Analytical Data
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Gene name
AKR1B10
- Application
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Alternative Names
ARL-1 Aldose reductase-like Aldose reductase-related protein
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O60218
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Expression Region
1-316aa
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Molecular Weight
63 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
AKR1B10, a member of the aldo-keto reductase (AKR) superfamily, is a key enzyme involved in the metabolism of various endogenous and exogenous substrates, including steroids, drugs, and carbonyl compounds. Research on AKR1B10 has gained significant attention due to its potential implications in cancer progression, diabetes, and other metabolic disorders. Particularly, AKR1B10 has been found to be overexpressed in several types of cancer, where it may contribute to tumorigenesis by altering key metabolic pathways and facilitating the detoxification of reactive aldehydes. Furthermore, its enzymatic activity can affect the pharmacokinetics of certain drugs, leading to variations in therapeutic efficacy and toxicity. As a result, scientists are increasingly focused on characterizing the biochemical properties, substrate specificity, and regulatory mechanisms of AKR1B10. Understanding its function and regulation could provide insights into its role in disease pathology and could help identify potential therapeutic targets for intervention. Recent advances in recombinant protein technology have enabled the production and purification of AKR1B10 for detailed structural and functional studies, facilitating the exploration of its mechanisms of action and interactions with various ligands. Through these investigations, researchers aim to delineate the therapeutic potential of targeting AKR1B10 in relevant disease contexts, thereby contributing to the development of innovative strategies for treatment and management.
