Analytical Data
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Gene name
RARS2
- Application
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Alternative Names
RARSL; DALRD2; ArgRS; Arginyl-tRNA Synthetase-Like; Arginine tRNA Ligase 2,Mitochondrial; Arginyl-tRNA synthetase
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Species
Rat
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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
F7FFR1
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Expression Region
Val313~Cys578
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Molecular Weight
34kDa
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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
RARS2 (Arginyl-tRNA Synthetase 2) is a crucial enzyme in the mitochondrial protein synthesis pathway, responsible for the charging of tRNA molecules with the amino acid arginine. Mutations in the RARS2 gene have been linked to a spectrum of mitochondrial disorders, including neurodegenerative diseases and myopathies, highlighting its significance in maintaining mitochondrial function and cellular health. Research has identified RARS2 as a vital component in the unfolded protein response, which is essential for mitigating mitochondrial stress and maintaining proteostasis. Furthermore, abnormal levels of RARS2 have been observed in various cancers, suggesting its potential role in tumorigenesis and metabolic regulation. The reconstitution of RARS2 proteins has become a focal point for understanding mitochondrial disease mechanisms, exploring therapeutic avenues, and developing novel diagnostic tools. As researchers investigate the structural and functional characteristics of RARS2, they aim to elucidate its interactions with other mitochondrial and cytoplasmic components, as well as assess how different mutations impact its activity. This line of inquiry not only aids in comprehending the molecular underpinnings of associated diseases but also opens pathways for innovative therapeutic strategies targeting mitochondrial dysfunction. Overall, the study of RARS2 recombinant proteins exemplifies the intricate relationship between mitochondrial biology and human health, underscoring the importance of continued research in this area to enhance our understanding of mitochondrial diseases.
