Analytical Data
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Gene name
AKR1B10
- Application
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Alternative Names
AKR1B10；AKR1B11；Aldo-keto reductase family 1 member B10
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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
O60218
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Expression Region
1-316aa
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AA Sequence
MATFVELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKLWPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKSGDDLFPKDDKGNAIGGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLNKPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHKKTAAQVLIRFHIQRNVIVIPKSVTPARIVENIQVFDFKLSDEEMATILSFNRNWRACNVLQSSHLEDYPFNAEY
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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 (Aldo-Keto Reductase Family 1 Member B10) is a member of the aldo-keto reductase enzyme family, known for its role in metabolizing a variety of endogenous and exogenous substrates, including glucose and lipid-derived compounds. Elevated expression levels of AKR1B10 have been linked to several pathological conditions, including cancer, diabetes, and cardiovascular diseases, making it a potential target for therapeutic interventions. Research has shown that AKR1B10 plays a crucial role in the detoxification of reactive carbonyl species, thereby contributing to cellular protection against oxidative stress. Furthermore, its involvement in the metabolic pathway of prostaglandins and steroids suggests that AKR1B10 may influence inflammatory processes and hormonal regulation. Recent studies have focused on the structural and functional characterization of AKR1B10, utilizing recombinant protein technology to produce active enzyme variants for in vitro analyses. Understanding the catalytic mechanisms and substrate specificity of AKR1B10 is essential for elucidating its physiological roles and potential implications in disease pathways. The development of selective inhibitors or modulators of AKR1B10 could pave the way for novel therapeutic strategies aimed at mitigating its pathological effects, underscoring the significance of ongoing research into this enzyme's function and regulation.
