| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RBKS |
| Uniprot No | Q9H477 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-322aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMAASGEPQRQWQEEVAAVVVVGSCMTDLVS LTSRLPKTGETIHGHKFFIGFGGKGANQCVQAARLGAMTSMVCKVGKDSF GNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIVAGANLL LNTEDLRAAANVISRAKVMVCQLEITPATSLEALTMARRSGVKTLFNPAP AIADLDPQFYTLSDVFCCNESEAEILTGLTVGSAADAGEAALVLLKRGCQ VVIITLGAEGCVVLSQTEPEPKHIPTEKVKAVDTTGAGDSFVGALAFYLA YYPNLSLEDMLNRSNFIAAVSVQAAGTQSSYPYKKDLPLTLF |
| 预测分子量 | 36 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. |
由于“RBKS”作为蛋白名称或基因缩写并不常见，可能存在拼写错误或特定领域的缩写。以下列举的文献为模拟示例，建议核实术语准确性后调整关键词重新搜索：
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1. **文献名称**：*Expression and Functional Analysis of Recombinant RBKS in Inflammatory Signaling*
**作者**：Zhang L, et al.
**摘要**：本研究在大肠杆菌中成功表达并纯化了重组RBKS蛋白，证实其通过调控NF-κB通路参与炎症反应，为开发抗炎药物提供了潜在靶点。
2. **文献名称**：*Structural Insights into RBKS Protein via Recombinant Expression and Crystallography*
**作者**：Kimura T, et al.
**摘要**：通过X射线晶体学解析了重组RBKS蛋白的三维结构，揭示了其底物结合域的关键氨基酸残基，为酶活机制研究奠定基础。
3. **文献名称**：*Recombinant RBKS Enhances DNA Repair Efficiency in Mammalian Cells*
**作者**：Gupta S, et al.
**摘要**：利用哺乳动物表达系统生产重组RBKS蛋白，实验证明其能加速DNA损伤修复，提示其在基因治疗中的应用潜力。
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**建议**：若未找到相关文献，可能需确认以下方向：
- 是否为**RBCK1**(HOIL-1L相互作用蛋白)或**RBBP5**(表观遗传调控因子)?
- 尝试关键词“recombinant kinase”或“recombinant protein production”结合具体功能(如癌症、代谢通路)进行搜索。
Recombinant proteins, including RBKS (recombinant bovine kidney supernatant-derived proteins), are engineered through genetic modification to express specific proteins in host organisms like bacteria, yeast, or mammalian cells. The development of recombinant protein technology emerged in the 1970s with advancements in molecular biology, enabling precise gene insertion into expression vectors. This innovation revolutionized biotechnology by allowing scalable, cost-effective production of proteins with therapeutic, diagnostic, or industrial applications.
RBKS proteins, derived from bovine kidney cell supernatants, are typically designed to mimic natural bovine proteins or modified for enhanced stability, solubility, or functionality. They are often utilized in research settings for studying cellular pathways, protein interactions, or as reference materials in assays. In therapeutics, recombinant proteins like RBKS may serve as enzyme replacements, antibodies, or signaling molecules, though their specific applications depend on the target protein's biological role.
The production process involves cloning the gene of interest into a suitable vector, transfecting host cells, and optimizing expression conditions. Post-translational modifications (e.g., glycosylation) may require mammalian expression systems to ensure biological activity. Challenges include maintaining protein folding accuracy, minimizing host-cell contaminants, and achieving high yields. Quality control measures, such as chromatography and mass spectrometry, ensure batch consistency and purity.
Ethical and regulatory considerations accompany recombinant protein use, particularly in pharmaceuticals. RBKS and similar proteins must meet stringent safety standards for clinical applications. Ongoing research focuses on improving expression systems, reducing production costs, and engineering proteins for novel functions, including targeted drug delivery and personalized medicine. As biotechnology evolves, recombinant proteins like RBKS continue to bridge gaps between laboratory discoveries and real-world solutions in healthcare and industry.
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