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Description

Microtubule-associated protein tau (UniProt: P10636, also known as Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau) is encoded by the MAPT (also known as MAPTL, MTBT1, TAU) gene (Gene ID: 4137) in human. Tau, a highly asymmetric and heat-stable protein, is expressed mainly in the brain, where it regulates the stability and orientation of microtubules in neurons, astrocytes, and oligodendrocytes. Tau protein is reported to be the predominant component of the paired helical filaments (PHFs) and neurofibrillary tangles (NFTs) that are characteristic of pathological brain lesions in Alzheimer s disease. The dephosphorylation of Tau protein promotes rapid and extensive microtubule polymerization, while the phosphorylation of Tau decreases its ability to promote microtubule assembly. Tau is a substrate for a multitude of protein kinases, including CaM kinase II, casein kinase II, protein kinase A (PKA), MAP kinase (ERK2), Cdk5/ p35, and glycogen synthase kinase-3 (GSK-3) and is phosphorylated at many different sites in Alzheimer s disease brain. It is believed that the phosphorylation of specific sites, rather than the overall extent of phosphorylation, is important in modulating the ability of Tau to bind microtubules and promote microtubule assembly. This antibody (clone RN235) specifically reacts with tau phosphorylated at serine 235, and detects intraneuronal NFTs (iNFTs), and extraneuronal NFTs (eNFTs) in the brain tissue. Although theoretically it can also react with phospho Thr231, but EC50 is very high compared to reactivity with phospho Ser235 (407 nM vs 0.61 nM). (Ref.: Brici, D., et al. (2018). J. Alzheimer s Dis. 61(3), 899-905).