Analytical Data
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Gene name
DUS4L
- Application
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Alternative Names
DUS4LtRNA-dihydrouridine(20a/20b) synthase [NAD(P)+]-like; EC 1.3.1.-; pp35; tRNA-dihydrouridine synthase 4-like
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O95620
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Expression Region
1-317aa
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AA Sequence
MKSDCMQTTICQERKKDPIEMFHSGQLVKVCAPMVRYSKLAFRTLVRKYSCDLCYTPMIVAADFVKSIKARDSEFTTNQGDCPLIVQFAANDARLLSDAARIVCPYANGIDINCGCPQRWAMAEGYGACLINKPELVQDMVKQVRNQVETPGFSVSIKIRIHDDLKRTVDLCQKAEATGVSWITVHGRTAEERHQPVHYDSIKIIKENMSIPVIANGDIRSLKEAENVWRITGTDGVMVARGLLANPAMFAGYEETPLKCIWDWVDIALELGTPYMCFHQHLMYMMEKITSRQEKRVFNALSSTSAIIDYLTDHYGI
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Molecular Weight
62.2 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
The DUS4L protein, a member of the dus (dihydrouridine synthase) family, is integral in the post-transcriptional modification of tRNA, specifically in the isomerization of uridine to dihydrouridine. This modification is crucial for the proper functioning of tRNA, as it influences the stability, folding, and interactions of the tRNA molecules, ultimately impacting protein synthesis. Research into DUS4L has gained importance due to its potential implications in various biological processes and diseases. Studies have shown that modifications in tRNA, mediated by proteins like DUS4L, can play a role in cancer development, response to stress, and modulation of gene expression. Additionally, the understanding of DUS4L’s structure and function could reveal insights into the general mechanisms of tRNA modification and its evolutionary significance across different organisms. Given the increasing interest in tRNA biology and its connection to human health, investigations into DUS4L are essential for unlocking new therapeutic avenues and enhancing our comprehension of translational regulation in cellular systems.
