Unknown

Dataset Information

0

Tau13 Antibody Preferentially Immunoprecipitates High Molecular Weight Tau Proteins.


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.

SUBMITTER: Umstead A 

PROVIDER: S-EPMC6516460 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature

altmetric image

Publications

Tau13 Antibody Preferentially Immunoprecipitates High Molecular Weight Tau Proteins.

Umstead Andrew A   Vega Irving E IE  

Journal of Alzheimer's disease : JAD 20190101 2


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 a  ...[more]

Similar Datasets

| S-EPMC4743414 | biostudies-literature
| S-EPMC5906480 | biostudies-literature
| S-EPMC5752625 | biostudies-literature
2020-12-04 | PXD020483 | Pride
| S-EPMC2779374 | biostudies-literature
| S-EPMC5091298 | biostudies-literature