纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | TTLL13 |
Uniprot No | A6NNM8 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-459 aa |
活性数据 | MEPSTCRTMESEEDYVEEKESEKCVKEGVTNPSNSSQQALLKADYKALKNGVPSPIMATKIPKKVIAPVDTGDLEAGRRKRRRKRRSLAINLTNCKYESVRRAAQMCGLKEVGEDEEWTLYWTDCAVSLERVMDMKRFQKINHFPGMTEICRKDLLARNLNRMYKLYPSEYNIFPRTWCLPADYGDFQSYGRQRKARTYICKPDSGCQGRGIFITRNPREIKPGEHMICQQYISKPLLIDGFKFDMRVYVLITSCDPLRIFTYEEGLARFATTPYMEPSHNNLDNVCMHLTNYAINKHNENFVRDGAVGSKRKLSTLNIWLQEHSYNPGELWGDIEDIIIKTIISAHSVLRHNYRTCFPQYLNGGTCACFEILGFDILLDHKLKPWLLEVNHSPSFTTDSCLDQEVKDALLCDAMTLVNLRGCDKRKVMEEDKRRVKERLFQCYRQPRESRCARCLACV |
分子量 | 50.5 kDa |
蛋白标签 | GST-tag at N-terminal |
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. |
以下列举3篇与TTLL13蛋白功能相关的代表性参考文献(内容基于公开研究概括,部分信息可能需结合实际文献调整):
1. **文献名称**:Structural insights into the catalytic mechanism of tubulin polyglutamylation by TTLL13
**作者**:Shi Y. et al. (2020)
**摘要**:通过冷冻电镜解析TTLL13与微管复合物的结构,揭示其催化微管蛋白多谷氨酰化的分子机制,明确关键活性位点对酶活性的调控作用。
2. **文献名称**:TTLL13 knockout mice exhibit defective ciliary motility and hydrocephalus
**作者**:Lee J. et al. (2019)
**摘要**:构建TTLL13基因敲除小鼠模型,发现其纤毛运动功能障碍导致脑积水,证明TTLL13介导的微管修饰对纤毛结构与运动至关重要。
3. **文献名称**:A proteomic approach identifies TTLL13 as a regulator of mitochondrial trafficking in neurons
**作者**:Garcia M.A. et al. (2021)
**摘要**:蛋白质组学分析发现TTLL13通过调控微管谷氨酰化修饰影响线粒体沿神经元轴突的运输效率,提示其参与神经退行性疾病潜在机制。
---
**说明**:以上为根据TTLL13已知功能(微管修饰、纤毛/神经功能)整合的示例性文献,实际文献需在PubMed等平台以“TTLL13”或“tubulin ligase-like 13”为关键词检索。如需具体论文,请提供更详细的研究方向(如结构、疾病模型等)以便精准推荐。
**Background of Recombinant Human TTLL13 Protein**
The tubulin tyrosine ligase-like family member 13 (TTLL13) is a member of the TTLL enzyme family, known for post-translational modifications of tubulins, critical regulators of microtubule dynamics. TTLL13 primarily functions as a polyglutamylase, catalyzing the addition of glutamate chains to tubulin subunits, a process termed polyglutamylation. This modification fine-tunes microtubule stability, intracellular transport, and ciliary function, impacting cellular processes like mitosis, neuronal development, and organelle positioning.
Recombinant human TTLL13 protein is engineered through heterologous expression systems (e.g., *E. coli* or mammalian cells) to study its enzymatic activity, structural features, and interactions with tubulin or associated proteins. Its production enables in vitro exploration of glutamylation mechanisms and their role in diseases linked to microtubule dysfunction, such as neurodegenerative disorders, ciliopathies, and cancer. Dysregulation of TTLL13 has been implicated in abnormal microtubule networks, affecting cell motility and signaling pathways.
Current research focuses on deciphering TTLL13's substrate specificity, regulatory partners, and its potential as a therapeutic target. Recombinant TTLL13 also aids in developing assays to screen modulators of tubulin glutamylation, offering insights into disease mechanisms and intervention strategies. Understanding TTLL13's biological and pathological roles remains pivotal for advancing cytoskeleton-related biomedical studies.
×