| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | STOML1 |
| Uniprot No | Q9UBI4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 79-398aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSLKIVPTY ERMIVFRLGR IRTPQGPGMV LLLPFIDSFQ RVDLRTRAFN VPPCKLASKD GAVLSVGADV QFRIWDPVLS VMTVKDLNTA TRMTAQNAMT KALLKRPLRE IQMEKLKISD QLLLEINDVT RAWGLEVDRV ELAVEAVLQP PQDSPAGPNL DSTLQQLALH FLGGSMNSMA GGAPSPGPAD TVEMVSEVEP PAPQVGARSS PKQPLAEGLL TALQPFLSEA LVSQVGACYQ FNVVLPSGTQ SAYFLDLTTG RGRVGHGVPD GIPDVVVEMA EADLRALLCR ELRPLGAYMS GRLKVKGDLA MAMKLEAVLR ALK |
| 预测分子量 | 37 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STOML1重组蛋白的3篇代表性文献摘要(文献标题及内容为示例性概括，实际文献需根据具体研究补充)：
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1. **标题**：*STOML1重组蛋白促进胶质瘤细胞迁移的机制研究*
**作者**：Zhang Y, et al.
**摘要**：研究通过原核表达系统纯化STOML1重组蛋白，发现其通过激活MAPK信号通路增强胶质瘤细胞侵袭能力，提示STOML1可能作为肿瘤治疗的潜在靶点。
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2. **标题**：*STOML1在阿尔茨海默病中的表达及其重组蛋白功能分析*
**作者**：Wang L, et al.
**摘要**：利用哺乳动物细胞表达体系获得高纯度STOML1重组蛋白，实验表明其通过调控线粒体膜稳定性影响神经元凋亡，可能与神经退行性疾病病理相关。
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3. **标题**：*STOML1重组蛋白的晶体结构解析及其与脂质结合特性*
**作者**：Chen X, et al.
**摘要**：通过X射线衍射解析STOML1重组蛋白的晶体结构，揭示其N端结构域在脂质结合中的关键作用，为研究其膜定位机制提供结构基础。
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如需具体文献，建议通过PubMed或Google Scholar检索关键词“STOML1 recombinant protein”或“STOML1 expression and function”获取最新研究。
STOML1 (Stomatin-like protein 1) is a member of the stomatin protein family, which shares structural homology with the erythrocyte membrane protein stomatin. It is a highly conserved, ubiquitously expressed protein localized primarily in cellular membranes, including mitochondria and lipid rafts. STOML1 is characterized by an N-terminal prohibitin homology (PHB) domain and a C-terminal stomatin domain, which are implicated in protein-protein interactions and membrane scaffolding. Though its precise molecular mechanisms remain under investigation, STOML1 is suggested to regulate ion channel activity, membrane organization, and mitochondrial dynamics. Studies link it to mitochondrial fusion-fission processes, potentially influencing cellular energy metabolism and apoptosis.
Emerging evidence associates STOML1 with pathological conditions. Overexpression has been observed in cancers, such as hepatocellular carcinoma and glioblastoma, where it may promote tumor growth, metastasis, and chemoresistance. Conversely, reduced STOML1 levels correlate with neurodegenerative disorders like Alzheimer’s disease, possibly due to disrupted mitochondrial function. Its dual roles in health and disease highlight its therapeutic potential.
Recombinant STOML1 protein, produced via prokaryotic or eukaryotic expression systems, retains functional domains for biochemical studies. It serves as a critical tool for elucidating STOML1’s interactions with partners (e.g., ion channels, mitochondrial proteins) and validating its role in signaling pathways. Purified recombinant proteins, often tagged with His or GST for affinity chromatography, enable antibody development, structural analysis, and high-throughput drug screening. Further research on STOML1 recombinant proteins may advance diagnostics and targeted therapies for cancer and neurodegenerative diseases.
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