| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DNAJC7 |
| Uniprot No | Q99615 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-484aa |
| 氨基酸序列 | MAATEPELLDDQEAKREAETFKEQGNAYYAKKDYNEAYNYYTKAIDMCPKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAQQEFKNANAVMEYEKIAETDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHEKACIACRNAKALKAKKEDGNKAFKEGNYKLAYELYTEALGIDPNNIKTNAKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKAYLRRAQCYMDTEQYEEAVRDYEKVYQTEKTKEHKQLLKNAQLELKKSKRKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEVQKEEEKKFKEVGEAFTILSDPKKKTRYDSGQDLDEEGMNMGDFDPNNIFKAFFGGPGGFSFEASGPGNFFFQFG |
| 分子量 | 78.98 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3篇与重组人DNAJC7蛋白研究相关的虚构参考文献(基于真实研究背景编写)：
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1. **Title**: "Recombinant human DNAJC7 chaperone inhibits tau aggregation in Alzheimer's disease models"
**Authors**: Chen L., et al.
**Summary**: 研究利用大肠杆菌系统表达了重组人DNAJC7蛋白，发现其作为HSP40辅助伴侣蛋白可抑制tau蛋白的病理性聚集，机制可能与增强HSP70的ATP酶活性有关，为神经退行性疾病治疗提供新靶点。
2. **Title**: "Structural characterization of DNAJC7's J-domain interaction with HSP70"
**Authors**: Yamamoto S., et al.
**Summary**: 通过X射线晶体学解析重组DNAJC7蛋白的J-domain与HSP70复合体结构，揭示其通过保守的HPD基序调控HSP70的构象变化，阐明该分子伴侣在蛋白质折叠中的关键作用机制。
3. **Title**: "DNAJC7 variants impair proteostasis in prion disease pathogenesis"
**Authors**: Rodriguez A., et al.
**Summary**: 发现朊病毒病患者中DNAJC7基因突变导致重组蛋白功能障碍，无法协助HSP70清除错误折叠的PrP蛋白，首次将DNAJC7缺陷与朊蛋白病理毒性关联。
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注：以上文献为示例性内容，实际研究需查阅PubMed等数据库(可尝试关键词："DNAJC7 recombinant"、"DNAJC7 chaperone function")。真实存在的相关研究多集中于DNAJC7在神经退行性疾病中作为分子伴侣的功能探索。
DNAJC7 is a member of the HSP40/DNAJ protein family, which functions as co-chaperones to regulate the activity of HSP70 chaperones. As a molecular chaperone, DNAJC7 plays a critical role in maintaining proteostasis by assisting in the folding, stabilization, and degradation of misfolded proteins. It is expressed in various tissues, including the brain, liver, and kidney, with prominent roles in cellular stress responses. The protein contains a conserved J-domain that mediates interactions with HSP70 to stimulate ATPase activity, facilitating substrate recognition and processing. Additionally, DNAJC7 may possess substrate-binding regions to directly engage with client proteins.
Recombinant human DNAJC7 protein is engineered using expression systems (e.g., E. coli, mammalian cells) to enable functional studies. Its production allows researchers to dissect molecular mechanisms underlying protein quality control pathways, particularly in neurodegenerative diseases like Alzheimer's and Parkinson's, where protein aggregation is a hallmark. DNAJC7’s involvement in cancer progression and cellular stress adaptation has also drawn attention, with studies exploring its role in tumorigenesis and chemoresistance. The recombinant form is pivotal for structural analyses, biochemical assays, and screening therapeutic compounds targeting chaperone-mediated processes. Despite progress, its precise substrates and disease-specific regulatory networks remain partially characterized, necessitating further exploration.
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