Recombinant Human MAPT Protein

MAPT (microtubule-associated protein tau) is a neuronal protein encoded by the *MAPT* gene, primarily involved in stabilizing microtubules in axons, crucial for maintaining structural integrity and facilitating intracellular transport in neurons. Under physiological conditions, tau binds to tubulin, promoting microtubule assembly and regulating dynamics. However, abnormal post-translational modifications (e.g., hyperphosphorylation, truncation) or mutations in *MAPT* can lead to tau misfolding, aggregation, and the formation of neurofibrillary tangles (NFTs), a hallmark of neurodegenerative tauopathies such as Alzheimer’s disease, frontotemporal dementia, and progressive supranuclear palsy.

Recombinant MAPT proteins are engineered in vitro using expression systems (e.g., *E. coli*, mammalian cells) to produce purified, sequence-specific tau isoforms for research and therapeutic development. These proteins retain key functional domains, including microtubule-binding repeats and proline-rich regions, while enabling precise manipulation of phosphorylation sites or disease-associated mutations (e.g., P301L, R406W). Researchers utilize recombinant tau to study aggregation mechanisms, screen potential inhibitors, and model tau pathology in cellular or animal systems.

Advantages include batch consistency, scalability, and reduced ethical concerns compared to brain-derived tau. However, challenges remain in replicating native post-translational modifications and isoform diversity (e.g., six splice variants in the human brain). Current applications span drug discovery, biomarker validation, and structural studies using cryo-EM or NMR to elucidate tau-microtubule or tau-ligand interactions. As tau-targeted therapies gain momentum, recombinant MAPT proteins serve as indispensable tools for deciphering pathogenic pathways and advancing precision medicine for neurodegenerative diseases.