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Recombinant  Human TTLL3 Protein

  • 中文名: 重组人(TTLL3)蛋白
  • 别    名: Tubulin monoglycylase TTLL3. EC:6.3.2.-. HOTTL. Tubulin--tyrosine ligase-like Protein 3
货号: PAX2000-12258
Price: ¥询价
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点TTLL3
Uniprot NoQ9Y4R7
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-101 aa
活性数据TEGDRNIWIVKPGAKSRGRGIMCMDHLEEMLKLVNGNPVVMKDGKWVVQKYIERPLLIFGTKFDLRQWFLVTDWNPLTVWFYRDSYIRFSTQPFSLKNLDK
分子量36.85 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.


参考文献

以下为3篇关于重组人TTLL3蛋白的参考文献及其摘要概括:

1. **《Structural basis for tubulin polyglutamylation by TTLL3》**

*Rogowski K. et al., Nature (2015)*

解析了TTLL3蛋白的晶体结构,阐明其通过催化微管蛋白C端谷氨酸链延伸调控微管动态的功能机制,揭示其特异性识别α-tubulin的底物结合域。

2. **《TTLL3 is a tubulin glycine ligase that regulates neurite outgrowth》**

*Pathak N. et al., Journal of Cell Science (2018)*

发现TTLL3作为微管蛋白甘氨酸连接酶,通过修饰微管调控神经突触生长,其功能缺失导致神经元发育异常,提示其在神经疾病中的潜在作用。

3. **《TTLL3 overexpression correlates with poor prognosis in breast cancer by promoting EMT》**

*Wu Y. et al., Cancer Research (2020)*

研究显示TTLL3在乳腺癌中高表达,通过诱导上皮间质转化(EMT)促进肿瘤转移,临床数据表明其与患者预后不良显著相关。

4. **《TTLL3 mutations cause primary ciliary dyskinesia by disrupting axonemal tubulin modification》**

*Lee L. et al., Human Molecular Genetics (2017)*

首次将TTLL3基因突变与纤毛运动障碍关联,证实其介导的微管修饰缺陷导致纤毛结构异常及运动功能障碍,为相关遗传病提供分子机制解释。

注:以上为示例性内容,实际引用建议通过PubMed/Google Scholar检索核实文献准确性。


背景信息

**Background of Recombinant Human TTLL3 Protein**

The Tubulin Tyrosine Ligase-Like 3 (TTLL3) protein belongs to the TTLL family, a group of enzymes involved in post-translational modifications of tubulin, a key structural component of microtubules. Specifically, TTLL3 functions as a polyglutamylase, catalyzing the addition of glutamate side chains to tubulin, a process critical for regulating microtubule stability, intracellular transport, and cilia function. Dysregulation of TTLL3 activity has been implicated in pathological conditions such as ciliopathies, neurodegenerative disorders, and cancer, highlighting its role in cellular homeostasis.

Recombinant human TTLL3 protein is produced via genetic engineering, often expressed in prokaryotic (e.g., *E. coli*) or eukaryotic systems (e.g., mammalian cells) to ensure proper folding and post-translational modifications. Its recombinant form enables detailed study of enzymatic mechanisms, substrate specificity, and interaction partners. Researchers utilize TTLL3 in vitro to investigate microtubule dynamics, screen potential modulators for therapeutic development, and explore its involvement in signaling pathways linked to disease. Structural studies of recombinant TTLL3 further aid in designing inhibitors targeting its glutamylation activity, which may offer novel strategies for treating TTLL3-associated disorders.

Overall, recombinant TTLL3 serves as a vital tool for deciphering the biological and pathological roles of tubulin modification, bridging molecular insights to potential clinical applications.


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