Cat: IPD-X40020

Recombinant Human TIAF1 Protein ,GST

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Analytical Data

  • Gene name

    TIAF1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    12KDA TGF-beta-1-induced antiapoptotic factor

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- GST

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O95411

  • Expression Region

    1-115aa

  • Molecular Weight

    39.4 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

TIAF1 (TGF-β-induced anti-apoptotic factor 1) is a protein that plays a crucial role in cellular responses to stress and apoptosis regulation. Its overexpression has been implicated in various cancers, making it a significant focus of research in the fields of oncology and molecular biology. Studies have shown that TIAF1 can modulate signaling pathways, particularly those associated with the TGF-β family, influencing cell survival and proliferation. The protein's ability to interact with other cellular factors also suggests its involvement in broader biological processes, including inflammation and fibrosis. Understanding the mechanisms of TIAF1 action at the molecular level could provide insights into its potential as a therapeutic target. Recent advances in recombinant protein technology have enabled researchers to produce TIAF1 in controlled laboratory settings, facilitating the exploration of its structural and functional characteristics. This has led to a better understanding of how TIAF1 contributes to disease progression and the development of novel strategies for intervention in TGF-β-related pathologies. As the role of TIAF1 becomes clearer, it presents opportunities for targeted therapies that could improve patient outcomes in cancers and other diseases linked to TGF-β signaling dysregulation. Overall, the study of TIAF1 and its recombinant variants is an exciting area of research with implications for understanding cancer biology and developing new therapeutic strategies.


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