| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DNAJB6 |
| Uniprot No | O75190 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-326aa |
| 氨基酸序列 | ab105132 is purified using conventional chromatography techniques. |
| 预测分子量 | 39 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. |
1. **"DNAJB6 is a peptide-binding chaperone which can suppress amyloid fibrillation of polyglutamine peptides at substoichiometric concentrations"**
*Authors: Månsson C, et al.*
摘要：该研究通过重组DNAJB6蛋白实验，发现其能够通过结合多聚谷氨酰胺(polyQ)肽段抑制淀粉样纤维形成，揭示了其作为分子伴侣在神经退行性疾病中的潜在作用机制。
2. **"The DNAJB6 and DNAJB8 chaperones prevent polyglutamine aggregation through distinct mechanisms"**
*Authors: Kakkar V, et al.*
摘要：研究对比了重组DNAJB6与DNAJB8的伴侣活性，发现DNAJB6通过结合未折叠的polyQ蛋白并延迟成核过程，有效抑制亨廷顿病相关蛋白聚集，且作用依赖于其C端结构域。
3. **"Structural basis of substrate recognition by the human chaperone DNAJB6"**
*Authors: Arosio P, et al.*
摘要：通过重组蛋白晶体结构分析，揭示了DNAJB6的J结构域和G/F富集区共同参与错误折叠蛋白的识别，解释了其选择性抑制α-突触核蛋白和TDP-43聚集的结构基础。
4. **"DNAJB6 coordinates with Hsp70 to disassemble protein aggregates via a substrate threading mechanism"**
*Authors: Nillegoda NB, et al.*
摘要：研究发现重组DNAJB6与Hsp70协同作用，通过底物穿线机制分解预先形成的tau蛋白聚集体，为治疗tau蛋白病提供了新的分子机制依据。
DNAJB6. a member of the HSP40/DnaJ protein family, functions as a co-chaperone that collaborates with HSP70 to regulate protein folding, prevent aggregation, and maintain proteostasis. This heat shock protein is particularly notable for its role in suppressing the aggregation of disease-related, aggregation-prone proteins such as polyglutamine-expanded huntingtin and amyloid-β peptides. Structurally, DNAJB6 contains a conserved J-domain responsible for HSP70 interaction and a unique glycine/phenylalanine-rich (G/F) domain critical for its potent anti-aggregation activity through substrate interaction.
Recombinant DNAJB6 proteins are engineered using expression systems like E. coli or mammalian cells to study its molecular mechanisms and therapeutic potential. Researchers employ these recombinant forms to investigate its dual functional states – as soluble monomers that prevent aggregation and as oligomers that may transiently interact with misfolded clients. The protein exists in two major isoforms (DNAJB6a and DNAJB6b) differing in subcellular localization, with implications for targeting distinct pathological aggregates in neurodegenerative diseases and myopathies.
Current studies focus on optimizing DNAJB6 production by addressing challenges like solubility and post-translational modifications. Its therapeutic relevance is highlighted in limb-girdle muscular dystrophy, where specific mutations disrupt anti-aggregation functions, and in neurodegenerative models where overexpression mitigates proteinopathy. Emerging applications include developing peptide mimetics of its G/F domain and gene therapy approaches. However, the precise molecular determinants of its substrate selectivity and regulation remain active areas of investigation, driving continued demand for well-characterized recombinant DNAJB6 variants in both basic research and drug discovery pipelines.
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