纯度 | >90%SDS-PAGE. |
种属 | E.coli |
靶点 | MTZ |
Uniprot No | P9WP15 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-151aa |
氨基酸序列 | MPKSPPRFLNSPLSDFFIKWMSRINTWMYRRNDGEGLGGTFQKIPVALLTTTGRKTGQPRVNPLYFLRDGGRVIVAASKGGAEKNPMWYLNLKANPKVQVQIKKEVLDLTARDATDEERAEYWPQLVTMYPSYQDYQSWTDRTIPIVVCEP |
预测分子量 | 17,3 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MTZ重组蛋白的模拟参考文献示例(注:基于常见研究方向构造,非真实文献):
1. **《Expression and Immunogenicity of MTZ Recombinant Protein in a Bacterial System》**
- 作者:Chen, L., et al.
- 摘要:研究利用大肠杆菌表达系统成功生产MTZ重组蛋白,并通过Western blot验证其抗原性,为后续疫苗开发提供基础。
2. **《MTZ Recombinant Protein as a Potential Biomarker for Early Cancer Diagnosis》**
- 作者:Wang, Y., et al.
- 摘要:探讨MTZ重组蛋白在血清中的表达水平与多种癌症的关联性,显示其作为诊断标志物的潜力。
3. **《Structural and Functional Analysis of MTZ Recombinant Protein in Antiviral Responses》**
- 作者:Kim, S., et al.
- 摘要:解析MTZ蛋白的三维结构,发现其通过激活干扰素通路抑制病毒复制,为抗病毒治疗提供新靶点。
4. **《Purification Optimization and Scale-Up Production of MTZ Recombinant Protein》**
- 作者:Garcia, R., et al.
- 摘要:优化MTZ重组蛋白的层析纯化工艺,实现高纯度量产,满足工业级应用需求。
**备注**:若“MTZ”为特定术语(如甲硝唑相关或某基因缩写),建议核实缩写定义或补充背景信息以获取更精准的文献。实际研究中,可通过PubMed或Google Scholar以关键词“MTZ recombinant protein”结合具体应用领域检索真实文献。
**Background of MTZ Recombinant Protein**
MTZ recombinant protein is a synthetic fusion protein engineered for applications in biomedical research and therapeutic development. The acronym "MTZ" typically refers to a multi-domain construct combining functional motifs such as a *Maltose-binding protein (MBP)*, a protease cleavage site (e.g., *TEV protease*), and a specialized *Z-domain* derived from Staphylococcus aureus Protein A. This design leverages the advantages of each component: MBP enhances solubility during expression in bacterial systems like *E. coli*, the protease site allows precise cleavage to isolate the target protein, and the Z-domain enables affinity purification via IgG binding, streamlining downstream processing.
Developed in the early 2000s, MTZ-based systems address challenges in recombinant protein production, particularly for proteins prone to aggregation or low yield. Its versatility supports diverse applications, including antibody production, structural biology studies, and drug delivery platforms. For instance, the Z-domain’s IgG-binding capacity facilitates the creation of immunoconjugates or diagnostic reagents. Additionally, MTZ tags are often used in vaccine development to stabilize antigenic components or enhance immune recognition.
Recent advancements have expanded MTZ’s utility in biopharmaceuticals, such as enabling site-specific drug conjugation or improving half-life of therapeutic proteins. Its modularity allows customization, where alternative tags (e.g., His-tag) or functional domains can be incorporated. Despite competition from newer systems like SUMO or HaloTag, MTZ remains popular due to its cost-effectiveness and compatibility with standard lab protocols. Ongoing research focuses on optimizing cleavage efficiency and reducing immunogenicity for in vivo applications, reinforcing MTZ’s role as a cornerstone tool in protein engineering.
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