Cat: IPD-X38716

Recombinant Human PTPRE Protein,His

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Analytical Data

  • Gene name

    PTPRE

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    PTPR-E; HPTPE; PTPE; R-PTP-EPSILON; Receptor-type tyrosine-protein phosphatase epsilon

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P23469

  • Expression Region

    Ile346~Gln500

  • Molecular Weight

    23kDa

  • 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

PTPRE (Protein Tyrosine Phosphatase Receptor Type E) is a receptor-type protein tyrosine phosphatase that plays a significant role in various cellular processes, including cell adhesion, migration, and signaling. Its involvement in cellular signaling pathways makes it an attractive target for research into cancer and other diseases where such pathways are dysregulated. The study of PTPRE and its reconstitution as a recombinant protein has opened new avenues for understanding its function in physiological and pathological contexts. Researchers have focused on elucidating the structural characteristics, enzymatic activity, and interaction with other proteins of PTPRE, aiming to uncover its role in cell signaling and potential as a therapeutic target. Recombinant PTPRE, produced through genetic engineering techniques, allows for detailed biochemical analyses and functional assays, providing insights into how mutations or alterations in this protein could contribute to disease development. In recent years, studies have increasingly linked PTPRE dysfunction to various cancer types, emphasizing its significance in cancer biology and therapy. Furthermore, the ability to produce this protein in a laboratory setting has facilitated the exploration of its inhibitory mechanisms, potential as a biomarker, and role in therapeutic development. Overall, ongoing research into PTPRE's recombinant protein forms is crucial for advancing our understanding of its biological functions and therapeutic implications.

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