Cat: PA1000-2015

Recombinant Human MRPL13 Protein,His

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Analytical Data

  • Gene name

    MRPL13

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    MRPL13;Large ribosomal subunit Protein uL13m

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9BYD1

  • Expression Region

    1-178aa

  • AA Sequence

    MGSSHHHHHH SSGLVPRGSH MGSMSSFSRA PQQWATFARI WYLLDGKMQP PGKLAAMASI RLQGLHKPVY HALSDCGDHV VIMNTRHIAF SGNKWEQKVY SSHTGYPGGF RQVTAAQLHL RDPVAIVKLA IYGMLPKNLH RRTMMERLHL FPDEYIPEDI LKNLVEELPQ PRKIPKRLDE YTQEEIDAFP RLWTPPEDYR L

  • Molecular Weight

    23 kDa

  • 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

MRPL13, a critical mitochondrial ribosomal protein, plays a vital role in mitochondrial protein synthesis and cellular metabolism. Recent studies have highlighted its significance in the assembly of the mitochondrial ribosome and its potential involvement in various pathophysiological conditions, including neurodegenerative diseases and cancer. As mitochondrial dysfunction has been linked to a broad spectrum of diseases, understanding the function and regulatory mechanisms of MRPL13 is essential. Research has shown that mutations or dysregulation of MRPL13 can lead to impaired mitochondrial translation, influencing overall cellular energy production and contributing to disease progression. Furthermore, MRPL13 is implicated in the response to cellular stress, making it a potential biomarker for mitochondrial health. The recombinant expression of MRPL13 allows for the detailed study of its structure-function relationships and interactions with other mitochondrial components. This research is crucial not only for elucidating the molecular underpinnings of mitochondrial diseases but also for exploring therapeutic strategies aimed at restoring mitochondrial function. As a result, MRPL13 has emerged as a focal point in mitochondrial biology, warranting further investigation into its multifaceted roles in health and disease.

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