Analytical Data
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Gene name
Akr1c13
- Application
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Species
Mouse
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8VC28
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Expression Region
1-323aa
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Molecular Weight
44.5 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
Akr1c13, a member of the aldo-keto reductase (AKR) superfamily, plays a critical role in the metabolism of steroids, drugs, and other xenobiotics. This enzyme is predominantly expressed in the liver and has been implicated in various physiological and pathological processes, including endocrine regulation, oxidative stress response, and cancer progression. Research on Akr1c13 has gained momentum due to its potential involvement in metabolic disorders and its role in the biotransformation of pharmaceuticals, which can affect drug efficacy and toxicity. Moreover, polymorphisms in the Akr1c13 gene have been associated with individual variations in drug metabolism and susceptibility to certain diseases. Understanding the structure-function relationships of Akr1c13 through recombinant protein studies can provide insights into its catalytic mechanisms and regulatory pathways. Additionally, exploring its interactions with different substrates and inhibitors could unveil new therapeutic targets for optimizing drug therapies, particularly in patients with altered metabolic profiles. Thus, the recombinant expression and characterization of Akr1c13 are essential for elucidating its biological significance and advancing precision medicine strategies.
