Analytical Data
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Gene name
CBR3
- Application
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Alternative Names
SDR21C2; Short Chain Dehydrogenase/Reductase Family 21C,Member 2; NADPH-dependent carbonyl reductase 3
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O75828
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Expression Region
Met1~Trp277
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Molecular Weight
40kDa
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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
CBR3 (Carbonyl Reductase 3) is a member of the aldo-keto reductase superfamily, playing a crucial role in the metabolic processes involving carbonyl compounds. Its importance has been underscored by research indicating its involvement in the detoxification of xenobiotics and the metabolism of various endogenous substrates, which can influence drug efficacy and toxicity. Furthermore, CBR3 has been linked to various pathological conditions, including cancer and neurodegenerative diseases, as it modulates the levels of reactive oxygen species and participates in cellular redox homeostasis. Recent studies have explored the enzyme's structural and functional characteristics, revealing insights into its substrate specificity and regulatory mechanisms. The investigation of CBR3 at the protein level, including the assessment of its recombinant forms, has become pivotal for understanding its physiological relevance and potential therapeutic applications. Recombination techniques enable the production of CBR3 in a controlled environment, allowing for detailed biochemical analyses, structure-function relationship studies, and the development of inhibitors that could serve as novel drugs. Overall, the study of CBR3 not only enhances our understanding of this enzyme's role in human health and disease but also opens new avenues for pharmacological intervention in conditions associated with dysregulated carbonyl metabolism.
