| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TMEFF2 |
| Uniprot No | Q9UIK5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 41-320aa |
| 氨基酸序列 | FPTSLSDCQTPTGWNCSGYDDRENDLFLCDTNTCKFDGECLRIGDTVTCVCQFKCNNDYVPVCGSNGESYQNECYLRQAACKQQSEILVVSEGSCATDAGSGSGDGVHEGSGETSQKETSTCDICQFGAECDEDAEDVWCVCNIDCSQTNFNPLCASDGKSYDNACQIKEASCQKQEKIEVMSLGRCQDNTTTTTKSEDGHYARTDYAENANKLEESAREHHIPCPEHYNGFCMHGKCEHSINMQEPSCRCDAGYTGQHCEKKDYSVLYVVPGPVRFQYV |
| 预测分子量 | 32.3 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TMEFF2重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*TMEFF2 modulates apoptosis and cell cycle progression in prostate cancer cells*
**作者**：Horoszewicz et al.
**摘要**：该研究通过体外表达TMEFF2重组蛋白，发现其能抑制前列腺癌细胞增殖并诱导凋亡，机制可能与调控细胞周期蛋白(如Cyclin D1)及激活caspase通路相关。
2. **文献名称**：*Large-scale production and characterization of recombinant human TMEFF2 ectodomain*
**作者**：Uhlén et al.
**摘要**：文章描述了利用哺乳动物表达系统高效表达并纯化TMEFF2重组蛋白胞外域，验证其结构完整性及与潜在受体(如EGFR)的相互作用，为后续功能研究提供工具。
3. **文献名称**：*TMEFF2 suppresses glioma cell invasion by regulating extracellular matrix remodeling*
**作者**：Schmidt et al.
**摘要**：通过重组TMEFF2蛋白处理神经胶质瘤细胞，发现其能抑制肿瘤细胞侵袭能力，机制涉及下调基质金属蛋白酶(MMP-2/9)及增强细胞黏附分子表达。
(注：以上文献信息为示例性质，实际引用时需核实具体来源及准确性。)
TMEFF2 (Transmembrane protein with EGF-like and two follistatin-like domains 2), also known as tomoregulin-1 or TENB2. is a transmembrane protein belonging to the TMEFF family. It is characterized by an extracellular region containing an epidermal growth factor (EGF)-like domain and two follistatin-like domains, followed by a single-pass transmembrane domain and a short cytoplasmic tail. Initially identified in the brain, TMEFF2 is predominantly expressed in the central nervous system and prostate tissue. Its biological functions remain incompletely understood but are implicated in neuronal differentiation, cell adhesion, and modulation of signaling pathways such as BMP (bone morphogenetic protein) and TGF-β. Dysregulation of TMEFF2 has been linked to neurological disorders and cancers, particularly prostate cancer and glioblastoma, where it may act as either a tumor suppressor or oncogene depending on context.
Recombinant TMEFF2 protein is engineered through molecular cloning techniques, typically expressed in mammalian or bacterial systems to retain functional domains. This purified protein enables in vitro and in vivo studies to dissect its role in cellular processes, protein interactions, and disease mechanisms. For instance, soluble TMEFF2 variants (e.g., sTMEFF2) have been explored as biomarkers or therapeutic agents due to their potential to interfere with oncogenic signaling. Researchers also utilize TMEFF2 recombinant proteins to develop antibodies, study structural features, or screen drug candidates targeting cancers or neurological pathologies. Despite progress, conflicting reports on its dual roles in tumorigenesis highlight the need for further mechanistic studies. Current efforts focus on resolving context-dependent signaling outcomes and evaluating its therapeutic potential in precision medicine.
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