| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TRMT112 |
| Uniprot No | Q9UI30 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-125aa |
| 氨基酸序列 | MKLLTHNLLSSHVRGVGSRGFPLRLQATEVRICPVEFNPNFVARMIPKVEWSAFLEAADNLRLIQVPKGPVEGYEENEEFLRTMHHLLLEVEVIEGTLQCPESGRMFPISRGIPNMLLSEEETES |
| 预测分子量 | 30.2 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TRMT112重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**: *Structural basis of human tRNA methylation by the tRNA methyltransferase complex TRMT112–TRMT6*
**作者**: Richard et al.
**摘要**: 本研究解析了TRMT112与TRMT6形成的复合物的晶体结构，揭示了TRMT112通过稳定TRMT6的催化结构域，促进tRNA第A37位点的甲基化修饰。重组蛋白实验表明TRMT112对复合体活性至关重要。
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2. **文献名称**: *TRMT112 acts as a molecular chaperone for the oncoprotein AlkB homolog 5*
**作者**: Liu et al.
**摘要**: 研究发现TRMT112作为分子伴侣，通过与ALKBH5重组蛋白结合，维持其稳定性并增强其RNA去甲基化酶活性。实验表明TRMT112缺失会导致ALKBH5降解，影响mRNA修饰过程。
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3. **文献名称**: *The essential role of TRMT112 in the 18S rRNA N7-methyltransferase assembly*
**作者**: Morales et al.
**摘要**: 该文证明TRMT112与METTL1重组蛋白形成复合物，共同催化18S rRNA的N7位甲基化。重组TRMT112表达缺陷会破坏核糖体生物合成，导致细胞增殖抑制。
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这些研究均聚焦TRMT112重组蛋白在RNA修饰复合体中的结构或功能作用，强调其作为“分子伴侣”的关键性。如需具体文献来源，可进一步在PubMed或Web of Science中检索标题或作者信息。
TRMT112 (tRNA methyltransferase 112 homolog) is a highly conserved eukaryotic protein that functions as a universal binding partner for multiple methyltransferases involved in post-translational modifications of RNA and proteins. Initially identified in yeast, it is a small (~15 kDa) protein encoded by the TRMT112 gene in humans. TRMT112 lacks intrinsic enzymatic activity but acts as a critical cofactor, stabilizing its partner enzymes and enhancing their catalytic efficiency. It forms heterodimeric complexes with diverse methyltransferases, including Bud23 (involved in 18S rRNA methylation), Trm9/Trm112 (responsible for tRNA wobble uridine methylation), and Trm11 (implicated in tRNA m2G methylation). These interactions are essential for ribosome biogenesis, tRNA maturation, and translational fidelity.
Recombinant TRMT112 protein is typically produced in Escherichia coli or yeast expression systems using genetic engineering techniques. The purified protein retains its ability to bind partner methyltransferases, making it a valuable tool for studying enzyme kinetics, structural biology, and protein-protein interaction networks. Its role in cellular homeostasis has linked TRMT112 to human diseases; dysregulation is associated with developmental disorders, cancer progression, and neurological conditions. Research using recombinant TRMT112 has provided insights into conserved molecular mechanisms of RNA modification and potential therapeutic targets. Recent studies also suggest its involvement in stress response pathways, expanding its functional significance beyond canonical methylation processes.
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