| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DNAJC3 |
| Uniprot No | Q13217 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-234aa |
| 氨基酸序列 | MVAPGSVTSRLGSVFPFLLVLVDLQYEGAECGVNADVEKHLELGKKLLAAGQLADALSQFHAAVDGDPDNYIAYYRRATVFLAMGKSKAALPDLTKVIQLKMDFTAARLQRGHLLLKQGKLDEAEDDFKKVVFPVPSLLGLQRSLLDDLYLLFWFFLMKKVTFRCLSSAISECLPQSLNLMKFNLLISFLLLWTVRLVSCLRSIHYAVGSKTFLISSKSFMVLCFIFKPIVYLS |
| 分子量 | 51.48 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. |
以下是关于重组人DNAJC3蛋白的3篇参考文献及其简要摘要：
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1. **文献名称**：*"Recombinant Human DNAJC3 Protein Attenuates ER Stress-Induced Apoptosis via Regulation of the PERK Pathway"*
**作者**：Li X, Wang Y, Zhang H.
**摘要**：本研究在大肠杆菌中成功表达并纯化了重组人DNAJC3蛋白，发现其通过抑制PERK-eIF2α信号通路减轻内质网应激诱导的细胞凋亡，揭示了DNAJC3在调节未折叠蛋白反应中的作用。
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2. **文献名称**：*"Characterization of the Chaperone Activity of Recombinant DNAJC3 in Heat Shock Protein 70-Dependent Folding"*
**作者**：Chen J, Gupta R, Liu S.
**摘要**：作者通过体外实验验证了重组DNAJC3作为HSP70共伴侣蛋白的功能，证明其通过结合HSP70增强底物蛋白的折叠效率，为DNAJC3在蛋白质质量控制中的应用提供了依据。
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3. **文献名称**：*"Expression and Functional Analysis of DNAJC3 in Viral Infection Models"*
**作者**：Kim T, Lee S, Park M.
**摘要**：该研究在哺乳动物细胞中表达了重组DNAJC3.发现其通过抑制病毒蛋白的错误折叠降低病毒复制效率，提示DNAJC3可能参与抗病毒免疫反应。
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**备注**：上述文献为虚拟示例，实际研究需通过PubMed或Google Scholar以关键词“recombinant DNAJC3”、“p58IPK expression”等检索最新论文。
Human DNAJC3. also known as p58^IPK, is a member of the HSP40/DnaJ family of molecular chaperones. It plays a critical role in protein homeostasis, particularly within the endoplasmic reticulum (ER). DNAJC3 interacts with HSP70 to facilitate protein folding, mitigate ER stress, and regulate the unfolded protein response (UPR). Its structure includes a conserved J-domain for HSP70 binding, tetratricopeptide (TPR) motifs for phosphatase interaction, and substrate-binding regions.
This protein is implicated in cellular stress adaptation, where it prevents aggregation of misfolded proteins and aids in their refolding or degradation. Notably, DNAJC3 is involved in modulating insulin biosynthesis and secretion in pancreatic β-cells. Dysregulation or mutations in DNAJC3 are linked to diseases such as Wolcott-Rallison syndrome (neonatal diabetes with multisystemic manifestations), neurodegenerative disorders, and certain cancers.
Recombinant human DNAJC3 protein, produced via expression systems like *E. coli* or mammalian cells, serves as a tool to study ER stress mechanisms, chaperone functions, and disease pathology. Its recombinant form enables *in vitro* analyses of protein-protein interactions, enzymatic activity, and therapeutic screening for conditions tied to ER dysfunction. Research on DNAJC3 contributes to understanding cellular proteostasis and potential interventions for diabetes, neurodegeneration, and cancer.
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