| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | bCMO1 |
| Uniprot No | Q9HAY6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-547aa |
| 氨基酸序列 | MDIIFGRNRK EQLEPVRAKV TGKIPAWLQG TLLRNGPGMH TVGESRYNHW FDGLALLHSF TIRDGEVYYR SKYLRSDTYN TNIEANRIVV SEFGTMAYPD PCKNIFSKAF SYLSHTIPDF TDNCLINIMK CGEDFYATSE TNYIRKINPQ TLETLEKVDY RKYVAVNLAT SHPHYDEAGN VLNMGTSIVE KGKTKYVIFK IPATVPEGKK QGKSPWKHTE VFCSIPSRSL LSPSYYHSFG VTENYVIFLE QPFRLDILKM ATAYIRRMSW ASCLAFHREE KTYIHIIDQR TRQPVQTKFY TDAMVVFHHV NAYEEDGCIV FDVIAYEDNS LYQLFYLANL NQDFKENSRL TSVPTLRRFA VPLHVDKNAE VGTNLIKVAS TTATALKEED GQVYCQPEFL YEGLELPRVN YAHNGKQYRY VFATGVQWSP IPTKIIKYDI LTKSSLKWRE DDCWPAEPLF VPAPGAKDED DGVILSAIVS TDPQKLPFLL ILDAKSFTEL ARASVDVDMH MDLHGLFITD MDWDTKKQAA SEEQRDRASD CHGAPLT |
| 预测分子量 | 62,6 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是3-4条关于**bCMO1(β-carotene 15.15'-monooxygenase 1)重组蛋白**的模拟参考文献示例(实际文献请通过学术数据库检索)：
---
1. **文献名称**: *"Heterologous Expression and Functional Characterization of Recombinant bCMO1 in Escherichia coli"*
**作者**: Smith A, et al.
**摘要**: 研究报道了在大肠杆菌中成功克隆并表达了人源bCMO1重组蛋白，通过亲和层析纯化后，验证了其催化β-胡萝卜素转化为视黄醛的活性，并分析了酶的最适反应条件及动力学参数。
2. **文献名称**: *"Structural Insights into bCMO1 Reveal Substrate Binding Mechanism"*
**作者**: Zhang L, Wang H.
**摘要**: 利用X射线晶体学解析了重组bCMO1的三维结构，揭示了其与β-胡萝卜素结合的活性位点特征，并通过定点突变实验验证了关键氨基酸残基在催化中的作用。
3. **文献名称**: *"Enhancement of Recombinant bCMO1 Stability via Protein Engineering for Nutritional Applications"*
**作者**: Gupta R, et al.
**摘要**: 通过定向进化技术改造bCMO1重组蛋白，提高了其在体外环境下的热稳定性和抗氧化性，为开发基于β-胡萝卜素强化的食品添加剂提供了理论依据。
4. **文献名称**: *"Functional Comparison of bCMO1 Orthologs from Mammals and Teleost Fish"*
**作者**: Tanaka K, et al.
**摘要**: 比较了哺乳动物和鱼类bCMO1重组蛋白的酶学特性，发现鱼类酶对低浓度底物的催化效率更高，为研究维生素A代谢的物种差异提供了新视角。
---
**实际检索建议**：
- 使用关键词：`"bCMO1" OR "BCO1" AND "recombinant protein"`，在PubMed、Web of Science或Google Scholar中检索。
- 关注期刊：*Journal of Lipid Research*, *Biochimica et Biophysica Acta (BBA)-Molecular and Cell Biology of Lipids*等。
如需具体文献，建议提供更详细的研究方向(如表达系统、功能分析等)以便进一步筛选。
bCMO1 (beta-carotene 15.15'-monooxygenase 1), also known as BCO1. is a critical enzyme in the metabolism of provitamin A carotenoids, particularly β-carotene. This cytosolic enzyme catalyzes the symmetric cleavage of β-carotene at the central 15.15' double bond, producing two molecules of retinal (vitamin A aldehyde), which can subsequently be converted into retinol (vitamin A) or retinoic acid. As a key regulator of vitamin A homeostasis, bCMO1 plays an essential role in vision, immune function, and cellular differentiation. Its activity directly impacts dietary vitamin A sufficiency, especially in populations reliant on plant-based sources of provitamin A.
Recombinant bCMO1 protein is produced through genetic engineering techniques, typically expressed in heterologous systems like *E. coli* or mammalian cell lines. This allows large-scale purification and functional characterization of the enzyme. The recombinant form often retains catalytic activity comparable to the native protein, enabling studies on substrate specificity, enzymatic kinetics, and inhibitor interactions. Researchers frequently employ affinity tags (e.g., His-tag) for purification and tracking.
Current research focuses on bCMO1's structural biology, polymorphism effects (e.g., rs12934922 SNP influencing enzyme activity), and its relevance to diseases like age-related macular degeneration and metabolic disorders. In biotechnology, recombinant bCMO1 has applications in developing fortified foods and gene therapies for vitamin A deficiency. Its crystal structure, resolved in recent years, provides insights into substrate-binding domains and catalytic mechanisms, facilitating rational drug design and nutritional intervention strategies.
×
