Calmodulin-Dependent Protein Kinase II (290-309) is a potent CaMK antagonist with an IC50 of 52 nM for inhibition of Ca2+/calmodulin-dependent protein kinase II.
CAT No: R1268
CAS No:115044-69-4
Synonyms/Alias:115044-69-4;L-Alanine, L-leucyl-L-lysyl-L-lysyl-L-phenylalanyl-L-asparaginyl-L-alanyl-L-arginyl-L-arginyl-L-lysyl-L-leucyl-L-lysylglycyl-L-alanyl-L-isoleucyl-L-leucyl-L-threonyl-L-threonyl-L-methionyl-L-leucyl-;CaM kinase II (290-309);MFCD00076719;DA-62012;FC110422;PD076359;Calmodulin Binding Domain - CAS 115044-69-4;Calmodulin-dependent protein kinase ii(290-309);H-Leu-Lys-Lys-Phe-Asn-Ala-Arg-Arg-Lys-Leu-Lys-Gly-Ala-Ile-Leu-Thr-Thr-Met-Leu-Ala-OH; H-LKKFNARRKLKGAILTTMLA-OH;
Calmodulin-Dependent Protein Kinase II 290-309 is a synthetic peptide fragment derived from the regulatory region of the CaMKII enzyme, a serine/threonine kinase that plays a pivotal role in calcium signal transduction pathways. This peptide encompasses amino acids 290 to 309 of the CaMKII protein, a sequence known to participate in autoinhibitory and regulatory interactions that modulate kinase activity. Its unique biochemical properties make it a valuable molecular tool for dissecting the mechanisms of CaMKII-mediated signaling, which is integral to processes such as synaptic plasticity, learning, and memory. Researchers utilize this peptide to probe the structural and functional aspects of kinase regulation, providing insights into neuronal communication and cellular adaptation to calcium flux.
Kinase activity modulation: As a segment of the CaMKII regulatory domain, the 290-309 peptide is frequently employed to investigate the autoinhibitory mechanisms governing kinase activation. By acting as a competitive inhibitor or by mimicking endogenous regulatory sequences, it enables the study of how conformational changes influence substrate recognition and phosphorylation events. This application is particularly significant in elucidating the molecular basis of kinase switching between active and inactive states, thereby advancing understanding of signal transduction fidelity in neuronal and non-neuronal cells.
Protein-protein interaction studies: The 290-309 region of CaMKII is implicated in interactions with various binding partners, including calmodulin and other synaptic proteins. Researchers use the peptide to map interaction domains, assess binding affinities, and characterize the specificity of protein complexes involved in synaptic scaffolding and signaling. Such studies are crucial for unraveling the molecular architecture of postsynaptic density and the dynamic assembly of signaling networks that underlie synaptic strength and plasticity.
Phosphorylation site mapping: The synthetic peptide serves as a defined substrate in in vitro phosphorylation assays aimed at characterizing the specificity and kinetics of CaMKII and related kinases. By providing a controlled sequence context, it allows for precise identification of phosphorylation sites, examination of consensus motifs, and evaluation of the impact of post-translational modifications on regulatory function. This approach supports the development of targeted inhibitors and the exploration of phosphorylation-dependent signaling cascades.
Antibody generation and validation: Due to its well-characterized sequence and structural relevance, the 290-309 peptide is utilized as an immunogen for the production of polyclonal and monoclonal antibodies specific to the regulatory domain of CaMKII. These antibodies are essential tools for immunodetection, localization, and quantification of the kinase in various biological samples. Additionally, the peptide is employed in antibody validation assays to confirm specificity and to minimize cross-reactivity in downstream applications such as Western blotting, immunoprecipitation, and immunohistochemistry.
Structural and biophysical analysis: The defined sequence of the 290-309 peptide enables detailed structural studies using techniques such as NMR spectroscopy, circular dichroism, and molecular modeling. By examining its conformational properties in solution or in complex with binding partners, researchers gain insights into the folding, dynamics, and interaction interfaces of the CaMKII regulatory domain. These analyses contribute to a deeper understanding of the structural determinants that govern kinase function and regulation, informing the design of novel modulators for research and potential industrial applications.
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