| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CHMP6 |
| Uniprot No | Q96FZ7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-201aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMGNLFG RKKQSRVTEQ DKAILQLKQQ RDKLRQYQKR IAQQLERERA LARQLLRDGR KERAKLLLKK KRYQEQLLDR TENQISSLEA MVQSIEFTQI EMKVMEGLQF GNECLNKMHQ VMSIEEVERI LDETQEAVEY QRQIDELLAG SFTQEDEDAI LEELSAITQE QIELPEVPSE PLPEKIPENV PVKARPRQAE LVAAS |
| 预测分子量 | 26 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CHMP6重组蛋白的3篇代表性文献示例(注：文献信息为示例，具体内容需查阅实际数据库获取)：
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1. **文献名称**: "Structural basis for ESCRT-III CHMP6 filament assembly"
**作者**: Henne, W.M. et al.
**摘要**: 本研究解析了CHMP6重组蛋白的晶体结构，揭示其通过螺旋结构形成多聚化纤维的分子机制，并阐明其在ESCRT-III复合体中调控膜重塑的功能基础。
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2. **文献名称**: "CHMP6 and VPS4A interactions in HIV-1 budding"
**作者**: McCullough, J. et al.
**摘要**: 利用重组CHMP6蛋白进行体外结合实验，证明其与VPS4 ATP酶的直接互作对HIV-1病毒颗粒的释放至关重要，揭示了ESCRT通路在病毒出芽中的作用机制。
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3. **文献名称**: "Recombinant CHMP6 rescues autophagy defects in neurodegenerative disease models"
**作者**: Lee, J.A. et al.
**摘要**: 通过表达并纯化功能性CHMP6重组蛋白，研究发现其可恢复神经元细胞中异常的自噬体形成，为治疗tau蛋白病理相关疾病提供潜在靶点。
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**提示**：以上文献为示例，实际研究请通过PubMed、Google Scholar等平台检索关键词“CHMP6 recombinant protein”或“CHMP6 ESCRT”获取最新进展。
CHMP6 (Charged Multivesicular Body Protein 6) is a critical component of the Endosomal Sorting Complex Required for Transport (ESCRT) machinery, specifically within the ESCRT-III subcomplex. This conserved protein plays a central role in membrane remodeling processes, including multivesicular body (MVB) formation, cytokinesis, viral budding, and membrane repair. Structurally, CHMP6 adopts an autoinhibited monomeric conformation in the cytosol until recruited to target membranes, where it polymerizes into helical filaments to drive membrane deformation and scission.
Recombinant CHMP6 proteins are engineered for in vitro studies to dissect its molecular interactions, structural dynamics, and regulatory mechanisms. Typically produced in bacterial or mammalian expression systems, these purified proteins retain the ability to oligomerize and bind key partners like VPS4 ATPase and other ESCRT-III subunits. Researchers utilize CHMP6 recombinant proteins to reconstitute ESCRT-mediated processes in cell-free systems, analyze disease-associated mutations (linked to neurodegenerative disorders and cancer), and screen for potential modulators of membrane-remodeling activity. Its role in HIV-1 budding and nuclear envelope resealing has also made it a candidate for antiviral strategies and tissue repair studies. The development of active recombinant CHMP6 continues to advance our understanding of cellular homeostasis and pathological membrane-related processes.
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