| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DNAJB1 |
| Uniprot No | P25685 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-340aa |
| 氨基酸序列 | MGKDYYQTLGLARGASDEEIKRAYRRQALRYHPDKNKEPGAEEKFKEIAEAYDVLSDPRKREIFDRYGEEGLKGSGPSGGSGGGANGTSFSYTFHGDPHAMFAEFFGGRNPFDTFFGQRNGEEGMDIDDPFSGFPMGMGGFTNVNFGRSRSAQEPARKKQDPPVTHDLRVSLEEIYSGCTKKMKISHKRLNPDGKSIRNEDKILTIEVKKGWKEGTKITFPKEGDQTSNNIPADIVFVLKDKPHNIFKRDGSDVIYPARISLREALCGCTVNVPTLDGRTIPVVFKDVIRPGMRRKVPGEGLPLPKTPEKRGDLIIEFEVIFPERIPQTSRTVLEQVLPI |
| 分子量 | 65.0 kDa |
| 蛋白标签 | His tag N-Terminus |
| 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. |
以下是与重组人DNAJB1蛋白相关的3篇文献示例(文献信息为模拟创作，实际引用需核实)：
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1. **文献名称**：*DNAJB1 acts as a molecular chaperone to regulate the stability of HSP70 clients in cancer cells*
**作者**：Smith A, et al.
**摘要**：研究重组人DNAJB1蛋白与HSP70的相互作用机制，发现其通过增强HSP70对肿瘤相关蛋白的折叠能力，促进癌细胞存活。实验表明重组DNAJB1在体外可抑制错误折叠蛋白的聚集。
2. **文献名称**：*Recombinant DNAJB1 suppresses α-synuclein aggregation in Parkinson’s disease models*
**作者**：Chen L, et al.
**摘要**：利用重组DNAJB1蛋白在帕金森病细胞模型中干预α-突触核蛋白的异常聚集，证明其通过激活HSP70介导的清除途径，减少神经元毒性，为神经退行性疾病提供潜在治疗策略。
3. **文献名称**：*Structural analysis of the human DNAJB1-HSP70 complex by cryo-EM*
**作者**：Kimura T, et al.
**摘要**：通过冷冻电镜解析重组人DNAJB1与HSP70的复合物结构，揭示DNAJB1通过J结构域传递变构信号，调控HSP70的ATP酶活性，为靶向分子伴侣的药物设计提供依据。
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**说明**：以上内容为领域内典型研究方向(癌症、神经疾病、结构生物学)的模拟示例，实际文献需通过学术数据库(如PubMed、Web of Science)检索关键词“recombinant DNAJB1”或“DNAJB1 HSP40”获取。
**Background of Recombinant Human DNAJB1 Protein**
The DNAJB1 protein, also known as HSP40 (heat shock protein 40) or Hdj1. is a member of the Hsp40/DnaJ chaperone family, which plays a critical role in regulating protein homeostasis. Functioning as a co-chaperone for Hsp70. DNAJB1 facilitates ATP hydrolysis and substrate binding, enabling proper folding, stabilization, and intracellular trafficking of client proteins. It contains a conserved J-domain that mediates interaction with Hsp70. along with substrate-binding regions that recognize misfolded or denatured proteins, particularly under stress conditions.
Recombinant DNAJB1 is engineered through heterologous expression systems (e.g., *E. coli* or mammalian cells) to study its molecular mechanisms and therapeutic potential. Its roles span cellular stress responses, proteostasis, and protection against protein aggregation linked to neurodegenerative diseases (e.g., Alzheimer’s, Parkinson’s) and cancer. Studies highlight its ability to suppress toxic protein aggregates, modulate autophagy, and regulate apoptosis, making it a target for drug development.
As a research tool, recombinant DNAJB1 aids in elucidating chaperone networks, while its therapeutic applications are explored for diseases involving proteotoxic stress. Its conserved structure-function dynamics across species also make it valuable for comparative studies in molecular biology and translational medicine.
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