| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CYB5R1 |
| Uniprot No | Q9UHQ9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 29-305aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSLVRRSRR PQVTLLDPNE KYLLRLLDKT TVSHNTKRFR FALPTAHHTL GLPVGKHIYL STRIDGSLVI RPYTPVTSDE DQGYVDLVIK VYLKGVHPKF PEGGKMSQYL DSLKVGDVVE FRGPSGLLTY TGKGHFNIQP NKKSPPEPRV AKKLGMIAGG TGITPMLQLI RAILKVPEDP TQCFLLFANQ TEKDIILRED LEELQARYPN RFKLWFTLDH PPKDWAYSKG FVTADMIREH LPAPGDDVLV LLCGPPPMVQ LACHPNLDKL GYSQKMRFTY |
| 预测分子量 | 34 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CYB5R1重组蛋白的参考文献示例(注：以下文献为虚构示例，实际文献需通过学术数据库查询)：
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1. **文献名称**: "Recombinant Human CYB5R1: Expression, Purification, and Functional Characterization"
**作者**: Zhang L, et al.
**摘要**: 本研究利用大肠杆菌系统成功表达并纯化了重组人源CYB5R1蛋白，通过光谱分析和酶动力学实验验证其还原酶活性。结果显示，重组蛋白在NADH依赖性细胞色素b5还原反应中具有高效催化能力，为后续研究其生理功能及疾病机制提供了工具。
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2. **文献名称**: "Structural Insights into CYB5R1 and Its Role in Hereditary Methemoglobinemia"
**作者**: Tanaka K, et al.
**摘要**: 通过X射线晶体学解析了CYB5R1重组蛋白的三维结构，揭示了其与FAD辅因子的结合模式及突变位点对酶活性的影响。研究阐明了CYB5R1基因突变导致遗传性高铁血红蛋白血症的分子机制，为药物开发提供了结构基础。
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3. **文献名称**: "CYB5R1 Overexpression in Cancer Cells: Implications for Redox Homeostasis"
**作者**: Patel S, et al.
**摘要**: 利用重组CYB5R1蛋白探究其在肿瘤细胞氧化还原平衡中的作用。实验表明，CYB5R1过表达通过调节NAD+/NADH比例促进肿瘤细胞增殖，并增强其对化疗药物的耐药性，提示其作为潜在治疗靶点的可能性。
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4. **文献名称**: "Functional Interaction Between CYB5R1 and Cytochrome P450 Enzymes in Drug Metabolism"
**作者**: Kim H, et al.
**摘要**: 研究重组CYB5R1与细胞色素P450酶系的协同作用，发现CYB5R1通过传递电子参与P450介导的药物代谢过程，尤其在肝微粒体中对特定底物的代谢效率显著提高，强调了其在药物代谢研究中的重要性。
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**建议**：实际文献可通过以下数据库查询：
- **PubMed**(https://pubmed.ncbi.nlm.nih.gov/)
- **Google Scholar**(https://scholar.google.com/)
- **Web of Science**
**检索关键词**：CYB5R1 recombinant protein, cytochrome b5 reductase 1. enzyme kinetics, structure-function analysis.
如需具体文献，请提供更详细的研究方向或背景信息。
CYB5R1 (cytochrome b5 reductase 1) is an NADH-dependent oxidoreductase that plays a critical role in cellular redox metabolism. It catalyzes the transfer of electrons from NADH to cytochrome b5. a process essential for various biochemical pathways, including fatty acid desaturation, cholesterol synthesis, and drug metabolism. This enzyme exists in two isoforms: a soluble form primarily found in erythrocytes and a membrane-bound form localized to the endoplasmic reticulum and mitochondria. The soluble isoform is crucial for maintaining hemoglobin iron in its functional ferrous state (Fe²⁺), preventing oxidative damage in red blood cells.
Recombinant CYB5R1 protein is engineered using expression systems like *E. coli* or mammalian cell cultures to produce purified, functional enzyme for research and therapeutic applications. Its production enables detailed studies of enzymatic kinetics, structural properties, and interactions with redox partners. Mutations in the CYB5R1 gene are linked to hereditary methemoglobinemia, a disorder characterized by impaired oxygen transport due to excessive methemoglobin accumulation. Recombinant protein technology aids in elucidating disease mechanisms and developing targeted therapies.
Beyond clinical relevance, recombinant CYB5R1 is utilized in industrial biocatalysis for synthesizing specialized lipids and sterols. It also serves as a tool to investigate oxidative stress-related pathways in neurodegenerative diseases, cancer, and cardiovascular disorders. Recent advances in protein engineering aim to enhance its stability and catalytic efficiency for biomedical and biotechnological applications. Understanding CYB5R1’s role in cellular redox homeostasis continues to drive interest in its recombinant form as a model system for both basic research and translational innovation.
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