Tau Monoclonal Antibody (HT7), Invitrogen™

Description

• MN1000 recognizes normal Tau from human and bovine brain and PHF-Tau
• No cross reactivity with Tau from rat brain has been observed
• The epitope of this antibody has been mapped on human Tau between residue 159 and 163 (numbering according to human Tau40), corresponding to the amino acid sequence PPGQK
• MN1000 detects Tau which has a predicted molecular weight of approximately 79 kDa
• Purity is >95% as determined by SDS-PAGE
• Tau is a neuronal microtubule-associated protein found predominantly on axons
• The function of Tau is to promote tubulin polymerization and stabilize microtubules
• The C-terminus binds axonal microtubules while the N- terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both
• Axonal polarity is predetermined by TAU/MAPT localization (in the neuronal cell) in the domain of the cell body defined by the centrosome
• The short isoforms allow plasticity of the cytoskeleton while the longer isoforms may preferentially play a role in its stabilization
• In its hyper-phosphorylated form, Tau is the major component of paired helical filaments (PHF), the building block of neurofibrillary lesions in Alzheimer's diseases (AD) brain
• Hyper-phosphorylation impairs the microtubule binding function of Tau, resulting in the destabilization of microtubules in AD brains, μgtimately leading to the degeneration of the affected neurons
• Numerous serine/threonine kinases phosphorylate Tau, including GSK-3beta, protein kinase A (PKA), cyclin-dependent kinase 5 (cdk5) and casein kinase II
• Hyper-phosphorylated Tau is found in neurofibrillary lesions in a range and other central nervous system disorders such as Pick's disease, frontotemporal dementia, cortico-basal degeneration and progressive supranuclear palsy.