Analytical Data
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基因名
TRMT112
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简介
TRMT112 protein activates various methyltransferases for rRNA, tRNA, and protein modifications. It cooperates with BUD23 to methylate guanine N(7) of 18S rRNA. TRMT112 Protein, Human (His-SUMO) is the recombinant human-derived TRMT112 protein, expressed by E. coli , with N-His, N-SUMO labeled tag.
- Application
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别名
TRMT112; AD-001; HSPC152; HSPC170; Multifunctional methyltransferase subunit TRM112-like protein; tRNA methyltransferase 112 homolog
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种属
Human
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表达系统
E. coli
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标签
N-His;N-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9UI30-1
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表达区间
M1-S125
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蛋白长度
Full Length of Isoform-1
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分子量
32 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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保存条件 & 期限
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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运输条件
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
TRMT112 is a highly conserved protein that plays a crucial role in the post-transcriptional modification of tRNA by its involvement in the methylation of adenosine residues at position 37, a process essential for the stability and function of tRNA molecules. Disruptions in this modification can lead to various cellular dysfunctions and are associated with a range of diseases, including cancer and genetic disorders. Research on TRMT112 has gained traction due to its importance in cellular metabolism and gene expression regulation. Recent studies have highlighted TRMT112’s interaction with other methyltransferases, suggesting a complex network of regulatory mechanisms in tRNA biology. Furthermore, researchers are exploring the potential of TRMT112 as a therapeutic target, given its significant role in maintaining tRNA integrity and its implication in disease pathways. Understanding TRMT112’s structure, function, and interaction with other cellular components is therefore essential for elucidating its involvement in translational control and the broader implications for cellular health and disease. This ongoing research aims to provide insights that could lead to novel therapeutic strategies for conditions linked to tRNA dysregulation, showcasing the importance of TRMT112 in both fundamental biology and clinical applications.
