| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DNAJC24 |
| Uniprot No | Q6P3W2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-148aa |
| 氨基酸序列 | MAVEQMPKKD WYSILGADPS ANISDLKQKY QKLILMYHPD KQSTDVPAGT VEECVQKFIE IDQAWKILGN EETKREYDLQ RCEDDLRNVG PVDAQVYLEE MSWNEGDHSF YLSCRCGGKY SVSKDEAEEV SLISCDTCSL IIELLHYN |
| 预测分子量 | 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DNAJC24重组蛋白的3篇参考文献的简要信息：
1. **文献名称**：*DNAJC24 regulates the molecular chaperone function of HSPA8 through direct interaction*
**作者**：Zhang, Y., et al.
**摘要**：该研究报道了重组DNAJC24蛋白与热休克蛋白HSPA8的相互作用机制，证明DNAJC24通过调控HSPA8的ATP酶活性，影响其分子伴侣功能，为癌症中蛋白质错误折叠相关机制提供新见解。
2. **文献名称**：*Recombinant expression and functional characterization of DNAJC24 in neurodegenerative disease models*
**作者**：Smith, J.P., et al.
**摘要**：通过在大肠杆菌中表达重组DNAJC24蛋白，研究发现其可减少α-突触核蛋白在帕金森病模型中的异常聚集，提示其在神经退行性疾病中的潜在治疗作用。
3. **文献名称**：*Structural insights into the client recognition mechanism of DNAJC24*
**作者**：Tanaka, R., et al.
**摘要**：利用重组DNAJC24的晶体结构分析，揭示了其J结构域与客户蛋白结合的特定氨基酸残基，阐明了底物识别机制，为设计靶向分子伴侣的小分子奠定基础。
注：上述文献为示例，实际研究中建议通过PubMed或Web of Science以“DNAJC24 recombinant”等关键词检索最新文献。
DNAJC24 is a member of the DNAJ/Hsp40 protein family, which plays a critical role as a co-chaperone in regulating the activity of heat shock protein 70 (Hsp70). These proteins are essential for maintaining cellular proteostasis by assisting in protein folding, preventing aggregation, and facilitating the degradation of misfolded proteins. DNAJC24. also known as J-domain-containing protein 24. contains a conserved J-domain that enables interaction with Hsp70. stimulating its ATPase activity to drive substrate binding and processing. Unlike some DNAJ family members, DNAJC24 lacks additional domains, suggesting specialized or context-dependent functions.
Recombinant DNAJC24 is engineered for in vitro and in vivo studies to dissect its molecular mechanisms. Produced via heterologous expression systems (e.g., E. coli or mammalian cells), it enables researchers to explore its role in protein quality control pathways, stress responses, and disease-related processes. Dysregulation of chaperone systems is linked to neurodegenerative diseases (e.g., Alzheimer’s, Parkinson’s) and cancer, positioning DNAJC24 as a potential therapeutic target. Recombinant forms allow structural analysis (e.g., crystallography), interaction mapping with Hsp70 or client proteins, and screening for small-molecule modulators.
Recent studies highlight DNAJC24’s tissue-specific expression and involvement in stress adaptation, though its precise substrates remain less characterized compared to other DNAJ proteins. Its recombinant production facilitates functional studies, such as assessing its impact on amyloid aggregation or autophagy-lysosomal pathways. Ongoing research aims to clarify its regulatory networks and therapeutic potential, leveraging recombinant tools to bridge molecular insights with disease applications.
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