Analytical Data
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Gene name
DARS
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简介
DARS Protein, a central player, catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP, maintaining cellular energy homeostasis. It also exhibits nucleoside diphosphate kinase activity, producing various nucleoside triphosphates. At a low rate, DARS participates in thiamine triphosphate synthesis from thiamine diphosphate and ADP, showcasing its multifaceted role in nucleotide metabolism. DARS Protein, Human (His) is the recombinant human-derived DARS protein, expressed by E. coli , with N-His labeled tag.
- Application
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Alternative Names
Aspartate--tRNA ligase, cytoplasmic; AspRS; DARS1; PIG40
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Species
Human
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Source
E. coli
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Tag
N-His
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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
M1-P501
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Protein Length
Full Length
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Molecular Weight
47 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 (aspartyl-tRNA synthetase) is a crucial enzyme that catalyzes the attachment of aspartate to its corresponding tRNA, playing a vital role in protein synthesis and cellular function. Research on DARS has gained momentum due to its involvement in various cellular processes and diseases. Dysregulation of DARS has been linked to specific genetic disorders and neurodegenerative diseases, making it a target for therapeutic intervention. Moreover, DARS exhibits unique structural and functional properties that differentiate it from other tRNA synthetases, which has piqued the interest of researchers in understanding its mechanism and evolutionary significance. Studies have shown that DARS is not only involved in aminoacylation but may also participate in additional cellular functions, including regulatory roles in mitochondrial processes. Understanding the structure-function relationship of DARS through techniques such as X-ray crystallography and molecular dynamics simulations can provide insights into its specificity and potential implications in health and disease. Consequently, the investigation of DARS not only enhances fundamental biological knowledge but also opens avenues for developing novel therapeutic strategies targeting its dysfunction. This multifaceted interest underscores the importance of DARS in both basic and applied research contexts, reinforcing its status as a significant protein in molecular biology.
