Mouse Anti-PHF Recombinant Antibody (clone MN423) (CAT#: PABW-103)

Figure 1 Neurofibrillary Pathology of the Alzheimer’s Disease Brain.

Triple-labelled neurofibrillary tangle (white colour in the merge channel) is composed of Glu391-truncated tau (MN423-positive) in a conformationally altered state (Tau-66-positive). These alterations of the tau protein are absent in neuropil threads, which are predominantly observed in the red channel.

Basurto-Islas, G., Mondragón-Rodríguez, S., Binder, L. I., & García-Sierra, F. Pathology of the Cleaved Tau Protein in the Context of Toxicity and the Formation of Neurofibrillary Tangles.

Figure 2 Quantitative Western blot analysis of the core PHF subunit and its mutants gives results complementary to those obtained by ELISA.

100 ng of individual tau proteins were loaded onto 10–20% gradient SDS–PAGE. Following electroblotting, membrane was stained with peroxidase‐labeled mAb 423.

Skrabana, R., Kontsek, P., Mederlyova, A., Iqbal, K., & Novak, M. (2004). Folding of Alzheimer's core PHF subunit revealed by monoclonal antibody 423. FEBS letters, 568(1-3), 178-182.

Figure 3 Quantitative Western blot analysis of the core PHF subunit and its mutants gives results complementary to those obtained by ELISA.

Comparison of reactivity in competitive ELISA (expressed as reciprocal EC50 values) and Western blot reactivity (corrected for molecular weight of individual proteins). All data are normalized to 100% values of dGAE core PHF subunit.

Skrabana, R., Kontsek, P., Mederlyova, A., Iqbal, K., & Novak, M. (2004). Folding of Alzheimer's core PHF subunit revealed by monoclonal antibody 423. FEBS letters, 568(1-3), 178-182.

Figure 4 Folding of subunit core PHF into β‐sheet conformation.

(A) Immunoelectron microscopy of Pronase‐resistant core PHF shows typical immunogold decoration with mAb 423. Pronase‐resistant core was isolated and immunodecorated as described 5, 6. PHFs were isolated from AD brain, stage VI, according to Braak 20. (B) Primary structure of core PHF subunit (dGAE) with individual segments essential for polypeptide folding (red – based on EC50 values) and with regions of predicted β‐strands is shown. (C) Core PHF subunit adopts β‐sheet structure. Proposed core structure is based on predicted β‐strand propensities and experimental EC50 values of core PHF specific mAb 423.

Skrabana, R., Kontsek, P., Mederlyova, A., Iqbal, K., & Novak, M. (2004). Folding of Alzheimer's core PHF subunit revealed by monoclonal antibody 423. FEBS letters, 568(1-3), 178-182.