Analytical Data
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Gene name
bCMO1
- Application
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Alternative Names
BCO1; BCDO; BCDO1; BCMO; Beta-carotene dioxygenase 1; Beta-carotene oxygenase 1; Beta,beta-carotene 15,15'-monooxygenase
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9HAY6
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Expression Region
Gly6~Pro206
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Molecular Weight
27kDa
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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
BCMO1 (beta-carotene 15,15'-monooxygenase 1) is an enzyme crucial in the conversion of beta-carotene into retinal, a vital component of visual pigments in the retina. The significance of BCMO1 in human health lies in its role in vitamin A metabolism, as beta-carotene is a major dietary precursor of vitamin A. Variability in BCMO1 activity due to genetic polymorphisms can lead to differences in individual responses to beta-carotene intake, impacting vitamin A status and overall health. Research into BCMO1 recombinant proteins has gained traction as scientists aim to elucidate the enzyme’s structure-function relationship, regulatory mechanisms, and interaction with dietary carotenoids. Understanding BCMO1's biochemical pathways is essential for addressing public health issues related to vitamin A deficiency, which remains a significant concern in many parts of the world. Furthermore, studies on BCMO1 may provide insights into its therapeutic potential, as modulating its activity could enhance vitamin A bioavailability from plant sources, offering a dietary strategy for improving health outcomes in populations reliant on carotenoid-rich diets. Through recombinant protein studies, researchers can explore the enzyme's characteristics, assess the impact of polymorphisms, and evaluate potential applications in nutrition and health supplementation, contributing to a deeper understanding of how dietary components influence metabolic processes.











