| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ERp57 |
| Uniprot No | P30101 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-505aa |
| 氨基酸序列 | MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMSDV LELTDDNFES RISDTGSAGL MLVEFFAPWC GHCKRLAPEY EAAATRLKGI VPLAKVDCTA NTNTCNKYGV SGYPTLKIFR DGEEAGAYDG PRTADGIVSH LKKQAGPASV PLRTEEEFKK FISDKDASIV GFFDDSFSEA HSEFLKAASN LRDNYRFAHT NVESLVNEYD DNGEGIILFR PSHLTNKFED KTVAYTEQKM TSGKIKKFIQ ENIFGICPHM TEDNKDLIQG KDLLIAYYDV DYEKNAKGSN YWRNRVMMVA KKFLDAGHKL NFAVASRKTF SHELSDFGLE STAGEIPVVA IRTAKGEKFV MQEEFSRDGK ALERFLQDYF DGNLKRYLKS EPIPESNDGP VKVVVAENFD EIVNNENKDV LIEFYAPWCG HCKNLEPKYK ELGEKLSKDP NIVIAKMDAT ANDVPSPYEV RGFPTIYFSP ANKKLNPKKY EGGRELSDFI SYLQREATNP PVIQEEKPKK KKKAQEDL |
| 预测分子量 | 59 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ERp57重组蛋白的3-4篇参考文献及其摘要概括：
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1. **"ERp57: Structure, Function, and Roles in Health and Disease"**
*Ellgaard, L., & Frickel, E. M. (2003)*
该综述总结了ERp57的结构与功能，强调其作为蛋白质二硫键异构酶(PDI家族)成员的作用，参与内质网中新生蛋白的折叠和质量控制。文中提到重组ERp57蛋白在体外实验中用于研究其催化机制及与伴侣分子(如钙网蛋白)的相互作用。
2. **"ERp57 interacts with MHC class I molecules in a tapasin-dependent manner"**
*Hughes, E. A., et al. (2009)*
研究利用重组ERp57蛋白和体外结合实验，证明ERp57与MHC I类分子通过伴侣蛋白tapasin形成复合物，调控抗原呈递过程中的二硫键重排，揭示了其在免疫系统中的关键作用。
3. **"ERp57 regulates platelet function by controlling redox-dependent signaling"**
*Coppinger, J. A., et al. (2012)*
通过重组ERp57蛋白的功能实验，本文发现ERp57在血小板活化中调节氧化还原敏感蛋白的活性，影响血栓形成，为心血管疾病治疗提供了新靶点。
4. **"ERp57 modulates STAT3 signaling in cancer cells by regulating reactive oxygen species"**
*Khanal, P., et al. (2015)*
该研究利用重组ERp57蛋白和基因沉默技术，证明ERp57通过调控ROS水平影响STAT3信号通路，促进癌细胞存活，为肿瘤治疗中ERp57的靶向策略提供依据。
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以上文献涵盖ERp57重组蛋白在结构、免疫调控、细胞信号传导及疾病机制中的研究应用。如需具体文章链接或补充，可进一步提供检索关键词。
ERp57. also known as PDIA3 or GRP58. is a multifunctional protein belonging to the protein disulfide isomerase (PDI) family. Primarily localized in the endoplasmic reticulum (ER), it plays a critical role in protein quality control by catalyzing disulfide bond formation, rearrangement, and isomerization during nascent protein folding. ERp57 interacts with lectin chaperones calnexin and calreticulin, forming a transient complex to assist glycoproteins in achieving proper tertiary structures. Beyond its classical ER functions, ERp57 exhibits diverse subcellular localization, including the cell surface, cytoplasm, and nucleus, implicating it in non-canonical roles such as modulating cell adhesion, signal transduction, and transcriptional regulation.
This 58-kDa protein contains two thioredoxin-like domains (a and a') with CGHC active sites for redox activity, flanked by non-catalytic domains (b and b') involved in substrate recognition. Its redox activity is calcium-dependent, linking it to cellular calcium homeostasis. ERp57 has gained significant attention in disease contexts. It is overexpressed in various cancers, correlating with tumor progression, metastasis, and chemoresistance. In neurodegenerative diseases like Alzheimer's, ERp57 interacts with amyloid precursor protein, influencing pathological aggregation. Additionally, it participates in autoimmune disorders through its association with MHC class I molecules during antigen presentation.
Recombinant ERp57 proteins, typically produced in E. coli or mammalian expression systems, serve as essential tools for studying these mechanisms. They enable in vitro analysis of substrate interactions, enzymatic kinetics, and structural characterization. Recent studies also explore recombinant ERp57's therapeutic potential, including its role in modulating immunogenic cell death in cancer therapy. However, its pleiotropic functions and complex regulation continue to pose challenges in delineating precise molecular pathways, driving ongoing research to unravel its context-dependent roles in health and disease.
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