Analytical Data
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Gene name
cyp102A1
- Application
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Alternative Names
(Cytochrome P450(BM-3))(Cytochrome P450BM-3)(Fatty acid monooxygenase)(Flavocytochrome P450 BM3)(Cytochrome P450 102A1)(NADPH--cytochrome P450 reductase)
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Species
Bacillus megaterium
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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
P14779
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Expression Region
2-472aa
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Molecular Weight
61.2 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
CYP102A1, a cytochrome P450 enzyme derived from the bacterium *Bacillus subtilis*, has garnered significant interest in biochemical and biotechnological research due to its unique properties and potential applications. This enzyme is known for its capability to catalyze various oxidative reactions, crucial for metabolic processes, including the hydroxylation of fatty acids and steroids. The study of CYP102A1 is particularly relevant in the context of biocatalysis, where it serves as a model system for understanding P450 enzyme function and for developing sustainable industrial processes. Unlike many eukaryotic P450 enzymes, CYP102A1 is more stable and exhibits higher activity under a range of conditions, making it an attractive candidate for enzymatic applications in organic synthesis, drug metabolism, and environmental remediation. Furthermore, advances in recombinant protein expression technologies have enabled the production and characterization of CYP102A1, paving the way for its functional engineering. Research exploring the structure-function relationships and enzyme kinetics of CYP102A1 has the potential to enhance its catalytic efficiency and substrate specificity, leading to innovations in green chemistry. Overall, the investigation of CYP102A1 not only contributes to the fundamental understanding of P450 enzymes but also opens avenues for practical applications in biotechnology and pharmaceutical industries.
