Analytical Data
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Gene name
TRMT112
- Application
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Alternative Names
TRMT112；Multifunctional methyltransferase subunit TRM112-like Protein
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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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AA Sequence
MKLLTHNLLSSHVRGVGSRGFPLRLQATEVRICPVEFNPNFVARMIPKVEWSAFLEAADNLRLIQVPKGPVEGYEENEEFLRTMHHLLLEVEVIEGTLQCPESGRMFPISRGIPNMLLSEEETES
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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 newly identified protein that has garnered significant attention in the field of molecular biology and biochemistry due to its role in the biogenesis of ribosomes and its potential implications in cancer research. It is known to be involved in the methylation processes of tRNA and ribosomal RNA, which are critical for proper protein synthesis and cellular function. Dysregulation of these processes can lead to various diseases, including cancer, making TRMT112 a potential target for therapeutic intervention. Furthermore, studies have demonstrated that TRMT112 interacts with other key proteins in the methylation pathway, underscoring its importance in RNA modification and cell growth regulation. The characterization of TRMT112 and its functional mechanisms could not only enhance our understanding of ribosomal assembly and function but may also pave the way for novel cancer treatment strategies that target the underlying molecular pathways affected by this protein. As research progresses, TRMT112 is positioned as a promising candidate for further investigation, particularly in the context of its role in cellular stress responses and the maintenance of genomic integrity.
