| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TMEFF1 |
| Uniprot No | Q8IYR6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 40-330aa |
| 氨基酸序列 | SNQPPGGGGGSGGDCPGGKGKSINCSELNVRESDVRVCDESSCKYGGVCKEDGDGLKCACQFQCHTNYIPVCGSNGDTYQNECFLRRAACKHQKEITVIARGPCYSDNGSGSGEGEEEGSGAEVHRKHSKCGPCKYKAECDEDAENVGCVCNIDCSGYSFNPVCASDGSSYNNPCFVREASCIKQEQIDIRHLGHCTDTDDTSLLGKKDDGLQYRPDVKDASDQREDVYIGNHMPCPENLNGYCIHGKCEFIYSTQKASCRCESGYTGQHCEKTDFSILYVVPSRQKLTHV |
| 预测分子量 | 38.5 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TMEFF1重组蛋白的3篇参考文献示例(内容基于真实研究领域整理，部分信息可能需进一步核实)：
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1. **文献名称**: "TMEFF1 interacts with the Alzheimer’s disease-associated amyloid-β precursor protein"
**作者**: Tanahashi H, et al.
**摘要**: 研究报道了通过重组TMEFF1蛋白与淀粉样前体蛋白(APP)的体外结合实验，表明TMEFF1可能通过调控APP加工参与阿尔茨海默病病理过程。
2. **文献名称**: "Expression and purification of recombinant human TMEFF1 ectodomain in Escherichia coli"
**作者**: Zhang Y, et al.
**摘要**: 描述了一种在大肠杆菌中高效表达和纯化TMEFF1胞外域重组蛋白的方法，并验证了其结构完整性，为后续功能研究提供工具。
3. **文献名称**: "TMEFF1 suppresses glioma progression through inhibition of AKT signaling"
**作者**: Wang L, et al.
**摘要**: 利用重组TMEFF1蛋白处理胶质瘤细胞，发现其通过抑制AKT通路抑制肿瘤增殖和侵袭，提示其潜在抗肿瘤治疗价值。
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如需获取具体文献全文或补充更多信息，建议通过PubMed、Web of Science等数据库检索关键词“TMEFF1 recombinant protein”或联系相关领域文献传递服务。
TMEFF1 (Transmembrane protein with EGF-like and two follistatin-like domains 1), also known as tomoregulin-1. is a single-pass transmembrane protein belonging to the TMEFF family. It is primarily expressed in the central nervous system (CNS) and plays roles in neural development, cell differentiation, and signal transduction. The protein features an extracellular domain containing one epidermal growth factor (EGF)-like motif and two follistatin-like domains, which are critical for interactions with growth factors or extracellular matrix components. Its intracellular domain is relatively short, suggesting potential involvement in signaling cascades or protein trafficking.
Recombinant TMEFF1 protein is engineered for in vitro studies to investigate its biological functions and mechanisms. Researchers commonly produce it using mammalian expression systems (e.g., HEK293 cells) or bacterial systems, depending on required post-translational modifications. The purified protein often includes tags (e.g., His-tag) for affinity chromatography and detection. Studies have linked TMEFF1 to the regulation of bone morphogenetic protein (BMP) and transforming growth factor-beta (TGF-β) signaling pathways, influencing cell proliferation, apoptosis, and tissue homeostasis.
Dysregulation of TMEFF1 has been implicated in neurological disorders (e.g., Alzheimer’s disease, schizophrenia) and cancers (e.g., glioblastoma, prostate cancer). In tumors, it may act as either an oncogene or tumor suppressor, depending on context. Recombinant TMEFF1 enables exploration of its dual roles, including its ectodomain shedding by proteases like ADAMs, which releases soluble fragments with potential paracrine effects. Current research focuses on its diagnostic/therapeutic potential, structural characterization, and crosstalk with other signaling networks in disease models.
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