纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | CYB5B |
Uniprot No | O43169 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 16-122aa |
氨基酸序列 | KGQEVETSVTYYRLEEVAKRNSLKELWLVIHGRVYDVTRFLNEHPGGEEVLLEQAGVDASESFEDVGHSSDAREMLKQYYIGDIHPSDLKPESGSKDPSKNDTCKSC |
预测分子量 | 43.3 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. |
以下是关于CYB5B重组蛋白的模拟参考文献示例,涵盖不同研究方向:
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1. **文献名称**: *Heterologous Expression and Characterization of Recombinant Human CYB5B in Escherichia coli*
**作者**: Smith A, et al.
**摘要**: 本研究报道了人源CYB5B在大肠杆菌中的重组表达与纯化方法,成功获得高纯度可溶性蛋白。通过酶动力学分析,揭示了CYB5B对NADH的依赖性及其在氧化还原反应中的催化效率,为后续功能研究奠定基础。
2. **文献名称**: *Functional Interaction of Recombinant CYB5B with Cytochrome P450 Enzymes in Drug Metabolism*
**作者**: Chen L, et al.
**摘要**: 利用重组CYB5B蛋白,研究其与细胞色素P450(CYP3A4)的协同作用。实验表明,CYB5B通过传递电子显著增强CYP450对特定药物的代谢活性,提示其在肝脏解毒过程中的关键角色。
3. **文献名称**: *Crystal Structure of Recombinant CYB5B Reveals Insights into Substrate Binding*
**作者**: Tanaka K, et al.
**摘要**: 通过X射线晶体学解析了重组CYB5B的三维结构,发现其FAD结合域的关键氨基酸残基及底物通道构象,为理解其催化机制及设计靶向抑制剂提供了结构基础。
4. **文献名称**: *Recombinant CYB5B Ameliorates Oxidative Stress in a Cellular Model of Methemoglobinemia*
**作者**: Wang Y, et al.
**摘要**: 在先天性高铁血红蛋白血症细胞模型中,外源性重组CYB5B蛋白恢复了细胞还原能力,降低氧化损伤水平,证明其潜在的治疗应用价值。
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**注**:以上文献为示例性内容,实际研究中请通过学术数据库(如PubMed、Web of Science)检索具体文献。
CYB5B (cytochrome b5 type B) is a member of the cytochrome b5 family, a group of small hemoproteins widely distributed in eukaryotes. This protein localizes to the endoplasmic reticulum and mitochondrial outer membrane, where it plays a critical role in electron transfer reactions. It functions as an accessory protein that supports enzymatic activities of various cytochrome P450 (CYP) enzymes, particularly those involved in fatty acid desaturation, cholesterol biosynthesis, and drug/xenobiotic metabolism. Structurally, CYB5B contains a conserved heme-binding domain critical for its redox activity.
Recombinant CYB5B protein is engineered through heterologous expression systems (e.g., E. coli or mammalian cells) to produce purified, functional protein for research and industrial applications. Its recombinant form retains the ability to donate electrons to partner enzymes like NADH-cytochrome b5 reductase and CYP isoforms. Studies emphasize its role in modulating metabolic pathways – for instance, enhancing the activity of stearoyl-CoA desaturase in unsaturated fatty acid production and influencing steroidogenesis by interacting with 17.20-lyase.
Recent research explores CYB5B's involvement in disease mechanisms, including cancer progression (e.g., altering drug metabolism in chemotherapy resistance) and neurodegenerative disorders linked to lipid dysregulation. Recombinant CYB5B serves as a vital tool to study structure-function relationships, screen CYP enzyme modulators, and develop therapeutic strategies targeting metabolic syndromes. Its soluble domains are often prioritized in recombinant designs to improve experimental handling while preserving biological activity. Ongoing work also investigates genetic variants of CYB5B to understand interindividual differences in drug responses and disease susceptibility.
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