| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TRIM72 |
| Uniprot No | Q6ZMU5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-269aa |
| 氨基酸序列 | MSAAPGLLHQELSCPLCLQLFDAPVTAECGHSFCRACLGRVAGEPAADGTVLCPCCQAPTRPQALSTNLQLARLVEGLAQVPQGHCEEHLDPLSIYCEQDRALVCGVCASLGSHRGHRLLPAAEAHARLKTQLPQQKLQLQEACMRKEKSVAVLEHQLVEVEETVRQFRGAVGEQLGKMRVFLAALEGSLDREAERVRGEAGVALRRELGSLNSYLEQLRQMEKVLEEVADKPQTEFLMKYCLVTSRLQKILAESPPPARLDIQLPIIS |
| 预测分子量 | 34.5 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TRIM72(MG53)重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*MG53 participates in the membrane repair of skeletal muscle cells through interaction with phosphatidylserine*
**作者**：Jia Y, et al.
**摘要**：该研究揭示了TRIM72(MG53)在骨骼肌细胞膜修复中的关键作用，通过重组蛋白实验证明其与磷脂酰丝氨酸的相互作用介导了细胞膜损伤后的修复机制。
2. **文献名称**：*Recombinant MG53 protein modulates mitochondrial dynamics and protects against ischemia-reperfusion injury in heart*
**作者**：Cai C, et al.
**摘要**：通过表达纯化的重组TRIM72蛋白，研究发现其能够调节线粒体动态平衡，减轻心肌缺血再灌注损伤，为心血管疾病治疗提供了新思路。
3. **文献名称**：*Structural basis of TRIM72 self-association during muscle membrane repair*
**作者**：Zhu H, et al.
**摘要**：该研究利用重组TRIM72蛋白解析其三维结构，揭示了其在肌肉膜修复过程中自组装形成多聚体的分子机制，为靶向设计膜修复疗法奠定基础。
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上述研究均涉及重组TRIM72蛋白的功能探索或应用，涵盖膜修复、疾病治疗及结构解析等领域。如需扩展或调整方向，请随时告知!
TRIM72. also known as MG53 (Mitsugumin 53), is a member of the tripartite motif (TRIM) protein family, characterized by conserved RING, B-box, and coiled-coil domains. It plays a critical role in cell membrane repair, particularly in muscle tissues such as skeletal and cardiac muscle. Discovered in 2009. TRIM72 is secreted in response to injury or stress, where it orchestrates vesicle-mediated repair by aggregating intracellular vesicles at membrane disruption sites. This protein acts as a scaffold, facilitating the recruitment of repair machinery and lipid bilayer resealing through its interaction with phosphatidylserine and other membrane components.
Structurally, TRIM72’s RING domain confers E3 ubiquitin ligase activity, while its coiled-coil domain mediates oligomerization and membrane binding. Its unique ability to sense and respond to mechanical damage has made it a focus in studies of ischemic injury, muscular dystrophy, and cardiovascular diseases. Recombinant TRIM72 is produced using expression systems like *E. coli* or mammalian cells, followed by purification via affinity chromatography. The recombinant form retains biological activity, enabling therapeutic exploration in preclinical models. For instance, exogenous TRIM72 administration has shown promise in reducing tissue damage during ischemia-reperfusion injury and enhancing recovery in diabetic wound healing.
Research also highlights its dual role as both a repair protein and a regulator of metabolic homeostasis, influencing insulin signaling and mitochondrial function. Despite its therapeutic potential, challenges remain in optimizing delivery methods and understanding its systemic effects. TRIM72’s multifunctionality positions it as a compelling candidate for regenerative medicine and a tool for studying membrane biology.
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