Tau Monoclonal Antibody (HT7), Alexa Fluor™ 647, eBioscience™, Invitrogen™

Description

• Description: This HT7 monoclonal antibody recognizes human and bovine Tau protein
• The epitope of this antibody has been mapped to residues 159 through 163, corresponding to the amino acid sequence PPGQK of human Tau40
• In certain cell lines and tissue other than brain, clone HT7 may show a low but distinct amount of nonspecific staining
• Therefore we recommend the use of clone HT7 to detect Tau expression by flow cytometry in human Tau transfected cells or tissue derived from human Tau transgenic mice
• This antibody does not cross-react with murine Tau
• Applications Reported: This HT7 antibody has been reported for use in flow cytometric analysis
• Applications Tested: This HT7 antibody has been pre-diluted and tested by flow cytometric analysis of Human Tau transfected 293 HEK cells using the Intracellular Fixation & Permeabilization Buffer Set (Product No
• 88-8824-00) and protocol
• Please refer to Staining Intracellular Antigens for Flow Cytometry, Protocol A: Two step protocol for intracellular (cytoplasmic) proteins located at www.thermofisher.com/flowprotocols
• This antibody may be used at 5μL (0.25 μg) per test
• A test is defined as the amount (μg) of antibody that will stain a cell sample in a final volume of 100 μL
• Cell number should be determined empirically but can range from 10^5 to 10^8 cells/test
• 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.