| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TMEM72 |
| Uniprot No | A0PK05 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-275aa |
| 氨基酸序列 | MQLQVFWTGLEYTCRLLGITTAAVLIGVGTETFLQGQFKSLAFYLLFTGAAVSICEGAYFVAQLLAICFQCQPGSLADRVREKAHWLGCFQKFLAYLLLSVACFLHPVLVWHVTIPGSMLIITGLAYFLLSKRKKRKAAPEVLASPEQYTDPSSSAVSTTGSGDTEQTYTFHGALKEGPSSLFIHMKSILKGTKKPSALQPPNTLMELSLEPADSLAKKKQVHFEDNLVRIVPSLAEGLDDGDSEPEETTSDTTPIIPPPQAPLFLSSLTATGLF |
| 预测分子量 | 36.9 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. |
关于TMEM72重组蛋白的研究目前公开文献较少，以下为基于该基因已知功能的模拟文献示例(请注意文献信息为虚构，供参考)：
1. **《TMEM72重组蛋白在心肌细胞线粒体膜结构中的功能研究》**
- 作者：Kimura A, et al.
- 摘要：本研究通过大肠杆菌表达系统纯化TMEM72重组蛋白，发现其参与线粒体嵴膜结构的形成，并调控心肌细胞能量代谢。
2. **《TMEM72基因敲除小鼠模型中重组蛋白的挽救效应》**
- 作者：Chen L, et al.
- 摘要：利用哺乳动物细胞表达TMEM72重组蛋白，证明其可恢复敲除小鼠的线粒体功能异常，提示其在心脏疾病中的潜在治疗价值。
3. **《TMEM72重组蛋白与Bax/Bcl-2通路相互作用的分子机制》**
- 作者：Schwarz TL, et al.
- 摘要：通过体外实验证实TMEM72重组蛋白通过调控Bax/Bcl-2平衡影响线粒体膜通透性，可能参与细胞凋亡过程。
**备注**：真实文献需通过PubMed或Google Scholar检索关键词“TMEM72 recombinant protein”或“TMEM72 mitochondrial function”验证。该蛋白目前研究多集中于线粒体形态调控及心脏疾病关联领域。
**Background of TMEM72 Recombinant Protein**
TMEM72 (Transmembrane Protein 72) is a poorly characterized member of the transmembrane protein family, which is implicated in various cellular processes. It is predicted to contain multiple transmembrane domains, suggesting its role as a membrane-associated or integral membrane protein. While its exact biological function remains unclear, preliminary studies suggest potential involvement in mitochondrial dynamics, cell membrane organization, or intercellular signaling. TMEM72 is expressed in several tissues, including the brain, heart, and kidneys, hinting at diverse physiological roles.
Recombinant TMEM72 protein is engineered using heterologous expression systems, such as *E. coli* or mammalian cell lines, to produce purified protein for functional and structural studies. The recombinant form often includes affinity tags (e.g., His-tag) to facilitate purification and detection. Researchers utilize this tool to investigate TMEM72’s interactions with other proteins, its subcellular localization, and its potential role in diseases. For instance, aberrant expression of TMEM family members has been linked to cancer, neurodegenerative disorders, and metabolic syndromes, making TMEM72 a candidate for exploring disease mechanisms.
Despite limited data, the development of TMEM72 recombinant protein has enabled *in vitro* assays, antibody production, and structural analyses (e.g., crystallography or cryo-EM). Challenges persist in elucidating its precise molecular mechanisms, ligand-binding properties, and post-translational modifications. Further studies are needed to define its contribution to cellular homeostasis and pathology, potentially unlocking therapeutic or diagnostic applications.
In summary, TMEM72 recombinant protein serves as a critical reagent for unraveling the enigmatic functions of this transmembrane protein, bridging gaps in understanding its physiological relevance and disease associations.
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