| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DNAJC5G |
| Uniprot No | Q8N7S2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-189aa |
| 氨基酸序列 | MSTVKEAAHR LSKSEMSLYA VLDLKKGASP EDFKKSYSHS ALLPHPPFEY HLGRKLALRY HPDKNPGNAQ AAEIFKEINA AHAILSDSKK RKIYDQHGSL GIYLYDHFGE EGVRYYFILN SCWFKTLVIL CTLLTCCCFC CCCCFCCGAL KPPPEQDSGR KYQQNVQSQP PRSGAKCDFR SEENSEDDF |
| 分子量 | 21.4 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. |
以下为模拟生成的3篇关于重组人DNAJC5G蛋白的参考文献(注：内容为虚构，仅供示例参考)：
1. **文献名称**: "Characterization of Recombinant Human DNAJC5G: Chaperone Activity and Lysosomal Interaction"
**作者**: Zhang, L. et al.
**摘要**: 本研究成功在大肠杆菌中表达并纯化了重组人DNAJC5G蛋白，证实其具有ATP酶活性，并可通过结合HSP70调控溶酶体相关膜蛋白的稳定性。荧光标记实验显示DNAJC5G定位于溶酶体膜，提示其在细胞应激中起保护作用。
2. **文献名称**: "DNAJC5G Expression Attenuates Tau Aggregation in Neurodegenerative Models"
**作者**: Rodriguez, S.M. & Kumar, P.
**摘要**: 通过体外实验证明，重组DNAJC5G可抑制tau蛋白异常聚集，减少神经细胞毒性。在阿尔茨海默病模型中，过表达DNAJC5G改善了神经元存活率，提示其作为治疗神经退行性疾病的潜在靶点。
3. **文献名称**: "CRISPR/Cas9-based Knockout of DNAJC5G Disrupts Autophagic Flux in HeLa Cells"
**作者**: Tanaka, H. et al.
**摘要**: 利用基因编辑技术敲除DNAJC5G后，HeLa细胞的自噬小体-溶酶体融合受阻，导致自噬流异常。补充重组DNAJC5G蛋白可部分恢复功能，表明其在自噬调控中发挥关键作用。
4. **文献名称**: "Structural Insights into DNAJC5G’s Role in Prion-like Domain Recognition"
**作者**: Wei, X. et al.
**摘要**: 通过冷冻电镜解析DNAJC5G与病理性淀粉样蛋白的复合物结构，揭示了其J结构域特异性识别朊病毒样结构域的分子机制，为设计靶向分子伴侣药物提供了结构基础。
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注：以上文献信息均为虚构模拟，实际研究中请通过PubMed、Web of Science等平台检索真实文献。
The human DNAJC5G protein, a member of the J-domain protein family, functions as a co-chaperone in cellular processes involving heat shock proteins (HSPs), particularly HSP70. It shares homology with cysteine string protein (CSPα), playing critical roles in synaptic vesicle cycling, membrane trafficking, and neuroprotection. DNAJC5G is enriched in neuronal tissues and interacts with components of the SNARE complex, aiding in vesicle fusion and neurotransmitter release. Its unique N-terminal J-domain facilitates ATPase activation in HSP70. while the conserved "cysteine-string" domain (palmitoylation site) enables membrane association, crucial for synaptic transmission. Dysregulation of DNAJC5G is linked to lysosomal storage disorders (e.g., Gaucher disease) and neurodegenerative conditions, as it modulates lysosomal enzyme transport via the mannose-6-phosphate pathway. Recombinant DNAJC5G, typically produced in E. coli or mammalian systems with affinity tags (e.g., His-tag), enables studies on protein-protein interactions, vesicle dynamics, and lysosomal dysfunction. Recent research explores its therapeutic potential in rescuing synaptic defects or restoring lysosomal enzyme trafficking. Structural analyses reveal roles in lipid raft organization and exosome release, highlighting its dual impact on cellular proteostasis and membrane biology. This protein remains a focus for understanding neurodegenerative pathologies and developing targeted molecular therapies.
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