Name :
Recombinant Human HAO1 Protein (His Tag)
Biological Activity :
Background :
Hydroxyacid oxidase 1, also known as Glycolate oxidase, HAO1, and GOX1, is a member of the FMN-dependent alpha-hydroxy acid dehydrogenase family. HAO1 / GOX1 has 2-hydroxyacid oxidase activity. It is most active on the 2-carbon substrate glycolate, but is also active on 2-hydroxy fatty acids, with high activity towards 2-hydroxy palmitate and 2-hydroxy octanoate. HAO1 / GOX1 is a liver-specific peroxisomal enzyme that oxidizes glycolate to glyoxylate with the concomitant production of H2O2. In Hao1 messenger RNA (mRNA), an iron-responsive element (IRE) homologous to the sequence recognized by iron regulatory proteins (IRP), key regulators of iron homeostasis, is present. Mammalian HAO1 / GOX1 is a peroxisomal protein and that the C-terminal sequence SKI acts as the targeting signal. Down-regulation of HAO1 / GOX1 expression during oxidative stress may provide a mechanism to prevent excessive H2O2 formation in liver peroxisomes and may represent the prototype of a poorly recognized but potentially relevant response to an oxidative injury involving down-regulation of ROS-producing enzymes.
Biological Activity :
Testing in progress
Expression Host :
Human
Source :
E. coli
Tag :
Protein Accession No. :
NP_060015.1
NCBI Gene ID :
Synonyms :
Synonyms :
hydroxyacid oxidase (glycolate oxidase) 1
Amino Acid Sequence :
Molecular Weight :
The recombinant human HAO1 consisting of 376 amino acids and migrates as an 42 kDa band in SDS-PAGE under reducing conditions as predicted.
Purity :
> 97 % as determined by SDS-PAGE
State of Matter :
Product Concentration :
Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Endotoxin Level :
Please contact us for more information.
Protein Construction :
A DNA sequence encoding the native human HAO1 (NP_060015.1) (Leu 2-Ile 370) was expressed, with a polyhistide tag at the N-terminus.
Buffer Solution :
Lyophilized from sterile 20mM Tirs, 500mM NaCl, 10% glycerol, pH 8.0Please contact us for any concerns or special requirements. Normally 5 % – 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Synonyms :
GOX Protein, Human; GOX1 Protein, Human; HAOX1 Protein, Human HAO1 背景信息 Hydroxyacid oxidase 1, also known as Glycolate oxidase, HAO1, and GOX1, is a member of the FMN-dependent alpha-hydroxy acid dehydrogenase family. HAO1 / GOX1 has 2-hydroxyacid oxidase activity. It is most active on the 2-carbon substrate glycolate, but is also active on 2-hydroxy fatty acids, with high activity towards 2-hydroxy palmitate and 2-hydroxy octanoate. HAO1 / GOX1 is a liver-specific peroxisomal enzyme that oxidizes glycolate to glyoxylate with the concomitant production of H2O2. In Hao1 messenger RNA (mRNA), an iron-responsive element (IRE) homologous to the sequence recognized by iron regulatory proteins (IRP), key regulators of iron homeostasis, is present. Mammalian HAO1 / GOX1 is a peroxisomal protein and that the C-terminal sequence SKI acts as the targeting signal. Down-regulation of HAO1 / GOX1 expression during oxidative stress may provide a mechanism to prevent excessive H2O2 formation in liver peroxisomes and may represent the prototype of a poorly recognized but potentially relevant response to an oxidative injury involving down-regulation of ROS-producing enzymes.
References & Citations :
Jones J.M.et al., 2000, J. Biol. Chem. 275:12590-7. Recalcati,S. et al., 2001, J Cell Sci. 114 (Pt 9):1625-9. Recalcati,S. et al., 2003, Hepatology. 38 (5):1159-66. Murray M.S.et al., 2008, Biochemistry 47:2439-49. Bourhis J.M.et al., 2009, Acta Crystallogr. F 65:1246-53.
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