|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|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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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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