Abcam, ab256153, Recombinant human Tau (mutated P301S) protein monomer (Active)

Size: 100µg
Recombinant human Tau (mutated P301S) protein monomer (Active) is a Human Full Length protein, in the 1 to 441 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, WB, FuncS.
Key facts
Purity:>95%,
Expression system:Escherichia coli,
Tags:Tag free,
Applications:WB, SDS-PAGE, FuncSSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:Yes,
Biological activity:Thioflavin T emission curves show increased fluorescence (correlated to tau aggregation) over time in tau monomers (ab256153). A greater increase in fluorescence is seen when 50μM monomer (ab256153) is combined with 10 nM PFFs (ab246003 or ab256152), as the fibrils seed the formation of new fibrils from the pool of monomers. Thioflavin T ex = 450 nm, em = 485 nm.,
Accession:P10636,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 7.4Constituents: 0.58% Sodium chloride, 0.24% HEPES

Product details:
Monomer.

Properties and Storage Information:
Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--80°C, Appropriate long-term storage conditions--80°C

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Tau also known as microtubule-associated protein Tau (MAPT) plays an important role in stabilizing microtubules in neuronal cells. Tau is primarily found in the central nervous system but also exists in peripheral neurons. Human Tau protein comes in six isoforms due to alternative splicing with molecular weights ranging from 48 kDa to 67 kDa. This protein predominantly locates in the axons of neurons where it maintains the stability of microtubule tracks necessary for axonal transport.
Biological function summary
Tau is involved in the assembly and stabilization of microtubules essential for maintaining neuronal structure. It interacts with microtubule-binding domains (MBD) to bind and bundle microtubules facilitating intracellular transport. Tau forms a part of the neuronal cytoskeleton complex working closely with other cytoskeletal proteins to preserve the proper axonal transport and function. Abnormally phosphorylated Tau often termed phospho-Tau disrupts this complex affecting microtubule stability.
Pathways
Tau has critical involvement in several signaling cascades such as the microtubule-binding and transport pathways. Glycogen synthase kinase 3 beta (GSK3β) and cyclin-dependent kinase 5 (CDK5) frequently phosphorylate Tau controlling its interaction with microtubules. Phosphorylated Tau accumulates leading to the formation of neurofibrillary tangles often observed in neurodegenerative conditions. Additionally Tau interacts with GAPDH impacting cellular energy regulation through potential pathway cross-talk involving oxidative stress responses.
Tau is closely associated with Alzheimer's disease and frontotemporal dementia. In Alzheimer's disease hyperphosphorylated Tau aggregates into paired helical filaments forming neurofibrillary tangles while similar aggregates are observed in frontotemporal dementia. In these conditions Tau links to amyloid precursor protein (APP) where misregulated phosphorylation-driven interactions contribute to neurodegeneration. Identifying phospho-Tau and its altered interactions with related proteins aids in understanding and potentially treating these disorders.