Recombinant Human HAO1/GOX protein
Be the first to review this product! Submit a review
|
(1 Publication)
Recombinant Human HAO1/GOX protein is a Human Full Length protein, in the 1 to 370 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE.
View Alternative Names
GOX1, HAO1, 2-Hydroxyacid oxidase 1, HAOX1, Glycolate oxidase, Glyoxylate oxidase, GO, GOX
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human HAO1/GOX protein (AB113144)
15% SDS-PAGE analysis of ab113144 (3μg)
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
HAO1 facilitates the metabolism of hydroxyl acids playing an important role in glyoxylate and dicarboxylate metabolism. It does not form part of a multi-protein complex but operates as a monomer maintaining cellular homeostasis of organic acids. By helping convert glycolate into a form that cells use or excrete HAO1 prevents the accumulation of compounds that can become toxic at elevated levels.
Pathways
Glycolate oxidase takes part in the glyoxylate cycle and photorespiration in plants which also has parallels in animal metabolism where it participates in handling waste products. HAO1 interacts within the network of metabolic pathways along with proteins like lactate dehydrogenase that facilitate the conversion of chemical compounds. It plays a role in broader metabolomic balancing acts that maintain overall organismal homeostasis.
Specifications
Form
Liquid
Additional notes
ab113144 was purified using conventional chromatography.
General info
Function
Broad substrate specificity (S)-2-hydroxy-acid oxidase that preferentially oxidizes glycolate (PubMed : 10777549, PubMed : 10978532, PubMed : 17669354, PubMed : 18215067). The glyoxylate produced by the oxidation of glycolate can then be utilized by alanine-glyoxylate aminotransferase for the peroxisomal synthesis of glycine; this pathway appears to be an important step for the detoxification of glyoxylate which, if allowed to accumulate, may be metabolized to oxalate with formation of kidney stones (PubMed : 10978532, PubMed : 17669354). Can also catalyze the oxidation of glyoxylate, and long chain hydroxyacids such as 2-hydroxyhexadecanoate and 2-hydroxyoctanoate, albeit with much lower catalytic efficiency (PubMed : 10777549, PubMed : 17669354, PubMed : 18215067). Active in vitro with the artificial electron acceptor 2,6-dichlorophenolindophenol (DCIP), but O2 is believed to be the physiological electron acceptor, leading to the production of H2O2 (PubMed : 10777549, PubMed : 10978532, PubMed : 17669354, PubMed : 18215067). Is not active on L-lactate and 2-hydroxybutanoate (PubMed : 10777549).
Sequence similarities
Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.
Subcellular localisation
Peroxisome
Target data
Publications (1)
Recent publications for all applications. Explore the full list and refine your search
Scientific reports 6:34060 PubMed27670739
2016
Applications
Unspecified application
Species
Unspecified reactive species
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com