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Your Position: Home > Antibody > p-tau181 > PT1-Y2073

Monoclonal Anti-Human p-tau181 Antibody, Mouse IgG2a (8D8C10)

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  • Source

    Monoclonal Anti-Human p-tau181 Antibody, Mouse IgG2a (8D8C10) is a Mouse monoclonal antibody produced from a hybridoma created by fusing SP2/0 myeloma and Mouse B-lymphocytes.

  • Clone

    8D8C10

  • Species

    Mouse

  • Isotype

    Mouse IgG2a | Mouse Kappa

  • Conjugate

    Unconjugated

  • Antibody Type

    Hybridoma Monoclonal

  • Reactivity

    Human

  • Immunogen

    Recombinant phosphorylated Tau181(pTau181) polypeptide.

  • Specificity

    Specifically recognizes Human p-Tau181 Protein.

  • Application
    ApplicationRecommended Usage
    IF1:50-1:500
  • 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-tau181 SDS-PAGE

Monoclonal Anti-Human p-tau181 Antibody, Mouse IgG2a (8D8C10) 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-tau181 IMMUNOFLUORESCENCE

2D cell staining: Immunofluorescent staining (10X) of phosphorylated tau in treated SH-SY5Y neuroblastoma cells with purified PT1-Y2073 at 1:200 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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Price(USD) : $1980.00

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