Cat: IPD-X40648

Recombinant Arabidopsis thaliana NFYA3 Protein ,His

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Analytical Data

  • Gene name

    NFYA3

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Transcriptional activator HAP2;C

  • Species

    Arabidopsis thaliana

  • Source

    E. coli

  • Tag

    N- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q93ZH2

  • Expression Region

    1-340aa

  • Molecular Weight

    41.6 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

The NFYA3 protein, a member of the NFY (Nuclear Factor Y) family, plays a crucial role in gene regulation, influencing various cellular processes such as cell growth, differentiation, and response to stress. Its significance has garnered attention in the context of diseases, including cancer, where aberrant expression or function of NFYA3 can contribute to tumorigenesis and disease progression. Research has shown that NFYA3 can interact with various DNA sequences and proteins, thereby affecting the transcription of target genes. Furthermore, studies have indicated that NFYA3 may be involved in modulating processes such as apoptosis and cell cycle regulation. Given its pivotal role, understanding the structure and function of NFYA3, including its post-translational modifications and interactions with other regulatory proteins, is essential for delineating its role in cellular physiology and pathology. Advances in recombinant DNA technology have enabled the production of tagged or mutated NFYA3 proteins for biochemical and structural studies, allowing researchers to unravel its molecular mechanisms and potentially identify it as a therapeutic target. As research progresses, elucidating the precise functions and pathways of NFYA3 will not only enhance our understanding of fundamental biological processes but also pave the way for novel interventions in related diseases, particularly in oncology.

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