| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Mut |
| Uniprot No | P22033 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 33-750aa |
| 氨基酸序列 | LHQQQPLHPEWAALAKKQLKGKNPEDLIWHTPEGISIKPLYSKRDTMDLPEELPGVKPFTRGPYPTMYTFRPWTIRQYAGFSTVEESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPVLANFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAILELAYTLADGLEYSRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKMFQPKNSKSLLLRAHCQTSGWSLTEQDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLTNDVYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKYQLEKEDAVEVLAIDNTSVRNRQIEKLKKIKSSRDQALAERCLAALTECAASGDGNILALAVDASRARCTVGEITDALKKVFGEHKANDRMVSGAYRQEFGESKEITSAIKRVHKFMEREGRRPRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGISTLAAGHKTLVPELIKELNSLGRPDILVMCGGVIPPQDYEFLFEVGVSNVFGPGTRIPKAAVQVLDDIEKCLEKKQQSV |
| 预测分子量 | 84.8 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Mut重组蛋白的3-4篇参考文献示例(部分为模拟文献，供参考)：
---
1. **文献名称**：*"Expression and Purification of Recombinant MutS Protein for Mismatch Repair Studies"*
**作者**：Smith J, Brown K, Lee T.
**摘要**：本研究报道了在大肠杆菌系统中高效表达并纯化重组MutS蛋白的方法，通过亲和层析和尺寸排阻色谱获得高纯度蛋白，验证其在体外DNA错配结合活性中的应用。
2. **文献名称**：*"Structural Insights into the MutL Recombinant Protein from E. coli Using Crystallography"*
**作者**：Johnson R, Wang L, García-Sastre A.
**摘要**：通过X射线晶体学解析了重组MutL蛋白的三维结构，揭示了其ATP酶活性结构域的关键作用，为理解DNA错配修复机制提供分子基础。
3. **文献名称**：*"Application of Recombinant MutH Protein in Detecting DNA Methylation Defects"*
**作者**：Chen H, Zhang Y, Kim P.
**摘要**：开发了一种基于重组MutH蛋白的体外检测体系，用于快速识别DNA甲基化异常，在结直肠癌模型研究中展示了高灵敏度和特异性。
4. **文献名称**：*"Optimizing Mut Recombinant Protein Expression in Yeast for Industrial Enzymatic Applications"*
**作者**：Müller S, Fischer B, Schmidt D.
**摘要**：通过优化毕赤酵母表达系统的培养条件，显著提高了重组Mut蛋白的产量，并证明其在工业级核酸修复酶制剂中的潜力。
---
**注**：以上文献为示例性质，实际引用时建议通过PubMed、Web of Science或Google Scholar检索真实文献。若需具体文献支持，可提供更详细的研究背景或关键词。
**Background of Mut Recombinant Proteins**
Recombinant proteins, engineered through genetic modification, have revolutionized biotechnology and medicine. The term "Mut" (often shorthand for *mutant*) refers to recombinant proteins with intentionally altered amino acid sequences, designed to enhance or modify their native functions. These modifications are typically introduced via site-directed mutagenesis, CRISPR-based editing, or other molecular techniques, enabling precise changes in protein structure, stability, binding affinity, or enzymatic activity.
The development of Mut recombinant proteins stems from the need to overcome limitations of wild-type proteins in therapeutic and industrial applications. For example, natural proteins may exhibit low stability, immunogenicity, or suboptimal activity under specific conditions. By introducing targeted mutations, researchers can tailor proteins for improved performance. A classic example is engineered insulin analogs with altered pharmacokinetics for diabetes treatment. Similarly, Mut enzymes are widely used in industrial processes, such as thermostable polymerases in PCR.
In research, Mut proteins serve as tools to dissect structure-function relationships. For instance, mutating catalytic residues in an enzyme can elucidate mechanistic details. In therapeutics, Mut antibodies (e.g., humanized or affinity-matured variants) reduce immune reactions and enhance efficacy. The rise of computational modeling and AI-driven protein design has further accelerated the creation of Mut proteins with novel properties.
Despite their promise, challenges remain, including ensuring proper folding post-modification and predicting off-target effects. Nonetheless, Mut recombinant proteins continue to drive innovation across drug development, synthetic biology, and enzyme engineering, underscoring their pivotal role in advancing bio-based solutions.
×
