Cat: IPD-X26706

Recombinant Human U5A/SNRPA Protein,His & Myc

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Analytical Data

  • Gene name

    U5A/SNRPA

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    (U1 snRNP A)(U1-A)(U1A)

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P09012

  • Expression Region

    2-282aa

  • Molecular Weight

    38.6 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

U5A/SNRPA is a crucial protein involved in the splicing process of pre-mRNA, which is essential for gene expression regulation in eukaryotic cells. It forms part of the spliceosomal complex, interacting with small nuclear RNAs (snRNAs) and other protein components to facilitate the removal of introns from pre-mRNA. The importance of U5A/SNRPA in pre-mRNA splicing has prompted extensive research to elucidate its structural and functional properties. Mutations or dysregulation of SNRPA can lead to various diseases, including certain cancers and genetic disorders, highlighting its potential as a therapeutic target. Additionally, understanding the molecular mechanisms of U5A/SNRPA can provide insights into the broader splicing machinery and its role in maintaining cellular homeostasis. Researchers are using recombinant DNA technologies to produce U5A/SNRPA in bacterial or eukaryotic systems, enabling detailed studies of its biochemical activities, interaction networks, and potential post-translational modifications. Such investigations are critical for advancing our knowledge of RNA processing and its implications for human health.

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