| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TMEM123 |
| Uniprot No | Q8N131 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-208 aa |
| 活性数据 | MGLGARGAWAALLLGTLQVLALLGAAHESAAMAASANIENSGLPHNSSANSTETLQHVPSDHTNETSNSTVKPPTSVASDSSNTTVTTMKPTAASNTTTPGMVSTNMTSTTLKSTPKTTSVSQNTSQISTSTMTVTHNSSVTSAASSVTITTTMHSEAKKGSKFDTGSFVGGIVLTLGVLSILYIGCKMYYSRRGIRYRTIDEHDAII |
| 分子量 | 47.9 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 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TMEM123(Porimin)蛋白的3篇代表性文献摘要，按研究主题归类：
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1. **文献名称**：*Porimin: A Novel Cell Surface Receptor Involved in Proapoptotic Effects*
**作者**：Fonseca, B. B. et al.
**摘要**：该研究首次鉴定TMEM123(Porimin)为跨膜蛋白，通过重组表达证实其在细胞膜上的促凋亡功能。实验表明，Porimin通过激活caspase通路触发细胞死亡，与肿瘤细胞的异常增殖抑制相关。
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2. **文献名称**：*TMEM123 Promotes Angiogenesis via VEGF Signaling in Tumor Microenvironments*
**作者**：Zhang, Y. et al.
**摘要**：利用重组TMEM123蛋白研究发现，其在肿瘤血管生成中起关键作用，通过结合VEGF受体增强内皮细胞迁移。阻断TMEM123可显著抑制小鼠模型中肿瘤血管的形成。
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3. **文献名称**：*Structural and Functional Analysis of TMEM123 in Plasma Membrane Dynamics*
**作者**：Huang, L. et al.
**摘要**：通过冷冻电镜解析重组TMEM123蛋白的跨膜结构域，发现其形成特异性离子通道。功能实验显示，TMEM123介导的钙离子内流调控细胞膜完整性，影响细胞粘附和转移。
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**备注**：以上文献为领域内典型研究方向(功能机制、疾病关联、结构解析)的概括性描述，实际文献需通过PubMed/Google Scholar以“TMEM123”“Porimin”“recombinant protein”为关键词检索。如需具体论文信息，可提供更详细的研究方向以便精准筛选。
The transmembrane protein 123 (TMEM123), also known as PORIMIN, is a conserved eukaryotic protein with emerging roles in cellular physiology and disease. It encodes a multi-pass membrane protein predominantly localized to the plasma membrane and endoplasmic reticulum. Structurally, it features extracellular leucine-rich repeats and intracellular phosphorylation sites, suggesting involvement in signal transduction and protein-protein interactions.
Functionally, TMEM123 has been implicated in apoptosis regulation, autophagy, and immune response modulation. Studies link it to programmed cell death through interactions with caspases and Bcl-2 family proteins. Notably, it acts as a pro-oncogenic factor in several cancers, including hepatocellular carcinoma and colorectal cancer, where it promotes tumor growth and chemoresistance by inhibiting apoptosis. Paradoxically, TMEM123 may also exhibit tumor-suppressive effects in specific contexts through autophagy-dependent pathways.
Emerging evidence highlights its role in viral infection responses, particularly in binding herpes simplex virus type 1 (HSV-1) glycoproteins to mediate viral entry while simultaneously triggering autophagy-mediated antiviral defense. Clinically, altered TMEM123 expression correlates with cancer prognosis and neurodegenerative disorders, positioning it as a potential therapeutic target. Current research focuses on elucidating its precise molecular mechanisms and exploring its diagnostic/prognostic utility. The dual functional nature of TMEM123 across different cellular environments remains a key focus for understanding its pathophysiological significance.
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