| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MMT |
| Uniprot No | P39900 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 106-470aa |
| 氨基酸序列 | GPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDFHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTTHSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDIRGIQSLYGDPKENQRLPNPDNSEPALCDPNLSFDAVTTVGNKIFFFKDRFFWLKVSERPKTSVNLISSLWPTLPSGIEAAYEIEARNQVFLFKDDKYWLISNLRPEPNYPKSIHSFGFPNFVKKIDAAVFNPRFYRTYFFVDNQYWRYDERRQMMDPGYPKLITKNFQGIGPKIDAVFYSKNKYYYFFQGSNQFEYDFLLQRITKTLKSNSWFGC |
| 预测分子量 | 46.1kDa |
| 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3篇与MMT(金属硫蛋白，Metallothionein)重组蛋白相关的模拟参考文献示例，内容基于典型研究方向构建：
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1. **文献名称**：*Heterologous Expression and Characterization of Recombinant MMT Protein in Escherichia coli*
**作者**：Chen, L.; Wang, H.
**摘要**：本研究通过将人类MMT基因克隆至大肠杆菌表达系统，优化诱导条件实现可溶性重组MMT蛋白的高效表达。纯化后的蛋白通过质谱和圆二色谱验证结构完整性，并证实其具备对镉离子的高亲和力结合能力，为后续环境修复应用奠定基础。
2. **文献名称**：*Structural Insights into Metal Binding Specificity of Recombinant MMT Isoforms*
**作者**：Gupta, R.; Tanaka, K.
**摘要**：文章通过X射线晶体学解析了重组MMT-1和MMT-2亚型的金属结合域结构，揭示了不同亚型对锌、铜离子的选择性差异，为设计金属螯合剂或靶向药物递送系统提供分子机制依据。
3. **文献名称**：*Recombinant MMT Fusion Protein Enhances Antioxidant Capacity in Transgenic Plants*
**作者**：Zhang, Y.; Li, X.
**摘要**：将重组MMT与植物信号肽融合表达于拟南芥中，显著提升植株对重金属胁迫的耐受性。实验表明，转基因植株内活性氧(ROS)水平降低，证实重组MMT在植物抗逆基因工程中的潜在价值。
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**注**：以上文献为示例性质，实际研究中请通过学术数据库(如PubMed、Web of Science)检索真实发表的论文。若需具体领域文献，建议补充MMT蛋白的全称或研究背景。
**Background of MMT Recombinant Proteins**
Recombinant protein technology, a cornerstone of modern biotechnology, enables the production of specific proteins by introducing engineered DNA into host cells. Among various recombinant systems, MMT (Multimerization-competent Tag) recombinant proteins represent an innovative approach designed to address challenges in protein stability, solubility, and functional assembly.
Traditional recombinant protein production often faces issues such as misfolding, aggregation, or low yields, particularly for complex or multimeric proteins. MMT technology emerged to enhance the proper folding and oligomerization of target proteins. The MMT system incorporates a specialized peptide tag that promotes self-assembly into stable multimers. This tag, often derived from naturally occurring oligomerization domains, guides the target protein to adopt its native quaternary structure, improving both stability and biological activity.
The development of MMT recombinant proteins was driven by the growing demand for high-quality proteins in therapeutics, diagnostics, and structural biology. For example, multimeric proteins like antibodies, viral envelope proteins, or signaling receptors require precise assembly to function effectively. By leveraging MMT tags, researchers can bypass laborious refolding processes or costly mammalian expression systems, often achieving functional proteins in simpler hosts like *E. coli* or yeast.
Additionally, MMT technology aligns with the need for scalable and cost-effective biomanufacturing. Its versatility allows fusion with diverse protein classes, from enzymes to vaccine antigens, enabling tailored solutions for industrial and medical applications. Recent advancements in computational protein design and synthetic biology have further refined MMT systems, optimizing tag sequences for specific applications.
Overall, MMT recombinant proteins exemplify the integration of protein engineering and bioprocessing innovation, offering a robust platform to overcome longstanding barriers in recombinant protein production and expand their utility across biomedical and industrial fields.
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