Cat: IPD-X33625

Recombinant Human HARS/HisRS Protein,His

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Analytical Data

  • Gene name

    HARS/HisRS

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    HRS; Jo1; HisRS; Histidine tRNA Ligase 1,Cytoplasmic; Autoantigen Jo-1

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P12081

  • Expression Region

    Met1~Gln294

  • 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

HARS (Histidyl-tRNA Synthetase) and HisRS (Histidyl-tRNA Synthetase) are crucial enzymes in the process of protein synthesis, specifically in the accurate charging of histidine onto its corresponding tRNA molecule. The proper functioning of these enzymes is vital for maintaining the fidelity of translation, and any malfunction can lead to a range of diseases, including neurodegeneration and various forms of cancer. Research into HARS/HisRS has gained momentum due to their dual roles in both protein synthesis and signaling pathways that regulate cellular responses to stress. These enzymes are also implicated in various cellular processes, such as apoptosis and immune response, linking their function to broader biological contexts. The study of HARS/HisRS has not only advanced our understanding of tRNA synthetases but also opened potential therapeutic avenues, as targeting these proteins may provide novel strategies for treating diseases associated with their dysfunction. Understanding the structure-function relationships of HARS/HisRS at a molecular level can pave the way for drug discovery and the development of targeted therapies that can modulate their activity, thereby influencing protein translation dynamics in pathological states. Overall, the research on HARS/HisRS is pivotal in elucidating the complexities of cellular machinery and its implications for health and disease.

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