Analytical Data
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Gene name
HAO2
- Application
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Alternative Names
HAO2；HAOX2；2-Hydroxyacid oxidase 2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NYQ3
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Expression Region
2-351aa
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AA Sequence
SLVCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRY LRDVSEVDTRTTIQGEEISAPICIAPTGFHCLVWPDGEMSTARAAQAAGI CYITSTFASCSLEDIVIAAPEGLRWFQLYVHPDLQLNKQLIQRVESLGFK ALVITLDTPVCGNRRHDIRNQLRRNLTLTDLQSPKKGNAIPYFQMTPIST SLCWNDLSWFQSITRLPIILKGILTKEDAELAVKHNVQGIIVSNHGGRQL DEVLASIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLGR PILWGLACKGEHGVKEVLNILTNEFHTSMALTGCRSVAEINRNLVQFSRL
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Molecular Weight
55 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
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.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
HAO2 (Hydroxyacid oxidase 2) is an essential enzyme involved in various metabolic processes, particularly in ammonia oxidation and the regulation of cellular reactive oxygen species. Research into HAO2 has gained prominence due to its implications in both fundamental biology and potential therapeutic applications. The enzyme participates in the enzymatic pathway that converts L-amino acids into keto acids while producing hydrogen peroxide as a byproduct. This enzymatic activity is crucial for maintaining metabolic homeostasis. Moreover, dysregulation of HAO2 has been correlated with various diseases, including metabolic disorders and certain malignancies. Understanding the structure-function relationship of HAO2 can provide insights into its role in cellular metabolism and its potential as a target for drug development. Recent studies have utilized advanced techniques such as X-ray crystallography and molecular dynamics simulations to elucidate the enzyme's mechanism and substrate specificity. Identifying small molecules that can modulate HAO2 activity is an ongoing research focus, as such compounds could serve as novel therapeutic agents. Overall, the study of HAO2 is significant for comprehending metabolic pathways and offers potential avenues for medical intervention in disease contexts where HAO2 plays a critical role.
