Affiliations: [a] Department of Translational Science and Molecular Medicine, College of Human Medicine, Michigan State University, Grand Rapids, MI, USA
| [b]
Michigan Alzheimer’s Disease Center Core, Ann Arbor, MI, USA
| [c] Department of Neurology, University of Michigan, Ann Arbor, MI, USA
Correspondence:
[*]
Correspondence to: Irving E. Vega, PhD, 400 Monroe Ave NW, Grand Rapids, MI 49503, USA. Tel.: +1 616 234 2828; E-mail: irving.vega@hc.msu.edu.
Abstract: The accumulation of tau protein aggregates is a pathological hallmark in Alzheimer’s disease (AD) and other neurodegenerative diseases. However, the identity of the toxic tau conformation that propagates and induces neurodegeneration is still unknown. Anti-tau antibodies are a common tool used to differentiate between normal and pathological-associated tau forms or as passive immunotherapy in the quest to interfere with tau-mediated neurodegeneration. Here, we show that Tau13, a tau N-terminal antibody, preferentially enriches high molecular weight tau species produced in a tauopathy mouse model and AD. The data suggest that Tau13 has higher affinity to specific tau conformation presence in higher molecular weight tau species.
