Analytical Data
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Gene name
DARS
- Application
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Alternative Names
DARS；DARS;Aspartate--tRNA ligase. cytoplasmic
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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
P14868
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Expression Region
1-501aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMPSASASRKSQEKPREIMDAAEDYAKERYG ISSMIQSQEKPDRVLVRVRDLTIQKADEVVWVRARVHTSRAKGKQCFLVL RQQQFNVQALVAVGDHASKQMVKFAANINKESIVDVEGVVRKVNQKIGSC TQQDVELHVQKIYVISLAEPRLPLQLDDAVRPEAEGEEEGRATVNQDTRL DNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEG GANVFTVSYFKNNAYLAQSPQLYKQMCICADFEKVFSIGPVFRAEDSNTH RHLTEFVGLDIEMAFNYHYHEVMEEIADTMVQIFKGLQERFQTEIQTVNK QFPCEPFKFLEPTLRLEYCEALAMLREAGVEMGDEDDLSTPNEKLLGHLV KEKYDTDFYILDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQ RIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLF LGLHNVRQTSMFPRDPKRLTP
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Molecular Weight
59 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
DARS, or aspartyl-tRNA synthetase, is a critical enzyme responsible for the charging of tRNA molecules with aspartic acid, an essential amino acid in protein synthesis. Research into DARS has gained significant attention due to its vital role in generating the correct translation of genetic information into proteins. Mutations and dysfunctions in DARS have been linked to a variety of genetic disorders, including certain forms of neurodegenerative diseases and developmental abnormalities. Understanding the structural and functional dynamics of DARS is crucial for unraveling its involvement in these pathologies. Moreover, investigating DARS provides insights into the broader mechanisms of aminoacyl-tRNA synthetases, which are pivotal for cellular protein synthesis and overall metabolic function. The study of DARS also holds potential therapeutic implications, as targeting this enzyme may offer new avenues for treating associated diseases. Recent advances in techniques such as X-ray crystallography and NMR spectroscopy have facilitated a deeper understanding of the DARS structure and its interaction with tRNA substrates. These insights are instrumental in deciphering how mutations affect enzyme activity and lead to disease states. Thus, ongoing research into DARS not only enhances our understanding of fundamental biochemical processes but also contributes to the development of innovative therapeutic strategies for various ailments linked to protein synthesis errors.
