Analytical Data
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Gene name
TRDMT1
- Application
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Alternative Names
TRDMT1；DNMT2；tRNA (cytosine(38)-C(5))-methyltransferase
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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
O14717
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Expression Region
1-391aa
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AA Sequence
MEPLRVLELY SGVGGMHHAL RESCIPAQVV AAIDVNTVAN EVYKYNFPHT QLLAKTIEGI TLEEFDRLSF DMILMSPPCQ PFTRIGRQGD MTDSRTNSFL HILDILPRLQ KLPKYILLEN VKGFEVSSTR DLLIQTIENC GFQYQEFLLS PTSLGIPNSR LRYFLIAKLQ SEPLPFQAPG QVLMEFPKIE SVHPQKYAMD VENKIQEKNV EPNISFDGSI QCSGKDAILF KLETAEEIHR KNQQDSDLSV KMLKDFLEDD TDVNQYLLPP KSLLRYALLL DIVQPTCRRS VCFTKGYGSY IEGTGSVLQT AEDVQVENIY KSLTNLSQEE QITKLLILKL RYFTPKEIAN LLGFPPEFGF PEKITVKQRY RLLGNSLNVH VVAKLIKILY E
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Molecular Weight
67 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
TRDMT1, or tRNA-dihydrouridine synthase 1, is an essential enzyme involved in the post-transcriptional modification of tRNA molecules, specifically catalyzing the formation of dihydrouridine at certain positions within tRNA. This modification plays a critical role in the structural stability and proper functioning of tRNA, influencing the accuracy of protein synthesis. Recent studies have highlighted the significance of TRDMT1 in various biological processes, including cellular stress responses and the maintenance of genomic integrity. Dysregulation of TRDMT1 has been linked to several diseases, including cancer, where altered tRNA modifications can affect the translation of oncogenes and tumor suppressors. As a result, there is growing interest in the development of TRDMT1 recombinant proteins for research and therapeutic applications. Understanding the enzymatic mechanisms and the effects of TRDMT1 on tRNA dynamics can provide valuable insights into its potential as a novel drug target. Ongoing research focuses on characterizing the structure-function relationship of TRDMT1, its interaction with various substrates, and its role in modulating cellular responses under different physiological conditions. By elucidating these aspects, scientists aim to uncover new strategies for manipulating tRNA modifications to improve disease treatment and to enhance our understanding of the fundamental processes of protein synthesis.
