| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | R70M |
| Uniprot No | Q50927 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 27-198aa |
| 氨基酸序列 | AGVAEFNDKGELLLPKNYREWVMVGTQVTPNELNDGKAPFTEIMTVYVDPESYAHWKKTGEFRDGTVTVKELVSVGDRKGPGSGNGYFMGDYIGLEASVKDSQRFANEPGNWAFYIFYVPDTPLVAAAKNLPTAECAACHKENAKTDMVFTQFYPVLRAAKATGESGVVAPK |
| 预测分子量 | 34.7 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. |
以下是假设性的参考文献示例，供参考：
1. **"Structural and Functional Analysis of the R70M Mutant in SARS-CoV-2 Spike Protein"**
*Author: Zhang, L., et al.*
摘要：研究分析了SARS-CoV-2刺突蛋白R70M突变对受体结合域构象的影响，发现该突变可能增强病毒与宿主细胞的结合能力，为疫苗设计提供新靶点。
2. **"R70M Recombinant Protein as a Diagnostic Marker for Autoimmune Diseases"**
*Author: Patel, R., & Kumar, S.*
摘要：探讨R70M重组蛋白在类风湿性关节炎中的诊断价值，通过血清学实验证明其与特定抗体的高亲和力，提示其作为生物标志物的潜力。
3. **"Engineering R70M Mutant Enzymes for Enhanced Catalytic Efficiency"**
*Author: Müller, J., et al.*
摘要：通过定向进化技术构建R70M重组蛋白酶，证明突变体在工业催化反应中的稳定性及活性显著提升，为生物催化剂的开发提供新策略。
4. **"Immunogenicity of R70M-Modified Influenza Hemagglutinin in Murine Models"**
*Author: Chen, H., et al.*
摘要：评估流感血凝素R70M重组蛋白的免疫原性，实验显示其诱导更强中和抗体反应，可能优化流感疫苗设计。
注：以上为模拟示例，实际文献需通过学术数据库检索确认。若需真实文献，请提供更具体的研究背景或蛋白全称。
The R70M recombinant protein is a genetically engineered variant derived from a parent protein through site-directed mutagenesis, where the arginine (R) residue at position 70 is substituted with methionine (M). This modification is often designed to enhance stability, alter substrate binding, or modulate functional interactions while retaining the core structural framework of the original protein. Recombinant protein technology enables its production in heterologous expression systems, such as *E. coli*, yeast, or mammalian cells, followed by purification using affinity chromatography or other methods.
The R70M mutation may target specific functional domains, such as catalytic sites or receptor-binding regions, depending on the protein’s native role. For instance, if the parent protein is an enzyme, this substitution could reduce enzymatic activity or shift substrate specificity, making it valuable for mechanistic studies or therapeutic applications. In therapeutic contexts, such mutations might improve pharmacokinetics or reduce immunogenicity.
Research on R70M often focuses on structure-function relationships, leveraging techniques like X-ray crystallography or cryo-EM to assess conformational changes. Its applications span drug development, diagnostics, and biotechnology. For example, in oncology, engineered proteins like R70M could inhibit aberrant signaling pathways, while in infectious diseases, they might serve as antigenic components in vaccines.
The development of R70M reflects broader trends in precision bioengineering, where single-residue changes are strategically employed to optimize protein behavior. Challenges include ensuring proper folding post-modification and scalability in production. Ongoing studies aim to validate its efficacy in preclinical models, addressing safety and functional consistency for translational use.
Overall, R70M exemplifies the intersection of molecular biology and protein engineering, offering tailored solutions for both research and therapeutic innovation.
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