Tau protein (592-597), Human (TFA) is a peptide fragment of human Tau protein. The dysfunction of Tau protein is involved in neurodegeneration and dementia.
CAT No: R1710
Tau protein (592-597), Human TFA is a synthetic peptide fragment derived from the human tau protein, corresponding to amino acids 592 through 597. As a key component of the microtubule-associated protein tau, this peptide represents a specific sequence within the C-terminal region, which is of significant interest in neurobiological and biochemical research. The tau protein is widely recognized for its role in stabilizing microtubules in neuronal cells, and its dysfunction is closely linked to the development of neurodegenerative disorders characterized by tauopathies. The 592-597 fragment provides a valuable molecular tool for dissecting the structural and functional aspects of tau, enabling researchers to explore mechanisms of aggregation, phosphorylation, and protein-protein interactions relevant to disease progression and cellular biology.
Aggregation studies: The 592-597 tau peptide is frequently employed in aggregation assays to investigate its propensity to form fibrillar or oligomeric structures under specific biochemical conditions. Researchers utilize this fragment to model the nucleation and elongation phases of tau aggregation, which are critical for understanding the formation of neurofibrillary tangles observed in tauopathies. By isolating this sequence, scientists can assess its intrinsic aggregation behavior and determine how modifications or interactions with cofactors influence pathological assembly processes.
Epitope mapping: The defined sequence of the 592-597 region serves as an essential tool for immunological studies aimed at mapping antibody binding sites on tau. Antibodies raised against this peptide or used in competition assays can help delineate linear epitopes, facilitating the development and validation of tau-specific immunoreagents. Such mapping is instrumental in generating highly specific antibodies for research applications, including immunodetection, immunoprecipitation, and the exploration of conformational changes in the full-length protein.
Phosphorylation analysis: As post-translational modifications like phosphorylation play a pivotal role in tau function and dysfunction, the 592-597 fragment is utilized to study kinase-substrate specificity and phosphorylation kinetics. Researchers can employ this peptide in in vitro kinase assays to determine which kinases target this region and to analyze the impact of phosphorylation on peptide structure, aggregation propensity, or downstream signaling events. These insights contribute to a deeper understanding of tau regulation and pathology.
Protein-protein interaction studies: Investigations into the molecular interactions involving tau often leverage synthetic peptides such as the 592-597 fragment to probe binding partners and interaction motifs. This approach enables identification of proteins or small molecules that specifically associate with the C-terminal region of tau, providing mechanistic insights into cellular pathways affected by tau dysregulation. Such studies are foundational for elucidating the broader interactome of tau and for screening potential modulators of its activity.
Analytical standards: The well-defined nature and sequence fidelity of the tau 592-597 peptide make it suitable as a reference standard in analytical techniques such as mass spectrometry or high-performance liquid chromatography. Researchers use this peptide to calibrate instruments, validate detection methods, and quantify tau-derived fragments in complex biological samples. Employing synthetic standards enhances the accuracy and reproducibility of analytical workflows focused on tau quantification and characterization in both basic and applied research settings.
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