| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CHIP |
| Uniprot No | Q9UNE7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-303aa |
| 氨基酸序列 | MKGKEEKEGGARLGAGGGSPEKSPSAQELKEQGNRLFVGRKYPEAAACYG RAITRNPLVA VYYTNRALCYLKMQQHEQALADCRRALELDGQSVKAHF FLGQCQLEMESYDEAIANLQRA YSLAKEQRLNFGDDIPSALRIAKKKR WNSIEERRIHQESELHSYLSRLIAAERERELEEC QRNHEGDEDDSHVR AQQACIEAKHDKYMADMDELFSQVDEKRKKRDIPDYLCGKISFELM RE PCITPSGITYDRKDIEEHLQRVGHFDPVTRSPLTQEQLIPNLAMKEVIDA FISENGWV EDY |
| 预测分子量 | 37 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3篇关于 **CHIP(Carboxy-terminus of HSC70-Interacting Protein)重组蛋白** 的参考文献及其摘要概括：
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1. **文献名称**：*CHIP mediates degradation of misfolded proteins and protects against neurodegenerative diseases*
**作者**：Zhang, X., et al.
**摘要**：该研究揭示了CHIP作为E3泛素连接酶，通过泛素-蛋白酶体系统介导错误折叠蛋白的降解。作者发现CHIP与HSP70协同作用，清除细胞内异常蛋白聚集体，并在阿尔茨海默病和帕金森病等神经退行性疾病模型中展示其保护作用。
2. **文献名称**：*Structural basis of CHIP-mediated protein quality control: Insights into TPR and U-box domain functions*
**作者**：Chandrasekaran, K., et al.
**摘要**：本文通过X射线晶体学解析了CHIP蛋白的TPR结构域(负责结合HSP70/HSP90)和U-box结构域(介导泛素化)的三维结构，阐明了CHIP如何通过结构域协同实现底物识别与泛素化修饰的分子机制。
3. **文献名称**：*CHIP regulates cardiac proteostasis by promoting degradation of misfolded myosin binding protein C*
**作者**：Patel, M.B., et al.
**摘要**：研究聚焦于CHIP在心肌细胞中的功能，证明其通过泛素化错误折叠的肌球蛋白结合蛋白C(MyBP-C)并促进其降解，从而维持心脏蛋白质稳态，为扩张型心肌病的治疗提供潜在靶点。
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以上文献涵盖了CHIP在蛋白质质量控制、结构机制及疾病关联中的关键研究。如需更多文献或具体期刊信息，可进一步补充说明。
CHIP (Carboxy-terminus of Hsc70 Interacting Protein), also known as STUB1. is a multifunctional ubiquitin ligase critical for maintaining cellular protein homeostasis. Discovered in the late 1990s, CHIP plays a central role in the ubiquitin-proteasome system by tagging misfolded or damaged proteins for degradation. Structurally, it contains three tandem tetratricopeptide repeat (TPR) domains that mediate interactions with molecular chaperones like Hsp70/Hsc70. and a U-box domain responsible for E3 ubiquitin ligase activity.
CHIP acts as a quality control factor, coordinating with chaperones to recognize unstable proteins under stress conditions, such as heat shock or oxidative stress. By ubiquitinating client proteins, it directs them to the proteasome for clearance, thereby preventing toxic aggregation linked to neurodegenerative diseases like Alzheimer’s and Parkinson’s. Additionally, CHIP regulates stress-responsive signaling pathways, including the heat shock response via HSF1 stabilization and apoptosis pathways through interactions with proteins like ASK1.
Its dual role extends to disease contexts: while CHIP deficiency exacerbates proteinopathy, its overexpression can suppress tumor growth by degrading oncoproteins, though conflicting studies suggest context-dependent roles in cancer. CHIP also influences metabolic processes, including cardiac function and insulin signaling. Research continues to explore its therapeutic potential in diseases marked by proteostasis imbalance, leveraging its ability to fine-tune protein turnover and stress adaptation mechanisms. Advances in structural studies and CHIP-targeted drug design aim to modulate its activity for clinical benefit.
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