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. ||Source:|Recombinant corresponding to human HAGH, fused to His-tag at N-terminus, expressed in E. coli.||Molecular Weight:|~31.4kD||Sequences of Amino Acids:|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||Enzyme Activity: |Specific activity is > 500 units/mg, and is defined as the amount of enzyme that reduces 1.0 umole of 5,5 -Dithiobis(2-nitrobenzoic acid) (DTNB) with reduced glutathione per minute at pH 7.5 at 37°C.||Storage and Stability:|May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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