Active Human Recombinant Truncated Tau Fragment (AA297-391) (dGAE C322A) Protein Monomer


Curves show increased fluorescence (correlated to tau aggregation) over time when truncated tau fragment (AA297-391) (dGAE C322A) monomer is combined with truncated tau fragment (AA297-391) (dGAE C322A) preformed fibrils (Type 1).

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Active Human Recombinant Truncated Tau Fragment (AA297-391) (dGAE C322A) Protein Monomer

For Research Use Only

Specificity: 10.133 kDa
Species: Human
Expression System: E. coli
Buffer: PBS pH 7.4
Storage Temperature: -80ºC

Product manufactured in Canada by StressMarq.

Additional Information

Scientific Background

Alzheimer’s Disease (AD) is the most common neurodegenerative disease, affecting 10% of seniors over the age of 65 (1). It was named after Alois Alzheimer, a German scientist who discovered tangled bundles of fibrils where neurons had once been in the brain of a deceased patient in 1907 (2). Tau (tubulin-associated unit) is normally located in the axons of neurons where it stabilizes microtubules. Tauopathies such as AD are characterized by neurofibrillary tangles containing paired helical filaments (PHFs). A truncated 95-amino acid fragment corresponding to residues 297-391 of full-length tau has been shown to assemble into PHF-like fibrils in vitro in the absence of additives or templates (3). This fragment has been found in the core of PHFs from AD brains and forms filaments that closely resemble PHFs isolated from AD brains (3). The C322A mutation leads to enhanced self-assembly into long and ordered PHFs (3).

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