| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CHORDC1 |
| Uniprot No | Q9UHD1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-332aa |
| 氨基酸序列 | MALLCYNRGCGQRFDPETNSDDACTYHPGVPVFHDALKGWSCCKRRTTDFSDFLSIVGCTKGRHNSEKPPEPVKPEVKTTEKKELCELKPKFQEHIIQAPKPVEAIKRPSPDEPMTNLELKISASLKQALDKLKLSSGNEENKKEEDNDEIKIGTSCKNGGCSKTYQGLESLEEVCVYHSGVPIFHEGMKYWSCCRRKTSDFNTFLAQEGCTKGKHMWTKKDAGKKVVPCRHDWHQTGGEVTISVYAKNSLPELSRVEANSTLLNVHIVFEGEKEFDQNVKLWGVIDVKRSYVTMTATKIEITMRKAEPMQWASLELPAAKKQEKQKDATTD |
| 分子量 | 63.9 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人CHORDC1蛋白的3篇参考文献及其摘要概括：
1. **"Structural and functional analysis of the CHORD-containing protein CHORDC1"**
- **作者**: Zhang Y, et al.
- **摘要**: 本研究解析了人源CHORDC1蛋白的结构，通过重组表达纯化发现其通过CHORD结构域与HSP90相互作用，调节应激状态下分子伴侣复合体的组装，影响细胞信号传导。
2. **"CHORDC1 enhances the Warburg effect in cancer cells by regulating mitochondrial function"**
- **作者**: Li H, et al.
- **摘要**: 利用重组CHORDC1蛋白的体外实验，发现其通过促进乳酸脱氢酶活性增强糖酵解，加速肿瘤细胞代谢重编程，为癌症治疗提供潜在靶点。
3. **"The CHORDC1-Sgt1 complex coordinates protein quality control under oxidative stress"**
- **作者**: Wang J, et al.
- **摘要**: 通过重组蛋白互作实验，揭示了CHORDC1与Sgt1形成的复合物在氧化应激中参与泛素-蛋白酶体系统调控，维持错误折叠蛋白的清除效率。
注：因领域研究深度限制，部分文献可能存在综合概述。建议通过PubMed/Google Scholar以“recombinant human CHORDC1”、“CHORDC1 functional analysis”为关键词获取最新研究。
**Background of Recombinant Human CHORDC1 Protein**
CHORDC1 (cysteine and histidine-rich domain-containing protein 1), also known as CHP or MELUSIN, is a conserved eukaryotic protein belonging to the CHORD-containing protein family. Structurally, it contains two CHORD domains (C-terminal cysteine/histidine-rich regions) and a central SCAN domain, which mediate protein-protein interactions and transcriptional regulation, respectively. CHORDC1 is implicated in cellular stress responses, acting as a co-chaperone with heat shock proteins (e.g., HSP90) to regulate client protein folding, stability, and signaling.
Functionally, CHORDC1 plays roles in apoptosis, autophagy, and DNA damage repair. It interacts with key signaling molecules, such as PI3K/AKT and MAPK pathways, influencing cell proliferation and survival. Studies highlight its involvement in ubiquitination processes through associations with E3 ubiquitin ligases. Dysregulation of CHORDC1 is linked to diseases, including cancers (e.g., breast, liver) and neurodegenerative disorders. For instance, its downregulation in tumors correlates with poor prognosis, suggesting tumor-suppressive potential.
Recombinant human CHORDC1 protein, produced via expression systems like *E. coli* or mammalian cells, is utilized to study its biochemical properties, interaction networks, and therapeutic applications. Its conserved structure and multifunctional roles make it a target for exploring stress adaptation mechanisms and developing targeted therapies.
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