| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DnaJ |
| 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 |
| 预测分子量 | 65.0kDa |
| 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DnaJ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**：*"The Hsp70 and Hsp60 chaperone machines"*
**作者**：Hartl, F.U., et al.
**摘要**：该综述系统总结了Hsp70(DnaK)与Hsp40(DnaJ)家族在蛋白质折叠中的协同机制，强调重组DnaJ通过结合底物并激活Hsp70的ATP酶活性，辅助错误折叠蛋白的修复，为体外研究分子伴侣功能提供了理论基础。
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2. **文献名称**：*"Recombinant DnaJ from *Escherichia coli* stimulates the ATPase activity of DnaK and the retention of denatured proteins"*
**作者**：Wall, D., et al.
**摘要**：本研究通过在大肠杆菌中表达并纯化重组DnaJ蛋白，验证其与DnaK的相互作用。实验表明，DnaJ显著增强DnaK的ATP酶活性，并促进对变性蛋白的结合，揭示了其在蛋白质质量控制中的关键作用。
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3. **文献名称**：*"A plant DnaJ homolog enhances thermotolerance in transgenic rice by promoting chloroplast development"*
**作者**：Sarkar, N.K., et al.
**摘要**：通过在水稻中异源表达拟南芥来源的重组DnaJ蛋白，发现其通过调控叶绿体蛋白稳态，显著提升植株耐热性，为利用分子伴侣工程改良作物抗逆性提供了依据。
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4. **文献名称**：*"DnaJ/hsp40 chaperones inhibit α-synuclein aggregation in vitro and in a Parkinson’s disease model"*
**作者**：Luo, G.R., et al.
**摘要**：该研究证明重组DnaJ蛋白在体外和帕金森病模型中均能抑制α-突触核蛋白的异常聚集，减少神经元毒性，提示其作为神经退行性疾病治疗策略的潜力。
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以上文献涵盖DnaJ重组蛋白的功能机制、表达应用及疾病关联研究，均为该领域的代表性成果。
**Background of Recombinant DnaJ Proteins**
DnaJ, a member of the Hsp40 (heat shock protein 40) family, is a highly conserved molecular chaperone critical for protein homeostasis. It functions as a co-chaperone by interacting with Hsp70 to regulate ATPase activity, facilitating protein folding, disaggregation, and stress response. Structurally, DnaJ proteins typically contain a J-domain (responsible for Hsp70 binding), a glycine/phenylalanine-rich (G/F) region, and a substrate-binding C-terminal domain.
Recombinant DnaJ proteins are engineered through genetic cloning and heterologous expression in systems like *E. coli*, yeast, or mammalian cells. These proteins retain the functional domains of native DnaJ but are optimized for stability, solubility, and ease of purification via affinity tags (e.g., His-tag). Their recombinant production enables scalable studies on chaperone mechanisms, protein misfolding diseases (e.g., Alzheimer’s, Parkinson’s), and microbial stress adaptation.
In biotechnology, recombinant DnaJ is used to enhance the yield and solubility of co-expressed proteins by preventing aggregation during heterologous expression. It also serves as a tool in structural biology to stabilize client proteins for crystallization or cryo-EM. Additionally, DnaJ homologs from pathogens (e.g., bacterial DnaJ) are explored as vaccine candidates or antimicrobial targets.
Recent advances focus on engineering DnaJ variants with altered substrate specificity or improved chaperone activity, offering potential therapeutic applications in neurodegenerative diseases and cancer. The study of recombinant DnaJ continues to bridge fundamental biology and industrial innovation, underscoring its versatility in both research and applied sciences.
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