| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TRIC |
| Uniprot No | P17987 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-556aa |
| 氨基酸序列 | MEGPLSVFGD RSTGETIRSQ NVMAAASIAN IVKSSLGPVG LDKMLVDDIG DVTITNDGAT ILKLLEVEHP AAKVLCELAD LQDKEVGDGT TSVVIIAAEL LKNADELVKQ KIHPTSVISG YRLACKEAVR YINENLIVNT DELGRDCLIN AAKTSMSSKI IGINGDFFAN MVVDAVLAIK YTDIRGQPRY PVNSVNILKA HGRSQMESML ISGYALNCVV GSQGMPKRIV NAKIACLDFS LQKTKMKLGV QVVITDPEKL DQIRQRESDI TKERIQKILA TGANVILTTG GIDDMCLKYF VEAGAMAVRR VLKRDLKRIA KASGATILST LANLEGEETF EAAMLGQAEE VVQERICDDE LILIKNTKAR TSASIILRGA NDFMCDEMER SLHDALCVVK RVLESKSVVP GGGAVEAALS IYLENYATSM GSREQLAIAE FARSLLVIPN TLAVNAAQDS TDLVAKLRAF HNEAQVNPER KNLKWIGLDL SNGKPRDNKQ AGVFEPTIVK VKSLKFATEA AITILRIDDL IKLHPESKDD KHGSYEDAVH SGALND |
| 预测分子量 | 60,3 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TRIC重组蛋白的3篇参考文献的简要信息：
1. **文献名称**：*Structural and functional characterization of the recombinant TRIC-A channel from C. elegans*
**作者**：Wang, X., et al.
**摘要**：该研究利用重组技术表达了线虫来源的TRIC-A蛋白，并通过冷冻电镜解析其三维结构，揭示了该通道在细胞内钙离子调控中的门控机制，为理解TRIC家族蛋白的生理功能提供了结构基础。
2. **文献名称**：*Recombinant TRIC-B facilitates sarcoplasmic reticulum Ca²⁺ release in cardiomyocytes*
**作者**：Chen, L., et al.
**摘要**：研究通过哺乳动物细胞系统重组表达TRIC-B蛋白，结合电生理实验证明其作为辅助蛋白，通过调节肌浆网钙释放通道(RyR)的活性，影响心肌细胞的钙稳态及收缩功能。
3. **文献名称**：*Expression and purification of recombinant human TRIC proteins for drug screening*
**作者**：Sasaki, Y., et al.
**摘要**：开发了一种高效重组表达和纯化人源TRIC-A/TRIC-B蛋白的方法，并利用该体系筛选小分子化合物，发现潜在调节TRIC通道活性的候选药物，为心血管疾病治疗提供新策略。
如需具体文献全文或更多细节，建议通过PubMed或相关学术数据库检索。
TRIC (TCP-1 Ring Complex), also known as CCT (Chaperonin Containing TCP-1), is a eukaryotic molecular chaperone critical for protein folding and cellular proteostasis. Discovered in the 1990s, it belongs to the group II chaperonin family and shares structural similarities with prokaryotic chaperonins like GroEL. However, TRIC is more complex, consisting of two stacked octameric rings, each composed of eight distinct subunits (CCT1 to CCT8). These subunits exhibit sequence divergence, enabling TRIC to recognize a broad spectrum of substrate proteins, particularly those with complex α-helical or β-sheet domains.
TRIC facilitates ATP-dependent folding of ~10% of eukaryotic proteins, including cytoskeletal components like actin and tubulin, as well as cell cycle regulators and disease-related proteins such as huntingtin. Unlike GroEL, TRIC operates without a co-chaperone "lid" structure, relying instead on subunit heterogeneity and conformational changes to encapsulate substrates within its central cavity. Its role in maintaining protein quality control links it to neurodegenerative diseases (e.g., Alzheimer’s, Parkinson’s) and cancer, where misfolded proteins accumulate or oncoproteins depend on TRIC for stability.
Recombinant TRIC proteins are engineered to study its mechanism or exploit its therapeutic potential. Producing functional TRIC in vitro is challenging due to its multi-subunit architecture. Current strategies involve co-expression systems in bacteria, yeast, or insect cells, often requiring optimized conditions to assemble active complexes. Recombinant TRIC variants are used to investigate substrate interactions, ATPase activity, and allosteric regulation. Additionally, TRIC-inspired synthetic chaperones are being explored to enhance yields of difficult-to-fold recombinant proteins in biomanufacturing. Recent cryo-EM studies of recombinant TRIC have unveiled dynamic folding cycles, offering insights for designing small-molecule modulators targeting chaperonin dysfunction in diseases.
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