MAPT Human
Description
MAPT Recombinant Human (Isoform-4) produced in E.Coli is a single, non-glycosylated polypeptide chain containing 372 amino acids (1-352 a.a.) and having a molecular mass of 38.9 kDa (Real molecular weight on SDS-PAGE will be shift up). The MAPT is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Microtubule-Associated Protein Tau (MAPT), commonly referred to as Tau, is a protein predominantly expressed in neurons of the central nervous system. It plays a crucial role in stabilizing microtubules, which are essential components of the cytoskeleton. The recombinant form of human Tau protein is produced using Escherichia coli (E. coli) expression systems, allowing for detailed studies of its structure and function.
Tau protein is characterized by its ability to bind to microtubules and promote their assembly and stability. The protein has several isoforms resulting from alternative splicing, with the 441 amino acid isoform being one of the most studied. This isoform is known as “2N4R,” “Isoform Tau-F,” “Tau-4,” or "Tau 441" .
The carboxy-terminal domains of Tau associate with microtubules, stabilizing their structure, while other domains interact with the plasma membrane . Tau’s binding to microtubules is highly dynamic and regulated by phosphorylation, with more than 40 potential phosphorylation sites . Properly folded Tau is highly soluble, but when misfolded, it forms insoluble aggregates that can interfere with cellular functions and lead to cell death .
Abnormal phosphorylation of Tau can result in the self-assembly of tangles of paired helical and/or straight filaments. These aggregates are a hallmark of several neurodegenerative diseases, collectively known as tauopathies, which include Alzheimer’s disease . In Alzheimer’s disease, the aggregation of Tau into fibrils correlates with cognitive impairment . Understanding the mechanisms of Tau aggregation and its role in neurodegeneration is crucial for developing therapeutic strategies.
Producing recombinant human Tau protein involves expressing the protein in E. coli and purifying it using various chromatographic techniques. The purification process can be challenging due to Tau’s intrinsically disordered nature and its tendency to degrade . However, protocols have been developed to obtain high-purity, stable preparations of Tau suitable for in vitro studies, including aggregation experiments that mimic neurodegenerative processes .
Recombinant human Tau protein is widely used in research to study its biochemical properties, interactions with microtubules, and role in disease. It is also used in drug discovery efforts aimed at finding compounds that can prevent or reverse Tau aggregation. The availability of recombinant Tau allows researchers to conduct experiments under controlled conditions, providing valuable insights into the protein’s behavior and its implications for neurodegenerative diseases.
