Microtubule-associated protein 1A
Microtubule-associated protein 1A (806-814) is a synthetic peptide fragment derived from the larger microtubule-associated protein 1A (MAP1A), a key cytoskeletal component involved in microtubule stabilization and neuronal development. Comprising amino acids 806 to 814 of the parent protein, this peptide segment offers a focused tool for dissecting the molecular interactions and regulatory mechanisms governing microtubule dynamics. Researchers value such defined peptide sequences for their capacity to model specific binding domains, elucidate protein-protein interactions, and serve as substrates or probes in biochemical assays aimed at understanding cytoskeletal organization and neuronal function.
Protein-protein interaction studies: The 806-814 peptide fragment is frequently utilized in mapping interaction domains within the MAP1A protein, enabling researchers to pinpoint specific regions responsible for binding to microtubules or associated regulatory proteins. By incorporating this peptide into in vitro binding assays, investigators can systematically assess its affinity for tubulin, other microtubule-associated proteins, or candidate binding partners. This targeted approach provides valuable insights into the molecular determinants of cytoskeletal assembly and the modulation of microtubule stability in neuronal and non-neuronal cells.
Antibody epitope mapping: As a well-defined peptide segment, the 806-814 region of MAP1A is instrumental in the characterization and validation of antibodies raised against MAP1A or related cytoskeletal proteins. Researchers employ this peptide as a synthetic epitope to test antibody specificity, enabling the identification of antibody binding sites and the refinement of immunoreagents for use in western blotting, immunoprecipitation, or immunocytochemistry. Such applications are essential for ensuring the reliability of immunodetection techniques in neurobiological research.
Phosphorylation and post-translational modification studies: The peptide corresponding to residues 806-814 serves as a convenient substrate for in vitro kinase assays and other enzymatic modification studies. By exposing this fragment to specific kinases or modifying enzymes, scientists can monitor phosphorylation events or other post-translational modifications, facilitating the identification of regulatory sites within MAP1A. These experiments contribute to a deeper understanding of how dynamic modifications influence cytoskeletal function and neuronal signaling pathways.
Structural and biophysical analysis: Synthetic peptides derived from MAP1A, such as the 806-814 fragment, are valuable tools in structural biology for probing the conformational properties of microtubule-associated domains. Techniques such as circular dichroism spectroscopy, nuclear magnetic resonance (NMR), or surface plasmon resonance can be applied to this peptide to characterize its secondary structure, binding kinetics, or interaction thermodynamics. These studies provide foundational data for modeling the structural basis of microtubule association and regulation.
Peptide-based assay development: The defined sequence and biochemical relevance of the 806-814 peptide make it suitable for use in custom assay systems designed to monitor microtubule assembly, protein recruitment, or inhibitor screening. By serving as a capture or detection element in ELISA-style assays, or as a competitive ligand in binding studies, this peptide enables the quantitative analysis of molecular interactions relevant to cytoskeletal research. Such assay platforms are instrumental in advancing both basic research and the discovery of novel modulators of microtubule function.
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