This (S)-2-hydroxy-acid oxidase enzyme exhibits broad substrate specificity, with a preference for oxidizing glycolate. The glycolate oxidation product, glyoxylate, is subsequently used by alanine-glyoxylate aminotransferase in the peroxisomal synthesis of glycine—a crucial step in detoxifying glyoxylate. Accumulation of glyoxylate can lead to oxalate formation and kidney stones. The enzyme can also oxidize glyoxylate and long-chain hydroxyacids like 2-hydroxyhexadecanoate and 2-hydroxyoctanoate, albeit less efficiently. While active with the artificial electron acceptor 2,6-dichlorophenolindophenol (DCIP) in vitro, oxygen (O₂) is the physiological electron acceptor, producing hydrogen peroxide (H₂O₂). It is inactive on L-lactate and 2-hydroxybutanoate.
| Product Name | Recombinant Human HAO1 Protein (N-Trx-6His) |
| Accession | Q9UJM8 |
| Purity | Greater than 95% as determined by reducing SDS-PAGE. (QC verified) |
| Endotoxin | Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test. |
| Host Species | Human |
| Gene | HAO1 |
| Source | E.coli |
| Protein Expression Range | Met1-Ile370 |
| Tag | N-Trx-6His |
| Molecular Mass | 58.6 KDa |
| Buffer | Supplied as a 0.2 μm filtered solution of PBS, pH 7.4. |
| Storage | Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles. |
