Analytical Data
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Gene name
AKR1C2
- Application
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Alternative Names
3-alpha-HSD;3Chlordecone reductase homolog HAKRD;Dihydrodiol dehydrogenase 2 ;DD-2 ;DD2Dihydrodiol dehydrogenase/bile acid-binding protein ;DD/BABPTrans-1,2-dihydrobenzene-1,2-diol dehydrogenase (EC:1.3.1.20);Type III 3-alpha-hydroxysteroid dehydrogenase (EC:1.1.1.357)
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P52895
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Expression Region
1-323aa
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Molecular Weight
52.7 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
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Protein Description
AKR1C2, a member of the aldo-keto reductase (AKR) family, plays a crucial role in steroid metabolism and the regulation of various biological processes, including hormone signaling and drug metabolism. This enzyme is responsible for the reduction of ketones and aldehydes to their respective alcohols, which is vital for maintaining cellular homeostasis and energy balance. Its importance has gained attention in recent years due to its involvement in certain pathological conditions, such as cancer, diabetes, and cardiovascular diseases. Notably, AKR1C2 is implicated in the bioactivation of certain chemotherapeutic agents and in the resistance mechanisms against cancer therapies, making it a potential target for therapeutic intervention. The study of recombinant AKR1C2 proteins facilitates the understanding of the enzyme's structural and functional characteristics, enzymatic mechanisms, and interactions with substrates and inhibitors. By exploring the kinetics and substrate specificity of AKR1C2, researchers hope to unravel its role in various metabolic pathways and its potential as a biomarker for disease diagnosis and treatment responses. Furthermore, generating and characterizing recombinant proteins allows for detailed structure-function analyses that can lead to the development of selective inhibitors, contributing to more effective treatment strategies for diseases associated with dysregulated steroid metabolism and chemoresistance. Thus, AKR1C2 represents a significant target for research aimed at advancing our understanding of metabolic disorders and improving therapeutic approaches in oncology and other fields.
