Cat: IPD-X40133

Recombinant Enterobacteria phage T4 wac Protein ,His & SUMO

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Analytical Data

  • Gene name

    wac

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Collar protein Whisker antigen control protein

  • Species

    Enterobacteria phage T4

  • Source

    E. coli

  • Tag

    N- His-SUMO

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P10104

  • Expression Region

    2-487aa

  • Molecular Weight

    67.7 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

Wac (Wnt-Associated Protein) is a crucial protein involved in various cellular processes, including cell signaling, proliferation, and differentiation, particularly in the context of the Wnt signaling pathway. The study of Wac has gained significant importance due to its implications in developmental biology and cancer research. Abnormalities in Wnt signaling are often associated with various cancers, making Wac a potential target for therapeutic interventions. Recent research has focused on the structural and functional characterization of Wac, highlighting its role as a co-factor in modulating Wnt signaling activity. Understanding the mechanisms by which Wac interacts with other proteins and influences cellular outcomes could provide valuable insights into its potential as a biomarker for cancer diagnosis or as a target for novel cancer treatments. Additionally, the reconstitution of Wac in vitro has enabled researchers to dissect its biochemical properties and interactions, paving the way for further elucidation of its role in both normal physiology and disease states. This growing body of knowledge not only enhances our understanding of fundamental biological processes but also opens new avenues for the development of strategic therapeutic approaches in Wnt-related pathologies.

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