Technical Data
Tau (Neurofibrillary Tangles Marker, Microtubule-associated Protein, MAP, Paired helical filament-tau, PHF-tau)
Tau is a microtubule binding protein that promotes microtubule assembly and stability. Tau is found to be the major component of the paired helical filaments (PHFs) found in the brains of patients with Alzheimer disease (AD) (1,2). Tau is hyperphosphorylated in PHFs, and specific phosphorylation sites have been implicated in the loss of Taus association with the membrane cortex during AD disease state, including Ser 199/202, Thr 231, and Ser 393/404 (3). Glycogen synthase kinase-3, or GSK-3, phosphorylates Tau on Ser 396 (4).

Suitable for use in Flow Cytometry, Western Blot, Immunocytochemistry. Other applications not tested.

Recommended Dilution:
Western Blot: 1:5,000-1:20,000
Immunocytochemistry: 1:100-1:500
Flow Cytometry: 1:160
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4°C for short-term only. For long-term storage, aliquot and store at -20°C. Aliquots are stable for at least 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Manufactured incorporating RabMAb® technology under Epitomics US patents, No 5,675,063 and 7,429,487, owned by Abcam.
100ul-20°CBlue IceHumanRabbit
Not determined
A synthetic phospho-peptide corresponding to residues surrounding serine 622 of human Tau.
Supplied as a liquid in 50 mM Tris-Glycine, pH 7.4, 0.15 M sodium chloride, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
Recognizes Tau phospholyated and unphospholyated on serine 622. Species crossreactivity: mouse and rat.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Goedert, M., et al. Proc Natl Acad Sci U S A. 85: 4051–5 (1988). 2. Jakes, R., et al. EMBO J. 10: 2725–9 (1991). 3. Maas, T., et al. IJ Biol Chem. 275: 15733–40 (2000). 4. Singh, T.J., et al. Arch. Biochem. Biophys. 328: 43–50 (1996).