Calmodulin-Dependent Protein Kinase II 281-309

Calmodulin-Dependent Protein Kinase II (281-309) is a peptide of calcium/calmodulin-dependent protein kinase II (CaM-kinase II).

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: R1267

CAS No:116826-37-0

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M.F/Formula
C₁₄₆H₂₅₄N₄₆O₃₉S₃
M.W/Mr.
3374.06
Sequence
One Letter Code: MHRQETVDCLKKFNARRKLKGAILTTMLA
three Letter Code: Met-His-Arg-Gln-Glu-Thr-Val-Asp-Cys-Leu-Lys-Lys-Phe-Asn-Ala-Arg-Arg-Lys-Leu-Lys-Gly-Ala-Ile-Leu-Thr-Thr-Met-Leu-Ala

Calmodulin-Dependent Protein Kinase II 281-309 is a synthetic peptide fragment corresponding to amino acid residues 281 through 309 of the CaMKII enzyme, a key serine/threonine kinase involved in calcium signaling pathways. As a biologically relevant peptide, it represents a critical region of CaMKII implicated in regulatory interactions and post-translational modifications that govern neuronal plasticity, learning, memory, and diverse cellular responses. Researchers utilize this peptide to probe the structure-function relationships within the kinase, dissect protein-protein interactions, and investigate the molecular basis of CaMKII-mediated signal transduction, making it an essential tool in neurobiology and cell signaling research.

Protein-Protein Interaction Studies: The 281-309 sequence of CaMKII contains motifs essential for binding regulatory proteins and substrates. By employing this peptide in binding assays, researchers can map interaction domains, identify novel binding partners, and delineate the molecular determinants of CaMKII association with scaffolding proteins, phosphatases, or synaptic components. Such studies are fundamental for elucidating the dynamic assembly of signaling complexes that underlie synaptic plasticity and neuronal communication.

Phosphorylation Mechanism Analysis: As a substrate-mimetic peptide, the CaMKII 281-309 fragment enables detailed investigation of phosphorylation events catalyzed by CaMKII and related kinases. In vitro kinase assays utilizing this peptide allow for precise measurement of enzyme activity, determination of phosphorylation site specificity, and assessment of regulatory influences by calmodulin or autoinhibitory domains. These analyses provide insight into the mechanisms governing CaMKII activation and the broader regulation of calcium-dependent signaling pathways.

Antibody Generation and Validation: The defined sequence of the 281-309 peptide serves as an immunogen for the production of highly specific antibodies targeting CaMKII. Such antibodies are invaluable for the detection, quantification, and localization of the kinase in biochemical assays, immunoblotting, and immunohistochemistry. Furthermore, synthetic peptides of this region are commonly used in epitope mapping and antibody validation studies to ensure selectivity and minimize cross-reactivity in experimental applications.

Structural and Biophysical Characterization: The CaMKII 281-309 peptide provides a tractable model for structural studies aimed at elucidating secondary structure elements, conformational dynamics, and domain organization within the full-length kinase. Techniques such as circular dichroism spectroscopy, NMR, and X-ray crystallography utilize this fragment to resolve local folding patterns and to inform rational design of modulators or inhibitors targeting the regulatory region of CaMKII.

Peptide-Based Screening and Inhibitor Development: The 281-309 region is often leveraged in high-throughput screening assays to identify small molecules or peptides that disrupt critical protein interactions or modulate kinase activity. By serving as a competitive binding partner or functional probe, this peptide aids in the discovery and characterization of novel CaMKII modulators, supporting the development of research tools for dissecting complex signaling networks and advancing the understanding of calcium-dependent cellular regulation.

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