Cat: IPD-X28506

Recombinant Human NUP214 Protein,Strep & His

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Analytical Data

  • Gene name

    NUP214

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    CAIN; CAN; KIAA0023

  • Species

    Human

  • Source

    E. coli

  • Tag

    Strep;His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P35658-1

  • Expression Region

    M1-S450

  • 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

NUP214, also known as nucleoporin 214, is a crucial component of the nuclear pore complex, which mediates the transport of molecules between the nucleus and the cytoplasm. Recent studies have highlighted its significance in various cellular processes, including gene regulation and cell division. Abnormalities in NUP214 expression or function have been implicated in several diseases, particularly leukemia, where it can contribute to chromosomal translocations involving the mixed lineage leukemia (MLL) gene. This association underlines the importance of understanding NUP214's role in cellular pathways and its potential as a therapeutic target. The development of recombinant NUP214 protein has facilitated detailed studies of its structure and function, allowing researchers to investigate its interactions with other nuclear pore components and its involvement in cellular signaling pathways. Additionally, the study of NUP214 has expanded to include its role in viral infections, where viruses may hijack the nuclear transport system for their replication, further emphasizing its relevance in virology and potential as a drug target. As research progresses, the recombinant NUP214 protein serves as an essential tool for elucidating mechanisms underlying nuclear transport and disease pathogenesis, paving the way for innovative therapeutic strategies.

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