Analytical Data
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Gene name
cyp c 1.02
- Application
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Alternative Names
/
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Species
Cyprinus carpio
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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
Q8UUS2
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Expression Region
1-109aa
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Molecular Weight
27.6 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
CYP C 1.02, a member of the cytochrome P450 family, has garnered significant attention in pharmacological and biochemical research due to its pivotal role in drug metabolism and biotransformation processes. The cytochrome P450 enzymes are integral to the oxidative metabolism of a wide variety of substrates, including pharmaceuticals, environmental pollutants, and endogenous compounds. This particular isoenzyme is notable for its unique substrate specificity and catalytic efficiency, which can vary significantly across different species and individual organisms. Understanding CYP C 1.02 is critical for elucidating its involvement in detoxification pathways and the metabolic clearance of therapeutic agents, thus providing insights into drug-drug interactions and individual variability in drug responses. Additionally, given the increasing prevalence of polymorphisms and mutations in drug-metabolizing enzyme genes, research on CYP C 1.02 also holds promise for personalized medicine approaches, allowing for the optimization of treatment regimens based on an individual's metabolic profile. Studies have demonstrated that alterations in CYP C 1.02 activity can lead to significant pharmacokinetic changes, impacting drug efficacy and safety. Consequently, ongoing investigations aim to characterize the substrate specificity, expression patterns, and regulatory mechanisms of CYP C 1.02, contributing to the broader understanding of its functional role in human health and disease. The findings from such research may also inform the development of new therapeutic agents and strategies for minimizing adverse drug reactions. Overall, the study of CYP C 1.02 is essential for advancing our knowledge of metabolic enzymes and their implications in pharmacotherapy and toxicology.
