Hydroxyacid oxidase 1 Protein, Mouse (His)

Hydroxy acid oxidase 1 (HAO1) is a multifunctional (S)-2-hydroxyacid oxidase with a strong preference for glycolate oxidation. This enzymatic process produces glyoxylic acid, an important precursor for the synthesis of glycine by alanine glyoxylate aminotransferase, which prevents glyoxylic acid accumulation and kidney stone formation. Hydroxyacid oxidase 1 Protein, Mouse (His) is the recombinant mouse-derived Hydroxyacid oxidase 1 protein, expressed by E. coli , with N-His labeled tag. The total length of Hydroxyacid oxidase 1 Protein, Mouse (His) is 370 a.a., with molecular weight of ~45.0 kDa.

Hydroxyacid oxidase 1 (HAO1) is a versatile (S)-2-hydroxy-acid oxidase with a broad substrate specificity, exhibiting a marked preference for glycolate oxidation. This enzymatic activity results in the production of glyoxylate, a crucial precursor essential for the peroxisomal synthesis of glycine by alanine-glyoxylate aminotransferase. This pathway plays a pivotal role in detoxifying glyoxylate, preventing its accumulation and the potential formation of kidney stones. HAO1 further displays the ability to catalyze the oxidation of glyoxylate and long-chain hydroxyacids, such as 2-hydroxyhexadecanoate and 2-hydroxyoctanoate. While active in vitro with the artificial electron acceptor 2,6-dichlorophenolindophenol (DCIP), it is believed that O2 serves as the physiological electron acceptor, leading to the production of H2O2. HAO1's multifaceted enzymatic capabilities underscore its significance in various metabolic pathways.

Mouse

E. coli

N-His

Q9WU19 (1M-370I)

15112  [NCBI]

MLPRLVCISDYEQHVRSVLQKSVYDYYRSGANDQETLADNIQAFSRWKLYPRMLRNVADIDLSTSVLGQRVSMPICVGATAMQCMAHVDGELATVRACQTMGTGMMLSSWATSSIEEVAEAGPEALRWMQLYIYKDREISRQIVKRAEKQGYKAIFVTVDTPYLGNRIDDVRNRFKLPPQLRMKNFETNDLAFSPKGNFGDNSGLAEYVAQAIDPSLSWDDITWLRRLTSLPIVVKGILRGDDAKEAVKHGVDGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIIWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVRKNPLAVSKI

Approximately 45.0 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.