Analytical Data
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Gene name
cyp125
- Application
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Alternative Names
cyp125；cyp125A1；Steroid C26-monooxygenase
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P9WPP1
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Expression Region
1-433aa
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AA Sequence
MSWNHQSVEIAVRRTTVPSPNLPPGFDFTDPAIYAERLPVAEFAELRSAAPIWWNGQDPGKGGGFHDGGFWAITKLNDVKEISRHSDVFSSYENGVIPRFKNDIAREDIEVQRFVMLNMDAPHHTRLRKIISRGFTPRAVGRLHDELQERAQKIAAEAAAAGSGDFVEQVSCELPLQAIAGLLGVPQEDRGKLFHWSNEMTGNEDPEYAHIDPKASSAELIGYAMKMAEEKAKNPADDIVTQLIQADIDGEKLSDDEFGFFVVMLAVAGNETTRNSITQGMMAFAEHPDQWELYKKVRPETAADEIVRWATPVTAFQRTALRDYELSGVQIKKGQRVVMFYRSANFDEEVFQDPFTFNILRNPNPHVGFGGTGAHYCIGANLARMTINLIFNAVADHMPDLKPISAPERLRSGWLNGIKHWQVDYTGRCPVAH
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Molecular Weight
54.5 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
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Protein Description
CYP125 is a member of the cytochrome P450 superfamily, which plays a crucial role in the metabolism of various substrates, including drugs, steroids, and fatty acids. The study of CYP125 has garnered attention due to its distinct substrate specificity and its potential applications in bioremediation and drug development. This enzyme, originally isolated from certain bacterial species, exhibits notable catalytic efficiency and stability, making it an attractive candidate for further research. Understanding the structure-function relationship of CYP125 can provide insights into its unique enzymatic mechanisms and facilitate the engineering of this protein for enhanced performance in industrial applications. Additionally, the exploration of CYP125's interactions with different substrates can reveal novel pathways for drug metabolism, ultimately contributing to advancements in pharmacology. The recombinant expression of CYP125 allows for detailed studies of its activity and regulation, paving the way for innovations in metabolic engineering and synthetic biology. Thus, the ongoing research into CYP125 and its recombinant protein forms holds significant promise for both fundamental science and practical applications in biotechnology.
