Technical Data
Tau (Microtubule-associated Protein Tau, MAPT, DDPAC, FTDP-17, MAPTL, MSTD, MTBT1, MTBT2, Neurofibrillary Tangle Protein, Paired Helical Filament-tau, PHF-tau, PPND)
Tau is a microtubule-associated protein that is the major component of dense neurofibrillary tangles in brain tissue which are one of the characteristics of Alzheimer’s disease. This antibody will help identify the tau protein and positively stain neurofibrillary tangles, neuropil threads and abnormal neurites in senile plaques of Alzheimer’s diseased brain tissue for research applications.

Suitable for use in Immunohistochemistry. Other applications not tested.

Recommended Dilution:
Immunohistochemistry: 1:50-1:100 for 1 hr. at RT
Optimal dilutions to be determined by the researcher.

Positive Control:
Human brain, Alzheimer’s disease. Cytoplasmic labeling of neurofibrillary tangles, neuropil threads and dystrophic neurites surrounding senile plaques.

Storage and Stability:
Lyophilized powder may be stored at -20°C. Stable for 12 months at -20°C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Reconstituted product is stable for 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.
1ml-20°CBlue IceMouse
Not determined
Bovine tau protein.
Supplied as a lyophilized powder in 15mM sodium azide. Reconstitute with 1ml of dH2O.
Recognizes tau. Species Crossreactivity: Human.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1.Dickson D W, Ksiezak-Reding H, Liu W K, et al.. Immunocytochemistry of neurofibrillary tangles with antibodies to subregions of tau protein: identifica- tion of hidden and cleaved tau epitopes and a new phosphorylation site. Acta Neuropathol. 84:596-605 (1992). 2.Lang E and Otvos L. A serine to proline change in the Alzheimer’s disease-associated epitope tau 2 results in altered secondary structure, but phos- phorylation overcomes the conformational gap. Biochemical and Biophysical Research Communications. 188(1):162-169 (1992). 3.Papasozomenos S C. Tau protein immunoreactivity in dementia of the Alzheimer type: II. Electron microscopy and pathogenetic implications. Effects of fixation on the morphology of the Alzheimer’s abnormal filaments. Laboratory Investigation. 60(3):375-389 (1989).