Cat: IPD-X28563

Recombinant Human U2AF2 Protein,Strep & His

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Analytical Data

  • Gene name

    U2AF2

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    U2AF65

  • Species

    Human

  • Source

    E. coli

  • Tag

    Strep;His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P26368-1

  • Expression Region

    V140-A342

  • Protein Length

    Partial

  • 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

U2AF2, a member of the U2AF protein family, plays a crucial role in pre-mRNA splicing by binding to the polypyrimidine tract of introns and facilitating the recruitment of the U2 snRNP complex. Its function is pivotal in the spliceosome assembly, influencing alternative splicing events and thereby contributing to the regulation of gene expression. Recent studies have highlighted the importance of U2AF2 in various biological processes and its association with certain diseases, including cancers and neurodegenerative disorders. The overexpression or mutations in U2AF2 have been linked to altered splicing patterns that may lead to the dysregulation of critical pathways. Consequently, there is a growing interest in understanding the structural and functional properties of U2AF2, as well as its interactions with other spliceosomal components. Research involving the recombinant expression of U2AF2 aims to provide insights into its splicing mechanism and regulatory functions, facilitating the development of therapeutic strategies targeting splicing-related diseases. By elucidating the role of U2AF2 in splicing, scientists hope to advance our understanding of gene regulation and the potential for modulating splicing outcomes in various pathological conditions. As such, recombinant U2AF2 not only serves as a vital tool for biochemical assays and structural studies but also holds promise for uncovering novel insights into the intricate network of gene expression regulation.

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