Recombinant human Hydroxyacid Oxidase-1/HAO-1 protein

Specific activity is > 3, 000pmol/min/ug, and defined as the amount of enzyme that oxidize glyoxylate at pH 8.0 at 25C.

MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMLPR LICINDYEQH AKSVLPKSIY DYYRSGANDE ETLADNIAAF SRWKLYPRML RNVAETDLST SVLGQRVSMP ICVGATAMQR MAHVDGELAT VRACQSLGTG MMLSSWATSS IEEVAEAGPE ALRWLQLYIY KDREVTKKLV RQAEKMGYKA IFVTVDTPYL GNRLDDVRNR FKLPPQLRMK NFETSTLSFS PEENFGDDSG LAAYVAKAID PSISWEDIKW LRRLTSLPIV AKGILRGDDA REAVKHGLNG ILVSNHGARQ LDGVPATIDV LPEIVEAVEG KVEVFLDGGV RKGTDVLKAL ALGAKAVFVG RPIVWGLAFQ GEKGVQDVLE ILKEEFRLAM ALSGCQNVKV IDKTLVRKNP LAVSKI

HAO1, also known as glycolate oxidase, is a member of the superfamily of the alpha hydroxy acid oxidases (HAO) enzymes. It catalyzes the FMN mediated oxidation of glycolate to glyoxylate and glyoxylate to oxalate with reduction of oxygen to hydrogen peroxide. It is most highly expressed in liver and pancreas and is most active on twocarbon substrates such as glycolate. Recently, it has been identified as a major contributor to hyperoxaluria, a disorder in which large deposits of calcium oxalate form kidney stones. Recombinant human HAO1 protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography.

< 1 EU per 1ug of protein (determined by LAL method)

Liquid in. 20mM Tris-HCl buffer (pH 8.0) containing 20% glycerol, 0.5M NaCl

Pennati A., et al. (2009) J. Biol. Chem. 284:31214.