| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TMEM132A |
| Uniprot No | Q24JP5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 642-742aa |
| 氨基酸序列 | QPVMGISLTLSRGTAHPGEVTATCWAQSALPAPKQEVALSLWLSFSDHTVAPAELYDRRDLGLSVSAEEPGAILPAEEQGAQLGVVVSGAGAEGLPLHVAL |
| 预测分子量 | 17.4 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. |
以下是模拟生成的关于TMEM132A重组蛋白的参考文献示例(非真实存在，仅供格式参考)：
1. **文献名称**: "TMEM132A Recombinant Protein Modulates Neuronal Apoptosis in Alzheimer's Disease Models"
**作者**: Chen L, et al. (2022)
**摘要**: 研究通过构建TMEM132A重组蛋白，发现其通过调控线粒体膜电位抑制β-淀粉样蛋白诱导的神经元凋亡，提示其在阿尔茨海默病中的潜在治疗价值。
2. **文献名称**: "Expression and Functional Characterization of TMEM132A Recombinant Protein in Colorectal Cancer Metastasis"
**作者**: Kim S, et al. (2021)
**摘要**: 利用昆虫细胞系统表达TMEM132A重组蛋白，证实其与整合素β1相互作用，促进结直肠癌细胞侵袭迁移，为癌症靶向治疗提供新靶点。
3. **文献名称**: "Structural Insights into TMEM132A Extracellular Domain via Recombinant Protein Crystallography"
**作者**: Müller F, et al. (2020)
**摘要**: 首次解析TMEM132A胞外结构域重组蛋白的晶体结构，揭示其独特的跨膜螺旋折叠模式，为设计小分子抑制剂奠定结构基础。
4. **文献名称**: "TMEM132A Recombinant Protein Activates MAPK Signaling in Pulmonary Fibroblasts"
**作者**: Gonzalez R, et al. (2019)
**摘要**: 通过纯化TMEM132A重组蛋白，证明其结合肺成纤维细胞表面受体并激活MAPK通路，参与特发性肺纤维化进程。
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**注**: 实际文献需通过PubMed/Google Scholar等平台检索确认。建议使用关键词"TMEM132A recombinant protein"+"expression/function/structure"组合筛选。
The TMEM132A (Transmembrane Protein 132A) gene encodes a poorly characterized member of the transmembrane protein family, predicted to play roles in cellular signaling or adhesion. As a recombinant protein, TMEM132A is artificially expressed in vitro using heterologous systems like mammalian cells or *E. coli* for functional studies. Structurally, it contains conserved transmembrane domains, a large extracellular region with potential glycosylation sites, and a short cytoplasmic tail, suggesting involvement in extracellular interactions or receptor-like functions.
Research on TMEM132A remains limited, but emerging evidence links it to neurological disorders and cancer. Genome-wide association studies (GWAS) implicate TMEM132A polymorphisms in panic disorder and neurodevelopmental conditions, hinting at its role in neuronal signaling or stress response pathways. In oncology, elevated TMEM132A expression correlates with tumor progression in certain cancers, possibly influencing cell migration or survival. Its overexpression has been observed in glioblastoma and breast cancer, though mechanistic insights remain unclear.
Recombinant TMEM132A protein is typically engineered with tags (e.g., His, FLAG) to facilitate purification and detection. Applications include antibody production, interaction partner screening (e.g., receptors, ligands), and functional assays to dissect its role in disease pathways. Challenges persist in characterizing its native ligands and signaling cascades due to limited structural data and conflicting reports on subcellular localization. Recent studies suggest potential crosstalk with G protein-coupled receptors (GPCRs) or integrin-mediated pathways, warranting further exploration.
Current efforts focus on resolving TMEM132A’s 3D structure and tissue-specific expression patterns. Its recombinant form serves as a critical tool to unravel its physiological and pathological contributions, bridging gaps between genetic associations and molecular mechanisms. Despite its enigmatic nature, TMEM132A represents a promising target for therapeutic intervention in neurological and oncological contexts.
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