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Your Position: Casa > Antibody > p-tau217 > PT7-Y2074

Monoclonal Anti-Human p-tau217 Antibody, Mouse IgM (6G7C8)

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  • Source

    Monoclonal Anti-Human p-tau217 Antibody, Mouse IgM (6G7C8) is a Mouse monoclonal antibody produced from a hybridoma created by fusing SP2/0 myeloma and Mouse B-lymphocytes.

  • Clone

    6G7C8

  • Species

    Mouse

  • Isotype

    Mouse IgM | Mouse Kappa

  • Conjugate

    Unconjugated

  • Antibody Type

    Hybridoma Monoclonal

  • Reactivity

    Human

  • Immunogen

    Recombinant phosphorylated Tau217(pTau217) polypeptide.

  • Specificity

    Recombinant phosphorylated Tau217(pTau217) polypeptide.

  • Application
    ApplicationRecommended Usage
    IF1:50-1:200
  • Purity

    >95% as determined by SDS-PAGE.

  • Purification

    Protein A purified/ Protein G purified

  • Formulation

    Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

    Contact us for customized product form or formulation.

  • Reconstitution

    Please see Certificate of Analysis for specific instructions.

    For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

  • Storage

    For long term storage, the product should be stored at lyophilized state at -20°C or lower.

    Please avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. -20°C to -70°C for 12 months in lyophilized state;
    2. -70°C for 3 months under sterile conditions after reconstitution.
SDS-PAGE
p-tau217 SDS-PAGE

Monoclonal Anti-Human p-tau217 Antibody, Mouse IgM (6G7C8) on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95% (With Star Ribbon Pre-stained Protein Marker).

Immunofluorescence
 p-tau217 IMMUNOFLUORESCENCE

2D cell staining: Immunofluorescent staining (10X) of phosphorylated tau in treated SH-SY5Y neuroblastoma cells with purified PT7-Y2074 at 1:100 dilution. DAPI (blue) was used as nuclear counterstain.

  • Background
    Tau, the microtubule‐associated protein, forms insoluble filaments that accumulate as neurofibrillary tangles in Alzheimer's disease (AD) and related tauopathies. Under physiological conditions, tau regulates the assembly and maintenance of the structural stability of microtubules. In the diseased brain, however, tau becomes abnormally hyperphosphorylated, which ultimately causes the microtubules to disassemble, and the free tau molecules aggregate into paired helical filaments.
  • Clinical and Translational Updates

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