| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ERP27 |
| Uniprot No | Q96DN0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-273aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MEVEKSSDGP GAAQEPTWLT DVPAAMEFIA ATEVAVIGFF QDLEIPAVPI LHSMVQKFPG VSFGISTDSE VLTHYNITGN TICLFRLVDN EQLNLEDEDI ESIDATKLSR FIEINSLHMV TEYNPVTVIG LFNSVIQIHL LLIMNKASPE YEENMHRYQK AAKLFQGKIL FILVDSGMKE NGKVISFFKL KESQLPALAI YQTLDDEWDT LPTAEVSVEH VQNFCDGFLS GKLLKENRES EGKTPKVEL |
| 预测分子量 | 30 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ERP27重组蛋白的模拟参考文献示例(非真实文献，仅供格式参考)：
1. **标题**：*"ERP27: A Novel Endoplasmic Reticulum Protein Involved in Disulfide Bond Formation"*
**作者**：Zhang L, et al.
**摘要**：研究通过哺乳动物细胞重组表达ERP27.发现其与PDI(蛋白质二硫键异构酶)协同作用，参与内质网中蛋白质折叠的氧化还原调控，并证明其缺失导致错误折叠蛋白积累。
2. **标题**：*"Recombinant ERP27 Expression in E. coli and Its Role in Cellular Stress Response"*
**作者**：Smith J, Wang Y.
**摘要**：报道了在大肠杆菌系统中高效表达ERP27重组蛋白的优化方法，并发现其在热休克条件下稳定内质网应激相关蛋白，可能作为细胞应激反应的调控因子。
3. **标题**：*"Structural Analysis of ERP27 Reveals a Dual Chaperone Function in Cancer Cells"*
**作者**：Chen R, et al.
**摘要**：通过X射线晶体学解析ERP27重组蛋白的三维结构，揭示其通过两个独立结构域分别结合未折叠蛋白和钙离子，在乳腺癌细胞中抑制凋亡并促进耐药性。
4. **标题**：*"ERP27 Knockdown Impairs Secretory Pathway Efficiency in Recombinant Protein Production"*
**作者**：Kim S, et al.
**摘要**：利用CRISPR技术敲低ERP27.发现其在CHO细胞重组抗体生产中显著降低分泌效率，提示ERP27是工业重组蛋白生产的关键质量控制因子。
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**注意**：以上为模拟示例，实际文献需通过PubMed、Web of Science或Google Scholar等平台检索关键词(如"ERP27 recombinant protein" "ERP27 function")。如需真实文献，建议访问相关数据库并筛选近年高被引研究。
ERP27 (Endoplasmic Reticulum Protein 27), also known as ERp27 or PDIA5. is a member of the protein disulfide isomerase (PDI) family located in the endoplasmic reticulum (ER). It plays a critical role in protein folding and quality control by facilitating disulfide bond formation and isomerization during the maturation of secretory and membrane proteins. Unlike classical PDIs, ERP27 lacks a canonical C-terminal redox-active thioredoxin domain but retains a non-catalytic N-terminal domain that enables substrate binding and chaperone-like activity. This unique structural feature suggests its specialization in assisting substrate recognition or cooperating with other redox-active PDIs like PDI and ERp57.
ERP27 is ubiquitously expressed across tissues, with higher levels in secretory cells such as hepatocytes and pancreatic β-cells. It is implicated in maintaining ER homeostasis under stress conditions, such as hypoxia or nutrient deprivation, by mitigating unfolded protein response (UPR) activation. Studies link ERP27 dysregulation to diseases including cancer, neurodegenerative disorders, and metabolic syndromes. For instance, it may promote cancer cell survival by enhancing folding of oncogenic clients or modulating ER stress signaling.
Recombinant ERP27 is typically produced in E. coli or mammalian expression systems for structural and functional studies. Its recombinant form aids in elucidating mechanisms of ER protein folding networks and serves as a tool for drug screening targeting ER stress-related pathologies. Recent research focuses on its interaction with client proteins, redox-independent chaperone functions, and therapeutic potential in diseases driven by proteostatic imbalance. Further exploration of ERP27 could advance precision medicine strategies for conditions linked to ER dysfunction.
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