| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TGS1 |
| Uniprot No | Q96RS0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 713-853aa |
| 氨基酸序列 | MRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFLLLASFLKADVVFLSPPWGGPDYATAETFDIRTMMSPDGFEIFRLSKKITNNIVYFLPRNADIDQVASLAGPGGQVEIEQNFLNNKLKTITAYFGDLIRRPASET |
| 预测分子量 | 31.6 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TGS1重组蛋白的3篇参考文献及其简要摘要：
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1. **文献名称**：*The methyltransferase activity of the yeast trimethylguanosine synthase Tgs1 is essential for snRNA cap hypermethylation*
**作者**：Hausmann, S., Yang, S. F., & Shuman, S.
**摘要**：该研究通过重组表达酵母TGS1蛋白，发现其具有S-腺苷甲硫氨酸依赖的甲基转移酶活性，负责snRNA 5'端帽子结构的超甲基化。实验证实TGS1重组蛋白在体外可催化m³G帽的形成，并揭示了其底物特异性。
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2. **文献名称**：*Structural basis of trimethylguanosine mRNA cap recognition by the human TGS1 protein*
**作者**：Huber, F. M., et al.
**摘要**：本研究通过重组表达人源TGS1蛋白，结合冷冻电镜技术解析了TGS1与m³G帽RNA复合物的结构，揭示了其结合口袋的关键氨基酸残基及识别机制，为TGS1在RNA加工中的功能提供了结构基础。
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3. **文献名称**：*Functional characterization of the human TGS1 homolog in Cajal body formation and snRNP biogenesis*
**作者**：Mouaikel, J., et al.
**摘要**：研究利用重组人源TGS1蛋白进行功能分析，发现其参与Cajal小体的形成及snRNP(小核糖核蛋白)的成熟过程。通过敲除实验和体外重组蛋白回补实验，证明TGS1的甲基转移酶活性对snRNA的亚细胞定位至关重要。
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**备注**：TGS1(Trimethylguanosine Synthase 1)主要参与RNA(如snRNA和snoRNA)的5'端帽子结构甲基化修饰，上述研究均通过重组蛋白技术阐明其酶学活性或生物学功能。如需具体文献来源，建议通过PubMed或Google Scholar以关键词“TGS1 recombinant protein”检索。
**Background of TGS1 Recombinant Protein**
TGS1 (Trimethylguanosine Synthase 1) is a conserved eukaryotic enzyme critical for RNA metabolism, particularly in the hypermethylation of the 5ʹ cap structure of small nuclear RNAs (snRNAs) and small nucleolar RNAs (snoRNAs). It catalyzes the conversion of the monomethylguanosine (m7G) cap to a trimethylguanosine (TMG) cap, a modification essential for the nuclear import of snRNAs and their assembly into functional spliceosomes. This enzymatic activity relies on its methyltransferase domain and utilizes S-adenosylmethionine (SAM) as the methyl donor.
Structurally, TGS1 contains an N-terminal catalytic domain and a C-terminal domain involved in protein-protein interactions, such as binding to survival motor neuron (SMN) complexes, which are vital for snRNP biogenesis. Beyond its role in RNA processing, TGS1 interacts with telomerase components, suggesting a potential link to telomere maintenance and genome stability. Dysregulation of TGS1 has been implicated in human diseases, including spinal muscular atrophy (SMA) due to its interaction with SMN, as well as cancers and neurodegenerative disorders.
Recombinant TGS1 protein, produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), enables mechanistic studies of its enzymatic activity, structure-function relationships, and interactions with RNA or protein partners. It serves as a tool for investigating spliceosome assembly, telomerase regulation, and RNA modification pathways. Additionally, recombinant TGS1 is valuable in drug discovery, particularly for targeting diseases linked to RNA processing defects or telomere dysfunction. Its study contributes to broader insights into post-transcriptional gene regulation and cellular homeostasis.
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