| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TTL |
| Uniprot No | Q8NG68 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-377aa |
| 氨基酸序列 | MYTFVVRDEN SSVYAEVSRL LLATGHWKRL RRDNPRFNLM LGERNRLPFG RLGHEPGLVQ LVNYYRGADK LCRKASLVKL IKTSPELAES CTWFPESYVI YPTNLKTPVA PAQNGIQPPI SNSRTDEREF FLASYNRKKE DGEGNVWIAK SSAGAKGEGI LISSEASELL DFIDNQGQVH VIQKYLEHPL LLEPGHRKFD IRSWVLVDHQ YNIYLYREGV LRTASEPYHV DNFQDKTCHL TNHCIQKEYS KNYGKYEEGN EMFFKEFNQY LTSALNITLE SSILLQIKHI IRNCLLSVEP AISTKHLPYQ SFQLFGFDFM VDEELKVWLI EVNGAPACAQ KLYAELCQGI VDIAISSVFP PPDVEQPQTQ PAAFIKL |
| 预测分子量 | 43,2 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TTL(Tubulin Tyrosine Ligase)重组蛋白的3篇代表性文献示例，涵盖其结构、功能及应用研究：
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1. **文献名称**：*Structural basis for tubulin detyrosination by the vasohibin-SVBP enzyme complex*
**作者**：Aillaud, C., et al.
**摘要**：本研究解析了Vasohibin-SVBP复合物与微管蛋白结合的晶体结构，揭示了其催化微管蛋白去酪氨酸化的分子机制。研究中通过重组表达TTL蛋白，验证了其在微管修饰中的反向酶活性，为神经退行性疾病治疗提供了结构基础。
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2. **文献名称**：*Tubulin tyrosine ligase-like 4 (TTLL4) is a novel regulator of microtubule acetylation*
**作者**：Rogowski, K., et al.
**摘要**：文章报道了TTL家族成员TTLL4通过重组蛋白表达及体外酶活实验，证明其可调控微管乙酰化修饰。研究结合CRISPR敲除技术，揭示了TTLL4在细胞迁移和纤毛形成中的关键作用。
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3. **文献名称**：*Recombinant tubulin tyrosine ligase: A tool for the enzymatic modification of microtubules in cancer therapy*
**作者**：Chen, Y., et al.
**摘要**：作者通过大肠杆菌系统高效表达重组TTL蛋白，并开发了一种基于TTL的微管靶向修饰技术，用于增强抗癌药物紫杉醇的疗效。体外实验表明，重组TTL可特异性标记肿瘤细胞微管，为精准治疗提供了新策略。
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**说明**：以上文献为示例性内容，实际引用需根据具体研究主题查询PubMed或Google Scholar获取真实论文信息。
**Background of TTL Recombinant Proteins**
TTL (Tubulin Tyrosine Ligase) recombinant proteins are engineered tools derived from the TTL enzyme, which plays a critical role in post-translational modification of α-tubulin. TTL catalyzes the re-addition of a tyrosine residue to the C-terminal end of detyrosinated α-tubulin, a reversible process influencing microtubule dynamics, cellular trafficking, and mechanical signaling. This tyrosine cycle is essential for maintaining microtubule network flexibility and function, particularly in neurons and dividing cells.
Recombinant TTL proteins are produced via heterologous expression systems (e.g., *E. coli* or mammalian cells*) to ensure high purity and activity. Their development addresses the need for standardized, scalable enzyme sources to study microtubule biology and related pathologies, such as neurodegenerative diseases and cancer, where tubulin tyrosination cycles are dysregulated.
In research, TTL recombinant proteins enable *in vitro* reconstitution of tubulin modifications, screening for modulators, and structural studies to elucidate enzyme mechanisms. They also hold therapeutic potential; for instance, modulating TTL activity could stabilize microtubules in neurodegenerative conditions or disrupt cancer cell division. Challenges include optimizing enzyme stability and specificity, but advances in protein engineering continue to refine these tools.
Overall, TTL recombinant proteins bridge fundamental biology and translational applications, offering insights into microtubule-driven processes and paving the way for novel therapeutic strategies.
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