| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DNAJB8 |
| Uniprot No | Q8NHS0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-232aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMANYYEVLGVQASASPEDIKKAYRKLALRW HPDKNPDNKEEAEKKFKLVSEAYEVLSDSKKRSLYDRAGCDSWRAGGGAS TPYHSPFDTGYTFRNPEDIFREFFGGLDPFSFEFWDSPFNSDRGGRGHGL RGAFSAGFGEFPAFMEAFSSFNMLGCSGGSHTTFSSTSFGGSSSGSSGFK SVMSSTEMINGHKVTTKRIVENGQERVEVEEDGQLKSVTVNGKEQLKWMD SK |
| 预测分子量 | 28 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DNAJB8重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*DNAJB8 regulates the aggregation of α-synuclein in Parkinson’s disease models*
**作者**：Hagihara, H., Ishihara, T., Kudo, K. et al.
**摘要**：该研究通过体外实验证明，重组DNAJB8蛋白能够有效抑制α-突触核蛋白的病理性聚集，并增强其通过泛素-蛋白酶体系统的降解，提示其在神经退行性疾病中的潜在治疗作用。
2. **文献名称**：*DNAJB8 maintains cancer stem cells via chaperone-mediated autophagy suppression*
**作者**：Yoshida, S., Kato, T., Mizutani, A.
**摘要**：研究发现，重组DNAJB8在肾癌干细胞中高表达，通过抑制伴侣介导的自噬(CMA)维持干细胞特性，敲低DNAJB8可显著减少肿瘤形成能力，揭示了其在癌症干细胞中的关键调控机制。
3. **文献名称**：*Structural basis of DNAJB8-HSP70 interaction in protein disaggregation*
**作者**：Li, J., Wang, C., Zhang, Y.
**摘要**：通过冷冻电镜解析重组DNAJB8与HSP70复合物的结构，阐明二者协同解聚错误折叠蛋白的分子机制，为开发靶向蛋白聚集疾病的药物提供结构基础。
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**备注**：上述文献信息为示例性质，实际引用时需以真实发表文章为准。建议通过PubMed或Web of Science以关键词“DNAJB8 recombinant”检索最新研究。
**Background of DNAJB8 Recombinant Protein**
DNAJB8 is a member of the Hsp40/DnaJ protein family, which functions as co-chaperones for Hsp70 to regulate protein folding, disaggregation, and degradation. As a class II Hsp40 protein, DNAJB8 contains a conserved J-domain responsible for Hsp70 interaction, along with additional domains that modulate substrate specificity. Unlike other DnaJ homologs, DNAJB8 exhibits tissue-specific expression, primarily in the testes under normal conditions, but is aberrantly upregulated in certain cancers, such as renal cell carcinoma, where it is linked to tumor progression and chemoresistance.
Biochemically, DNAJB8 suppresses protein aggregation by stabilizing partially unfolded clients, a feature exploited in studies of neurodegenerative diseases involving misfolded proteins (e.g., α-synuclein or tau). Its recombinant form is engineered for in vitro and in vivo research, typically produced in *E. coli* or mammalian expression systems with tags (e.g., His-tag) for purification. Recombinant DNAJB8 retains chaperone activity, validated through ATPase stimulation assays and client protein refolding experiments.
Research applications include elucidating chaperone mechanisms, modeling cancer resistance pathways, and screening therapeutic compounds targeting protein quality control. Its role in stress granules and autophagy regulation further links it to cellular stress responses. Despite limited physiological expression, its cancer-associated overexpression and therapeutic potential make DNAJB8 a focus for developing inhibitors or gene therapies aimed at disrupting oncogenic chaperone networks.
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