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AB113144

Recombinant Human HAO1/GOX protein

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(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

1 Images
SDS-PAGE - Recombinant Human HAO1/GOX protein (AB113144)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human HAO1/GOX protein (AB113144)

15% SDS-PAGE analysis of ab113144 (3μg)

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

DDDDK tag N-Terminus His tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q9UJM8

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 20% Glycerol (glycerin, glycerine), 2.92% Sodium chloride, 0.32% Tris HCl

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Product details

Protein previously labeled as HAO1.

Sequence info

[{"sequence":"MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWGSMLPRLICINDYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAETDLSTSVLGQRVSMPICVGATAMQRMAHVDGELATVRACQSLGTGMMLSSWATSSIEEVAEAGPEALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDTPYLGNRLDDVRNRFKLPPQLRMKNFETSTLSFSPEENFGDDSGLAAYVAKAIDPSISWEDIKWLRRLTSLPIVAKGILRGDDAREAVKHGLNGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVGRPIVWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVRKNPLAVSKI","proteinLength":"Full Length","predictedMolecularWeight":"45 kDa","actualMolecularWeight":null,"aminoAcidEnd":370,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q9UJM8","tags":[{"tag":"DDDDK","terminus":"N-Terminus"},{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The enzyme HAO1 also known as GOX (glycolate oxidase) functions by catalyzing the oxidation of glycolate to glyoxylate generating hydrogen peroxide in peroxisomes. The molecular mass of HAO1 is approximately 43 kDa. It is expressed in several tissues with high levels found in liver and kidney. The protein may also be referred to as alpha GOX which highlights its identity and specialization within oxidase family.
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.

Mutations and dysfunctions in HAO1 have links to primary hyperoxaluria type 1 a disease characterized by excessive production and build-up of oxalate leading to kidney stones and renal failure. The interplay with proteins like alanine:glyoxylate aminotransferase which helps detoxify glyoxylate is important in these conditions. This disorder highlights the importance of proper glycolate metabolism and its regulation in maintaining health.

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

Product protocols

Target data

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).
See full target information HAO1

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Scientific reports 6:34060 PubMed27670739

2016

High throughput cell-based assay for identification of glycolate oxidase inhibitors as a potential treatment for Primary Hyperoxaluria Type 1.

Applications

Unspecified application

Species

Unspecified reactive species

Mengqiao Wang,Miao Xu,Yan Long,Sonia Fargue,Noel Southall,Xin Hu,John C McKew,Christopher J Danpure,Wei Zheng
View all publications

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