml solution in 20 mM Tris-HCl buffer (pH 8.0) containing 10% glycerol|
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Provided below are standard protocols that you may find useful for product applications.
HAGH is a member of the glyoxalase family and a thiolesterase which hydrolyses S-lactoyl-glutathione to reduced glutathione and D-lactate. This protein is a detoxifying enzyme of glycolysis byproduct methylglyoxal and a target of p63 and p73 and serves as a pro-survival factor of the p53 family. It exists only as a monomer and binds two zinc ions per subunit. Recombinant human HAGH protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography.
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Daniels R.J.,et al.Hum. Mol. Genet. 10:339-352(2001).
Martin J.,et al.Nature 432:988-994(2004).
Ridderstroem M.,et al.J. Biol. Chem. 271:319-323(1996).
Cordell P.A.,et al.J. Biol. Chem. 279:28653-28661(2004).
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