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Recombinant Human TRAPPC2L protein

  • 中文名: 运输蛋白颗粒复合物亚基2样蛋白(TRAPPC2L)重组蛋白
  • 别    名: TRAPPC2L;Trafficking protein particle complex subunit 2-like protein
货号: PA1000-3289
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点TRAPPC2L
Uniprot NoQ9UL33-2
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-139aa
氨基酸序列MGSSHHHHHH SSGLVPRGSH MGSMAVCIAV IAKENYPLYI RSTPTENELK FHYMVHTSLD VVDEKISAMG KALVDQRELY LGLLYPTEDY KVYGYVTNSK VKFVMVVDSS NTALRDNEIR SMFRKLHNSY TDVMCNPFYN PGDRIQSRAF DNMVTSMMIQ VC
预测分子量18 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.

参考文献

以下是关于TRAPPC2L重组蛋白的模拟参考文献示例(注:部分文献信息为假设性概括,实际引用请通过学术数据库核实):

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1. **文献名称**: *"TRAPPC2L regulates vesicular trafficking through interaction with the TRAPP complex in vitro"*

**作者**: Sacher M, Kim JJ, Graham LA

**摘要**: 本研究通过重组TRAPPC2L蛋白的体外实验,揭示了其与TRAPP复合体其他亚基的相互作用机制。研究发现,TRAPPC2L在调控高尔基体到内体囊泡运输中起关键作用,并可能通过影响GEF(鸟苷酸交换因子)活性参与Rab GTPase信号通路。

2. **文献名称**: *"Structural characterization of recombinant TRAPPC2L and its role in autophagy"*

**作者**: Chen X, Wang Y, Li R

**摘要**: 通过大肠杆菌表达系统成功纯化重组TRAPPC2L蛋白,并利用X射线晶体学解析其三维结构。功能实验表明,TRAPPC2L通过结合Atg8家族蛋白参与自噬体形成,为自噬相关疾病的分子机制提供了新见解。

3. **文献名称**: *"Recombinant TRAPPC2L expression in HeLa cells disrupts mitotic progression"*

**作者**: Zhang T, Liu H, Suzuki K

**摘要**: 过表达重组TRAPPC2L蛋白导致HeLa细胞有丝分裂异常,表现为纺锤体组装缺陷和染色体分离错误。研究提示TRAPPC2L可能在细胞周期调控中发挥重要作用,并与癌症发生相关。

4. **文献名称**: *"Optimization of TRAPPC2L recombinant protein production for functional assays"*

**作者**: Müller B, Patel RS

**摘要**: 本文报道了一种高效表达和纯化重组TRAPPC2L蛋白的改良方案,通过融合标签和缓冲液优化显著提高蛋白稳定性,为后续生化研究提供了可靠工具。

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**注意**:以上内容为基于TRAPPC2L已知功能的模拟概括,实际文献需通过PubMed、Google Scholar等平台检索关键词(如TRAPPC2L, recombinant protein, TRAPP complex)获取。如需具体文献,建议访问学术数据库或联系机构图书馆。

背景信息

TRAPPC2L (Transport Protein Particle Complex subunit 2-like) is a member of the TRAPP (TRAnsport Protein Particle) family, a conserved group of multi-subunit complexes involved in membrane trafficking and vesicle-mediated transport within eukaryotic cells. Specifically, TRAPP complexes regulate tethering and fusion of vesicles between the endoplasmic reticulum (ER), Golgi apparatus, and endosomal compartments, playing critical roles in maintaining cellular homeostasis, secretion, and autophagy. TRAPPC2L shares homology with TRAPPC2. a subunit implicated in mediating interactions with Rab GTPases, key regulators of vesicle trafficking. However, TRAPPC2L is distinct in its tissue distribution and functional specialization, with studies suggesting its involvement in Golgi organization, ciliogenesis, and cell cycle regulation.

The recombinant TRAPPC2L protein is engineered for in vitro studies to dissect its molecular interactions, structural features, and regulatory mechanisms. Produced via heterologous expression systems (e.g., E. coli or mammalian cells), it typically retains functional domains required for binding partner recognition, such as the conserved α-helical regions critical for TRAPP complex assembly. Researchers employ this recombinant protein to investigate its role in diseases linked to trafficking defects, including neurodegenerative disorders, ciliopathies, and cancers. For example, TRAPPC2L dysregulation has been associated with impaired autophagy in tumorigenesis and developmental abnormalities in model organisms. Structural analyses using recombinant TRAPPC2L also aid in mapping interaction networks with Rab proteins or other TRAPP subunits, providing insights into vesicle tethering mechanisms. Its applications extend to drug screening platforms targeting trafficking pathways, highlighting its utility as a tool for both basic research and therapeutic development.

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