Cat: IPD-X38971

Recombinant Mouse MRPL2 Protein,His

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Analytical Data

  • Gene name

    MRPL2

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    MRP-L2; MRP-L14; RPML14; CGI-22; L2mt

  • Species

    Mouse

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9D773

  • Expression Region

    Gln34~Asn306

  • Molecular Weight

    36kDa

  • 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

MRPL2 (Mitochondrial Ribosomal Protein L2) is an essential component of the mitochondrial ribosome, which plays a crucial role in the synthesis of mitochondrial proteins that are vital for cellular respiration and energy production. Understanding MRPL2's function has gained significance due to its involvement in various biological processes and potential implications in diseases, including neurodegenerative disorders and cancer. Research has shown that alterations in mitochondrial protein synthesis can lead to inefficient energy production and contribute to the pathogenesis of these conditions. Additionally, MRPL2 is implicated in the regulation of mitochondrial dynamics, biogenesis, and apoptosis. The study of MRPL2 recombinant protein is important for elucidating its structure-function relationship and its interactions with other mitochondrial components. This knowledge can pave the way for developing therapeutic targets aimed at mitigating mitochondrial dysfunction. Recombinant MRPL2 can be used in biochemical assays, aiding in the understanding of its role in mitochondrial protein synthesis and providing insights into its potential as a biomarker or therapeutic target in diseases associated with mitochondrial dysfunction. The ongoing research on MRPL2 not only contributes to fundamental biological knowledge but also holds promise for translational applications in improving the management of mitochondrial diseases and enhancing the understanding of mitochondrial contributions to overall cell health.

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