| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DNAJB12 |
| Uniprot No | Q9NXW2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-375aa |
| 氨基酸序列 | MESNKDEAERCISIALKAIQSNQPDRALRFLEKAQRLYPTPRVRALIESLNQKPQTAGDQPPPTDTTHATHRKAGGTDAPSANGEAGGESTKGYTAEQVAAVKRVKQCKDYYEILGVSRGASDEDLKKAYRRLALKFHPDKNHAPGATEAFKAIGTAYAVLSNPEKRKQYDQFGDDKSQAARHGHGHGDFHRGFEADISPEDLFNMFFGGGFPSSNVHVYSNGRMRYTYQQRQDRRDNQGDGGLGVFVQLMPILILILVSALSQLMVSSPPYSLSPRPSVGHIHRRVTDHLGVVYYVGDTFSEEYTGSSLKTVERNVEDDYIANLRNNCWKEKQQKEGLLYRARYFGDTDMYHRAQKMGTPSCSRLSEVQASLHG |
| 分子量 | 68.3 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 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3篇关于重组人DNAJB12蛋白的研究文献摘要概览：
1. **文献名称**：*DNAJB12 is a novel factor in regulating mitochondrial dynamics through its role in Parkin-mediated mitophagy*
**作者**：Lee S. et al.
**摘要**：该研究揭示了DNAJB12通过调控Parkin蛋白介导的线粒体自噬过程，影响线粒体动态平衡。重组人DNAJB12的体外实验表明其通过与Parkin互作增强受损线粒体的清除能力。
2. **文献名称**：*Expression and functional characterization of recombinant human DNAJB12 in cancer cell proliferation*
**作者**：Wang Y. et al.
**摘要**：研究团队在大肠杆菌系统中成功表达并纯化重组人DNAJB12蛋白，发现其过表达抑制肺癌细胞增殖，可能通过干扰HSP70复合体的致癌信号通路实现。
3. **文献名称**：*Structural insights into the chaperone activity of DNAJB12: A cryo-EM study*
**作者**：Zhang H. et al.
**摘要**：通过冷冻电镜解析重组人DNAJB12蛋白的复合体结构，发现其J结构域与HSP70结合模式独特，进一步阐释了其在蛋白质错误折叠疾病中的潜在修复机制。
注：以上文献信息为示例性虚构，真实文献需通过PubMed或Web of Science检索确认。建议使用关键词“recombinant DNAJB12”、“human DNAJB12 function”及“HSP40 chaperone”查询最新论文。
Recombinant human DNAJB12 protein is a molecular chaperone belonging to the heat shock protein 40 (Hsp40/DnaJ) family. It plays a critical role in proteostasis by regulating the ATPase activity of Hsp70 chaperones via its conserved J-domain. DNAJB12 is localized to the endoplasmic reticulum (ER) and cytosol, where it assists in folding nascent polypeptides, preventing aggregation of misfolded proteins, and directing terminally misfolded clients to ER-associated degradation (ERAD) pathways. Structurally, it contains a J-domain for Hsp70 interaction, a glycine/phenylalanine-rich region, and a C-terminal substrate-binding domain.
The recombinant form is typically expressed in bacterial or mammalian systems, enabling studies on its chaperone mechanisms, substrate specificity, and interactions with co-chaperones. Dysregulation of DNAJB12 has been implicated in diseases linked to proteostatic stress, including neurodegenerative disorders (e.g., Alzheimer's and Parkinson's) and cancers, where its overexpression correlates with tumor progression and chemoresistance. Additionally, DNAJB12 facilitates infection cycles of certain viruses by stabilizing viral proteins. Research on recombinant DNAJB12 provides insights into cellular stress responses and potential therapeutic strategies targeting protein misfolding pathologies. Its application extends to in vitro assays screening small molecules that modulate chaperone networks or ERAD efficiency.
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