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The Human Tau (Phospho) [pS396] ELISA quantitates Hu Tau (Phospho) [pS396] in human cerebrospinal fluid (CSF), buffered solution, or cell culture medium. The assay will exclusively recognize both natural and recombinant Hu Tau (Phospho) [pS396].
Principle of the method
The Human Tau (Phospho) [pS396] solid-phase sandwich ELISA (enzyme-linked immunosorbent assay) is designed to measure the amount of the target bound between a matched antibody pair. A target-specific antibody has been pre-coated in the wells of the supplied microplate. Samples, standards, or controls are then added into these wells and bind to the immobilized (capture) antibody. The sandwich is formed by the addition of the second (detector) antibody, a substrate solution is added that reacts with the enzyme-antibody-target complex to produce measurable signal. The intensity of this signal is directly proportional to the concentration of target present in the original specimen.
Rigorous validation
Each manufactured lot of this ELISA kit is quality tested for criteria such as sensitivity, specificity, precision, and lot-to-lot consistency. See manual for more information on validation.
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, ultimately 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.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Gene aliases : DDPAC, FTDP-17, MAPT, MAPTL, MSTD, MTBT1, MTBT2, PPND, PPP1R103, TAU
Gene ID : (Human) 4137
Gene symbol : MAPT
Protein Aliases : G protein beta1/gamma2 subunit-interacting factor 1, Microtubule-associated protein tau, microtubule-associated protein tau, isoform 4, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, protein phosphatase 1, regulatory subunit 103
UniProt ID (Human) P10636
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