Cat: IPD-X28093

Recombinant Human PTP-MEG2/PTPN9 Protein,His

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Analytical Data

  • Gene name

    PTP-MEG2/PTPN9

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    MEG2; Protein-tyrosine phosphatase MEG2; Tyrosine-protein phosphatase non-receptor type 9

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    P43378

  • Expression Region

    Gln289~Gln593

  • Molecular Weight

    39kDa

  • 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

PTP-MEG2 (Protein Tyrosine Phosphatase Megakaryocyte-Erythroid-Generated 2) and PTPN9 are members of the protein tyrosine phosphatase (PTP) family, which play crucial roles in cellular signaling processes by regulating phosphorylation states of tyrosine residues on proteins. These enzymes are implicated in various physiological processes, including cell growth, differentiation, and immune responses. Dysregulation of PTPs is often associated with diseases, including cancer and autoimmune disorders. The study of PTP-MEG2 and PTPN9 allows researchers to understand their specific functions and regulatory mechanisms in greater detail. Recent studies have suggested that these phosphatases may influence hematopoiesis and immune cell functions, making them potential targets for therapeutic interventions. Recombinant proteins of PTP-MEG2 and PTPN9 provide valuable tools for investigating their enzymatic activities, substrate interactions, and cellular roles. By utilizing recombinant technology, researchers can produce these proteins in a controlled manner, facilitating biophysical and biochemical analyses that may reveal novel insights into their contributions to cellular dynamics and disease pathology. This research is critical for identifying new biomarkers and therapeutic targets in hematological malignancies and autoimmune diseases, potentially leading to the development of innovative treatments.

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