Cat: PA2000-1661

Recombinant E.coli CTN Protein,His

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Analytical Data

  • Gene name

    CTN

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    CTN;Catenin alpha-3

  • Species

    E.coli

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P53441

  • Expression Region

    1-172aa

  • AA Sequence

    MQKYGSKKIG ATSATSSNKQ KVQIELTDEQ RQEIKEAFDL FDMDGSGKID AKELKVAMRA LGFEPKKEEI KKMISGIDNG SGKIDFNDFL QLMTAKMSEK DSHAEIMKAF RLFDEDDSGF ITFANLKRVA KDLGENMTDE ELREMIEEAD RSNQGQISKE DFLRIMKKTN LF

  • Molecular Weight

    19.6 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.

Quality inspection process

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Protein Description

CTN (Catenin) proteins are crucial multifunctional regulators that play significant roles in cellular processes such as adhesion, signaling, and gene expression. These proteins, particularly beta-catenin, are integral components of the Wnt signaling pathway, which is vital for various developmental processes and cellular homeostasis. Dysregulation of CTN proteins has been implicated in numerous diseases, including cancer, where aberrant activation of beta-catenin can lead to uncontrolled cell proliferation and tumor formation. The study of CTN recombinant proteins has gained momentum as researchers seek to understand the molecular mechanisms underlying their function and regulation. By producing CTN proteins through recombinant DNA technology, scientists can investigate their structure, interactions, and pathways in detail. This research holds promise not only for elucidating fundamental biological processes but also for developing targeted therapeutic strategies to combat diseases linked to CTN dysregulation. The advancement of techniques such as X-ray crystallography and cryo-electron microscopy allows for the precise characterization of CTN proteins, which may lead to the identification of novel drug targets and biomarkers for early disease detection. As a result, the exploration of CTN recombinant proteins represents an essential frontier in molecular biology and medicine, with the potential to impact cancer research and therapeutic development significantly.

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