Cat: IPD-X40570

Recombinant Human LSM10 Protein ,His & SUMO

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Analytical Data

  • Gene name

    LSM10

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    LSM10U7 snRNA-associated Sm-like protein LSm10

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- His-SUMO

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q969L4

  • Expression Region

    1-123aa

  • Molecular Weight

    30.1 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

The LSM10 protein is a crucial component of the spliceosomal machinery in eukaryotic cells, playing a significant role in RNA processing, specifically in the regulation of pre-mRNA splicing and RNA decay. Research into LSM10 emerged from the need to understand the complex mechanisms underpinning gene expression regulation, as improper spliceosome function can lead to various diseases, including cancer. LSM10 is part of the LSM gene family, which is characterized by its involvement in the assembly and stabilization of RNA-protein complexes that contribute to post-transcriptional modifications of RNA molecules. Its potential interactions with various RNA species, including small nucleolar RNAs (snoRNAs) and small nuclear RNAs (snRNAs), underscore its importance in the maintenance of cellular RNA integrity and function. Additionally, studies have suggested that LSM10 may have a role in stress responses and the regulation of cellular senescence, further enhancing its relevance in cellular physiology and pathology. Consequently, research on LSM10 has implications for understanding the molecular underpinnings of RNA metabolism in health and disease, making it an important target for therapeutic interventions aimed at correcting splicing defects or modulating RNA pathways. As such, ongoing investigations are focused on elucidating the structural dynamics, interacting partners, and functional roles of LSM10, paving the way for potential advancements in RNA-based therapeutic strategies.

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