| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TMED6 |
| Uniprot No | Q8WW62 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-240 aa |
| 活性数据 | MSPLLFGAGLVVLNLVTSARSQKTEPLSGSGDQPLFRGADRYDFAIMIPPGGTECFWQFAHQTGYFYFSCEVQRTVGMSHDRHVAATAHNPQGFLIDTSQGVRGQINFSTQETGFYQLCLSNQHNHFGSVQVYLNFGVFYEGPETDHKQKERKQLNDTLDAIEDGTQKVQNNIFHMWRYYNFARMRKMADFFLIQSNYNYVNWWSTAQSLVIILSGILQLYFLKRLFNVPTTTDTKKPRC |
| 分子量 | 54 kDa |
| 蛋白标签 | 0 |
| 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. |
以下是关于重组人TMED6蛋白的3篇代表性参考文献(注意：部分文献为示例性描述，实际引用请以具体论文信息为准)：
1. **文献名称**：TMED6 regulates liver cancer progression via Wnt/β-catenin signaling
**作者**：Li X. et al.
**摘要**：研究利用重组人TMED6蛋白过表达模型，揭示其在肝癌细胞中通过激活Wnt/β-catenin通路促进肿瘤迁移和侵袭的机制，为靶向治疗提供新靶点。
2. **文献名称**：Structural insights into TMED6-mediated cargo transport in the early secretory pathway
**作者**：Zhang Y. et al.
**摘要**：通过重组表达和冷冻电镜技术解析了人源TMED6蛋白的三维结构，阐明其作为COPII囊泡组分在内质网-高尔基体转运中的分子机制。
3. **文献名称**：TMED6 modulates Aβ production through interaction with γ-secretase complex
**作者**：Chen H. et al.
**摘要**：研究利用重组TMED6蛋白的体外互作实验，证明其与γ-分泌酶复合物结合并调控β-淀粉样蛋白生成，提示其在阿尔茨海默病中的潜在作用。
**提示**：以上文献信息为模拟示例，实际研究需通过PubMed(https://pubmed.ncbi.nlm.nih.gov)或Web of Science等数据库检索真实文献。近期研究多聚焦于TMED6在内质网蛋白分选、癌症及神经退行性疾病中的功能。
Transmembrane emp24 domain-containing protein 6 (TMED6) is a member of the TMED family, which comprises conserved transmembrane proteins involved in vesicular trafficking and cargo sorting. As a component of the endoplasmic reticulum (ER)-Golgi intermediate compartment, human TMED6 functions as a cargo receptor, facilitating selective transport of secreted proteins via COPII-coated vesicles. It contains a characteristic N-terminal signal peptide, a coiled-coil domain for oligomerization, and a C-terminal cargo-binding domain.
TMED6 plays critical roles in protein quality control by mediating the export of properly folded glycoproteins. Studies suggest its interaction with specific glycosylated clients, including components of the complement system and TGF-β family members. Dysregulation of TMED6 has been associated with inflammatory diseases and cancer progression, potentially linked to its role in modulating secretory pathways. Recombinant human TMED6 protein, typically produced in mammalian expression systems with appropriate post-translational modifications, serves as an essential tool for studying ER-Golgi trafficking mechanisms, host-pathogen interactions (e.g., coronaviruses exploiting vesicular transport), and therapeutic target validation. Its conserved structure across vertebrates underscores fundamental biological significance in cellular secretion processes.
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