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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human BCO1, N-His |
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Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 25.25 kDa |
Buffer | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
Form | Liquid |
Delivery condition | Dry Ice |
Delivery lead time in business days | 3-5 days if in stock; 3-5 weeks if production needed |
Storage condition | 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection) |
Brand | Arovia |
Host species | Escherichia coli (E.coli) |
Fragment Type | Gly6-Pro206 |
Aliases /Synonyms | BCMO1, Beta,beta-carotene 15,15'-dioxygenase, BCDO, BCO1, Beta-carotene oxygenase 1, BCDO1, Beta-carotene dioxygenase 1 |
Reference | YHK04701 |
Note | For research use only. |
Recombinant human BCO1 (Beta-Carotene Oxygenase 1) is a key enzyme involved in the metabolism of beta-carotene, a dietary source of vitamin A. This enzyme is encoded by the BCO1 gene and is primarily expressed in the liver and intestine. Recombinant human BCO1 has gained significant attention in the scientific community due to its potential therapeutic and industrial applications. In this article, we will discuss the structure, activity and application of recombinant human BCO1 in detail.
Recombinant human BCO1 is a 63 kDa protein consisting of 575 amino acids. It belongs to the carotenoid oxygenase family and has a conserved catalytic domain with a characteristic di-iron binding motif. The crystal structure of recombinant human BCO1 has been determined, revealing a unique fold with a central beta-sheet surrounded by alpha-helices. This structure is highly conserved across different species, indicating the importance of BCO1 in beta-carotene metabolism.
Recombinant human BCO1 acts as a key enzyme in the conversion of beta-carotene to retinol, the active form of vitamin A. This process involves the cleavage of beta-carotene into two molecules of retinal, which is then reduced to retinol by retinol dehydrogenase. The activity of recombinant human BCO1 is dependent on the presence of oxygen and iron ions, which act as cofactors in the catalytic reaction. Studies have shown that the activity of recombinant human BCO1 can be modulated by various factors such as pH, temperature, and substrate concentration.
Recombinant human BCO1 has potential therapeutic applications in the treatment of vitamin A deficiency and related diseases. Deficiency of vitamin A is a major global health problem, especially in developing countries. Recombinant human BCO1 can be used to produce retinol, which can then be used as a dietary supplement to combat vitamin A deficiency. In addition, studies have shown that recombinant human BCO1 can also be used to produce retinoids, which have been used in the treatment of various diseases such as cancer, skin disorders, and eye diseases.
Recombinant human BCO1 also has potential industrial applications in the food and feed industry. Beta-carotene is a widely used food additive for its antioxidant and colorant properties. However, its low bioavailability limits its application. Recombinant human BCO1 can be used to enhance the bioavailability of beta-carotene by converting it to retinol, which is more easily absorbed by the body. This can lead to the development of functional foods with increased nutritional value. In addition, recombinant human BCO1 can also be used in the production of animal feed to improve the vitamin A status of livestock.
Recombinant human BCO1 is a valuable tool for research in the field of carotenoid metabolism. It can be used to study the role of BCO1 in various physiological processes and to understand the mechanisms underlying vitamin A deficiency and related diseases. Recombinant human BCO1 can also be used to screen for potential inhibitors or activators of the enzyme, which can aid in the development of novel therapeutics.
In conclusion, recombinant human BCO1 is a crucial enzyme involved in the metabolism of beta-carotene and has significant potential in various
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