| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EPPK1 |
| Uniprot No | P58107 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-225aa |
| 氨基酸序列 | MSGHTLPPLPVPGTNSTEQASVPRAMAATLGAGTPPRPQARSIAGVYVEASGQAQSVYAAMEQGLLPAGLGQALLEAQAATGGLVDLARGQLLPVSKALQQGLVGLELKEKLLAAERATTGYPDPYGGEKLALFQAIGKEVVDRALGQSWLEVQLATGGLVDPAQGVLVAPEPACHQGLLDRETWHKLSELEPGTGDLRFLNPNTLERLTYHQLLERCVRAPGSG |
| 预测分子量 | 27.5 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EPPK1重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**: "Recombinant expression and functional characterization of Epiplakin1 (EPPK1) in keratinocyte cytoskeleton organization"
**作者**: Zhang Y, Wang L, et al.
**摘要**: 该研究报道了通过大肠杆菌系统成功表达并纯化重组人源EPPK1蛋白，并验证其与角蛋白网络的相互作用。实验表明，重组EPPK1在体外能够增强角蛋白丝的交联，提示其在维持表皮细胞机械稳定性中的作用，为研究皮肤相关疾病提供了工具。
2. **文献名称**: "EPPK1 as a novel regulator of cancer cell motility: Insights from recombinant protein-based assays"
**作者**: Lee S, Kim JH, et al.
**摘要**: 作者利用哺乳动物表达系统制备了带His标签的重组EPPK1蛋白，发现其通过调控细胞骨架动态促进乳腺癌细胞迁移。研究还通过免疫共沉淀揭示了EPPK1与肌动蛋白结合蛋白的相互作用机制。
3. **文献名称**: "Structural analysis of Epiplakin1 using recombinant protein expressed in insect cells"
**作者**: Gupta R, et al.
**摘要**: 本研究采用杆状病毒-昆虫细胞系统表达全长EPPK1重组蛋白，通过冷冻电镜解析其多结构域构象。结果表明，EPPK1的柔性结构域可能介导其在不同细胞应激条件下的差异性功能，为开发靶向EPPK1的分子探针奠定基础。
(注：以上文献为示例性内容，实际引用时需根据真实发表的论文调整信息。)
EPPK1 (Epiplakin 1) is a cytoskeletal linker protein belonging to the plakin family, primarily expressed in epithelial tissues, particularly the skin. It plays a critical role in maintaining epidermal integrity by interacting with intermediate filaments like keratins, stabilizing cell architecture during mechanical stress. Unlike other plakin proteins, EPPK1 lacks a rod domain and contains multiple plakin repeat domains, enabling flexible binding to diverse cytoskeletal components. Its unique modular structure allows dynamic involvement in cell adhesion, wound healing, and stress response.
Recombinant EPPK1 protein is engineered using expression systems (e.g., bacterial, mammalian) to produce purified, functional forms for research. Studies focus on its role in epithelial diseases, including skin blistering disorders, cancer progression, and inflammatory conditions. EPPK1’s interaction with keratin networks is implicated in modulating epithelial-mesenchymal transition (EMT), influencing tumor metastasis. Recombinant variants enable mechanistic studies through in vitro binding assays, structural analysis, and cellular localization experiments.
Recent research highlights EPPK1’s potential as a biomarker or therapeutic target. Its dysregulation correlates with poor prognosis in cancers like hepatocellular carcinoma. However, functional redundancy with other plakins and tissue-specific expression patterns complicate its pathophysiological characterization. Recombinant EPPK1 tools are essential for resolving these ambiguities, offering insights into epithelial resilience mechanisms and guiding therapeutic strategies for epithelial-derived diseases. Ongoing studies aim to map its interactome and validate its regulatory roles in stress adaptation.
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