Abcam, ab84770, Recombinant Tau381 protein

Size: 20µg / 50µg
Recombinant Tau381 protein is a Human Full Length protein, in the 1 to 381 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, WB.
Key facts
Purity:>90% Densitometry,
Expression system:Escherichia coli,
Tags:Tag free,
Applications:WB, SDS-PAGESee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:No,
Accession:P10636,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 7.5Constituents: 25% Glycerol (glycerin, glycerine), 0.87% Sodium chloride, 0.79% Tris HCl, 0.00385% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.00174% PMSF

Properties and Storage Information:
Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--80°C, Appropriate long-term storage conditions--80°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Tau381 also known as the Tau protein is a microtubule-associated protein with a molecular mass around 67 kDa found predominantly in neurons of the central nervous system. The Tau protein stabilizes microtubules which are important for maintaining cell structure intracellular transport and neuron stability. Tau is mostly localized in the axons of neurons where it facilitates the assembly and stabilization of microtubule structures.
Biological function summary
The Tau protein interacts with microtubules to help maintain the cellular architecture and transport mechanisms in neurons. Tau exists within various isoforms generated through alternative splicing of the MAPT gene. Tau interacts with other cytoskeletal proteins to preserve neuronal integrity and ensure efficient axonal transport. Not part of a larger complex Tau often undergoes phosphorylation affecting its binding properties and functional interactions with microtubules.
Pathways
Tau plays a significant role in the regulation of the microtubule-associated proteome and is essential for cytoskeletal dynamics. Key pathways involving Tau include the microtubule dynamics pathway and the phosphorylation regulation pathway. These pathways interact directly with proteins such as tubulin and glycogen synthase kinase 3 beta (GSK-3β) which modify Tau’s binding ability and influence microtubule stability.
Tau is closely linked to neurodegenerative conditions like Alzheimer's disease and frontotemporal dementia. Abnormal hyperphosphorylation of Tau results in the formation of neurofibrillary tangles a hallmark of Alzheimer’s pathology. This condition also involves the amyloid-beta protein which plays a role in disease progression and Tau protein aggregation. Understanding Tau and its relationship to amyloid-beta provides insights into potential therapeutic targets for these neurodegenerative disorders.