Cat: IPD-X39138

Recombinant Mouse LARS2 Protein,His

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Analytical Data

  • Gene name

    LARS2

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    LEURS; Leucine tRNA Ligase 2,Mitocondrial; Leucyl-tRNA synthetase

  • Species

    Mouse

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q8VDC0

  • Expression Region

    Gln609~Glu902

  • Molecular Weight

    37kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • 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.

  • 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.

  • 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.

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Protein Description

LARS2 (Leucyl-tRNA synthetase 2) is a mitochondrial enzyme that plays a critical role in the protein synthesis machinery of mitochondria by charging tRNA with the amino acid leucine. Its importance extends beyond basic translation processes, as mutations in the LARS2 gene have been implicated in various mitochondrial disorders, contributing to a complex clinical picture that includes neurological deficits, myopathy, and multi-organ dysfunction. Research on LARS2 has gained momentum due to the enzyme's essential contributions to mitochondrial function and its involvement in cellular energy metabolism. Scientists are increasingly focused on understanding the structure-function relationship of LARS2, characterizing its enzymatic activity, and elucidating the impact of mutations at both molecular and systemic levels. Additionally, the study of LARS2 is crucial for developing potential therapeutic strategies, including gene therapy and mitochondrial targeted interventions, to ameliorate the effects of LARS2-related diseases. As mitochondrial dysfunction is a central feature of numerous age-related and degenerative diseases, understanding the role of LARS2 in mitochondrial health could open new avenues for research and treatment. Overall, the exploration of LARS2 and its recombinant protein form is pivotal for gaining insights into mitochondrial biology and developing innovative strategies to combat mitochondrial disorders.

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