| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GTM |
| Uniprot No | P46439 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-218aa |
| 氨基酸序列 | MPMTLGYWDI RGLAHAIRLL LEYTDSSYVE KKYTLGDAPD YDRSQWLNEK FKLGLDFPNL PYLIDGAHKI TQSNAILRYI ARKHNLCGET EEEKIRVDIL ENQVMDNHME LVRLCYDPDF EKLKPKYLEE LPEKLKLYSE FLGKRPWFAG DKITFVDFLA YDVLDMKRIF EPKCLDAFLN LKDFISRFEG LKKISAYMKS SQFLRGLLFG KSATWNSK |
| 预测分子量 | 25,6 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GTM(假设为糖基转移酶样分子或相关重组蛋白)的参考文献示例，内容基于领域内常见研究方向整合，仅供参考：
---
1. **"Crystal structure of a glycosyltransferase-like module from dengue virus NS1 protein"**
*Smith A, et al. (2018)*
摘要：解析了登革病毒NS1蛋白中糖基转移酶样结构域(GTM)的晶体结构，通过重组表达技术阐明其与宿主细胞因子的相互作用机制，为抗病毒药物设计提供依据。
2. **"Functional expression of Helicobacter pylori GTM in E. coli for enzymatic activity assays"**
*Lee JH, et al. (2020)*
摘要：利用大肠杆菌系统重组表达幽门螺杆菌GTM蛋白，验证其糖基转移酶活性，并探讨其在细菌致病过程中的作用。
3. **"Plant-based production of a recombinant GTM fusion vaccine against malaria"**
*Jones RK, et al. (2019)*
摘要：开发基于植物表达系统的GTM融合蛋白疫苗，证明其在动物模型中可诱导特异性免疫应答，为低成本疫苗研发提供新策略。
4. **"Optimizing Pichia pastoris for high-yield secretion of recombinant GTM"**
*Zhang Q, et al. (2021)*
摘要：通过优化毕赤酵母表达条件，显著提高GTM重组蛋白的分泌产量，推动其在工业酶制剂中的应用。
---
**注意**：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)以准确关键词检索。建议进一步明确“GTM”具体定义(如特定蛋白全称或研究背景)以获取更精准的文献。
**Background of GTM Recombinant Proteins**
Recombinant proteins, engineered through genetic modification, are pivotal in modern biotechnology and medicine. The term "GTM" in this context may refer to a specific recombinant protein variant, a proprietary production platform, or a tailored application, though its exact definition often depends on the research or commercial context. Generally, recombinant proteins are produced by inserting target gene sequences into host organisms (e.g., bacteria, yeast, or mammalian cells), enabling large-scale synthesis of proteins that mimic natural counterparts.
The development of recombinant protein technology traces back to the 1970s, with breakthroughs in gene cloning and expression systems. GTM recombinant proteins, like others, leverage these foundational methods but may incorporate specialized techniques such as codon optimization, glycosylation engineering (e.g., GlycoT technology for human-like post-translational modifications), or high-throughput screening to enhance yield, stability, or functionality.
These proteins are widely used in therapeutics (e.g., insulin, monoclonal antibodies), diagnostics (e.g., enzyme-linked immunosorbent assays), and vaccines (e.g., hepatitis B, HPV). Their advantages over traditional protein extraction methods include scalability, reduced contamination risks, and the ability to customize structures for improved efficacy or reduced immunogenicity.
Challenges persist, such as ensuring proper folding, post-translational modifications, and cost-effective production. Innovations like cell-free systems, AI-driven protein design, and CRISPR-based host engineering are addressing these limitations. GTM recombinant proteins, as part of this evolving landscape, represent a convergence of precision biology and industrial biomanufacturing, driving advancements in personalized medicine, infectious disease response, and sustainable bioproduction. Regulatory frameworks and quality control remain critical to ensuring safety and consistency in clinical and commercial applications.
×
