Analytical Data
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Gene name
TRMT112
- Application
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Alternative Names
tRNA methyltransferase 112 homolog
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UI30
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Expression Region
1-125aa
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Molecular Weight
30.2 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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.
