Analytical Data
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Gene name
Cyp3a13
- Application
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Alternative Names
CYPIIIA13
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Species
Mouse
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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
Q64464
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Expression Region
1-503aa
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Molecular Weight
73.5 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
CYP3A13 is a member of the cytochrome P450 family of enzymes, primarily known for its significant role in drug metabolism and the biotransformation of various xenobiotics, including pharmaceuticals and environmental chemicals. Unlike its more widely studied counterpart, CYP3A4, CYP3A13 exhibits distinct substrate specificity and expression patterns, which can lead to variations in metabolic responses among individuals. Research into CYP3A13 is particularly relevant in the context of pharmacogenetics, as genetic polymorphisms in this enzyme may influence drug efficacy and toxicity. Additionally, CYP3A13 has been implicated in the metabolic activation of certain procarcinogens, raising concerns about its involvement in cancer risk. The recombinant expression of CYP3A13 in heterologous systems such as bacteria, yeast, or mammalian cells has become a vital tool for studying its enzymatic functions, substrate interactions, and regulatory mechanisms. By elucidating the biochemical properties of CYP3A13 through recombinant techniques, researchers aim to better understand its physiological and pharmacological significance, paving the way for improved therapeutic strategies and personalized medicine approaches. These studies are crucial for advancing our knowledge of individual variability in drug response and the potential implications of CYP3A13 in clinical settings.
