| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DNAJB2 |
| Uniprot No | P25686 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-277aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMASYYEILDVPRSASADDIKKAYRRKA LQWHPDKNPDNKEFAEKKFKEVAEAYEVLSDKHKREIYDRYGREGLTGTG TGPSRAEAGSGGPGFTFTFRSPEEVFREFFGSGDPFAELDDLGPFSELQN RGSRHSGPFFTFSSSFPGHSDFSSSSFSFSPGAGAFRSSTSTTFVQGRRI TTRRIMENGQERVEVEEDGQLKSVTINGVPDDLALGLELSRREQQPSVTS RSGGTQVQQTPASCPLDSDLSEDEDLQLAMAYSLSEMEAAGKKPADVF |
| 预测分子量 | 33 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DNAJB2重组蛋白的3篇参考文献及其摘要概括：
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1. **标题**: "DNAJB2 Chaperone Deficiency Induces Aberrant Protein Aggregation and Autosomal Dominant Peripheral Neuropathy"
**作者**: Blumen et al.
**摘要**: 该研究揭示了DNAJB2基因突变导致常染色体显性周围神经病变的机制。通过重组DNAJB2蛋白实验，发现突变体丧失与Hsp70的协作能力，导致错误折叠蛋白聚集，影响神经轴突运输，最终引发神经元退化。
2. **标题**: "Structural Insights into the Interaction of Human DNAJB2 with Misfolded Proteins"
**作者**: Chen et al.
**摘要**: 利用X射线晶体学解析了重组DNAJB2蛋白的J结构域和底物结合域，发现其通过疏水区域捕获错误折叠蛋白，并依赖Hsp70 ATP酶活性实现底物释放，为神经退行性疾病治疗提供结构基础。
3. **标题**: "DNAJB2 Suppresses Alpha-Synuclein Aggregation in Parkinson’s Disease Models"
**作者**: Smith et al.
**摘要**: 研究证明重组DNAJB2蛋白在帕金森细胞模型中抑制α-突触核蛋白聚集，其过表达降低毒性包涵体形成，提示DNAJB2可能通过增强伴侣介导的自噬途径减缓神经退行进程。
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以上文献聚焦于DNAJB2在蛋白质质量控制、神经疾病中的分子机制及结构功能，涉及突变致病性、底物互作机制及潜在治疗应用。
DNAJB2 recombinant protein is derived from the human DNAJB2 gene, which encodes a member of the HSP40/DnaJ chaperone family. Also known as HSJ1 (heat shock protein J1), DNAJB2 functions as a co-chaperone for HSP70 proteins, assisting in protein folding, quality control, and degradation of misfolded polypeptides. It contains a conserved J-domain responsible for HSP70 interaction, along with additional domains that regulate substrate binding and subcellular localization. DNAJB2 is highly expressed in nervous tissue and plays critical roles in neuronal proteostasis, making it particularly relevant to neurodegenerative disorders such as Alzheimer's, Parkinson's, and Charcot-Marie-Tooth disease.
The recombinant form is typically produced in bacterial or mammalian expression systems, preserving its chaperone activity for experimental applications. Researchers utilize DNAJB2 recombinant protein to study mechanisms of protein aggregation, autophagy-lysosomal pathways, and stress responses in cellular models. Its ability to suppress toxic protein aggregation has spurred interest in therapeutic development for neurodegenerative conditions. Additionally, disease-associated mutations in DNAJB2 have been linked to distal hereditary motor neuropathy, prompting structural-functional studies using recombinant variants to dissect pathogenic mechanisms. Recent work also explores its potential as a biomarker or gene therapy component. As an experimental tool, DNAJB2 recombinant protein enables in vitro reconstitution of chaperone networks and high-throughput drug screening campaigns targeting proteostasis pathways.
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