| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TG |
| Uniprot No | P01266 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 全长 |
| 氨基酸序列 | full |
| 预测分子量 | 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3-4篇关于重组TG(转谷氨酰胺酶，Transglutaminase)蛋白的文献摘要概览：
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1. **文献名称**：*Microbial transglutaminase: Production, optimization, and application in food processing*
**作者**：Cui L. et al.
**摘要**：研究利用大肠杆菌重组表达微生物转谷氨酰胺酶(MTG)，优化发酵条件以提高酶活性，并验证其在食品加工(如乳制品质构改良)中的应用效果。
2. **文献名称**：*Recombinant human tissue transglutaminase for celiac disease diagnosis*
**作者**：Sollid L.M. et al.
**摘要**：开发重组人组织型TG(tTG)作为乳糜泻血清学检测抗原，验证其与患者自身抗体的高特异性结合，为临床诊断提供可靠工具。
3. **文献名称**：*Expression and purification of recombinant transglutaminase from Streptomyces mobaraensis*
**作者**：Zhu Y. et al.
**摘要**：通过毕赤酵母系统高效表达茂原链霉菌来源的TG酶，建立纯化工艺，分析其催化交联明胶等底物的活性，为工业化生产提供方案。
4. **文献名称**：*Engineering thermostable transglutaminase for biomedical applications*
**作者**：Chen R.R. et al.
**摘要**：通过蛋白质工程改造重组TG酶的热稳定性，提升其在组织工程支架交联或药物递送系统中的性能，验证其生物相容性及长效催化能力。
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以上文献聚焦于重组TG蛋白的生产优化、医学诊断及工业应用。如需具体文章DOI或发表年份，可进一步补充说明。
**Background of Recombinant TG Proteins**
Recombinant transglutaminase (TG) proteins are engineered enzymes produced through genetic modification and microbial expression systems. Transglutaminases, naturally occurring enzymes found in animals, plants, and microbes, catalyze the formation of covalent bonds between glutamine and lysine residues in proteins, leading to cross-linking or modification of protein structures. This unique enzymatic activity has broad applications in food processing, biomedical research, and industrial biotechnology. However, traditional extraction of TG from animal tissues (e.g., guinea pig liver or fish blood) faces challenges, including limited yield, ethical concerns, and potential contamination risks.
To overcome these limitations, recombinant DNA technology has been adopted to produce TG enzymes in heterologous hosts such as *Escherichia coli*, yeast, or insect cells. By cloning the TG gene into expression vectors and optimizing fermentation conditions, large-scale production of highly pure and active recombinant TG is achievable. Microbial expression systems offer advantages like cost-effectiveness, scalability, and reduced batch-to-batch variability. For instance, microbial TG (mTG) from *Streptomyces mobaraensis* is widely commercialized for food applications, enhancing texture in products like processed meats and plant-based analogs.
In biomedicine, recombinant TG proteins are explored for tissue engineering, wound healing, and drug delivery due to their ability to stabilize extracellular matrices or functionalize biomaterials. Additionally, site-specific protein modifications enabled by TG-mediated conjugation are valuable in antibody-drug conjugates (ADCs) and diagnostic tools. Despite progress, challenges remain, including optimizing enzyme stability, minimizing immunogenicity, and tailoring substrate specificity for niche applications. Ongoing research focuses on protein engineering (e.g., mutagenesis or fusion tags) to enhance catalytic efficiency and expand utility across industries. Overall, recombinant TG proteins exemplify the synergy between enzymology and biotechnology in addressing industrial and therapeutic needs.
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