Malantide is a dodecapeptide phosphorylated by cyclic AMP-dependent protein kinase (PKA), and increases PKA activity.
CAT No: R1502
CAS No:86555-35-3
Synonyms/Alias:Malantide;86555-35-3;L-Isoleucine, L-arginyl-L-threonyl-L-lysyl-L-arginyl-L-serylglycyl-L-seryl-L-valyl-L-tyrosyl-L-alpha-glutamyl-L-prolyl-L-leucyl-L-lysyl-;Malantide, Protein Kinase Substrate;G12395;
Malantide is a synthetic peptide that functions as a potent and selective substrate for protein kinase C (PKC), making it a valuable biochemical tool in signal transduction research. Structurally derived from the myelin basic protein (MBP) sequence, Malantide encompasses a defined peptide motif recognized and phosphorylated by PKC isoforms. Its established role as a model substrate has positioned it as a standard reagent in kinase activity assays, facilitating investigations into cellular phosphorylation events and kinase signaling pathways. The defined sequence and biochemical properties of Malantide contribute to its widespread adoption in studies focused on kinase specificity, phosphorylation mechanisms, and the modulation of intracellular signaling cascades.
Enzyme activity assays: Malantide is extensively utilized as a reference substrate in PKC activity assays, enabling researchers to quantitatively measure kinase function in vitro. Its high specificity for PKC-mediated phosphorylation allows for sensitive detection and kinetic characterization of enzyme activity under various experimental conditions. By serving as a consistent and reproducible substrate, it supports the development and optimization of assays for screening PKC modulators, inhibitors, or activators, which are essential in basic research and early-stage drug discovery.
Signal transduction research: The peptide is instrumental in dissecting the molecular mechanisms underlying PKC-dependent signaling pathways. By providing a defined phosphorylation target, Malantide facilitates the study of downstream signaling events following PKC activation, such as substrate recognition, phosphorylation kinetics, and the impact of cofactors or second messengers. These insights are critical for understanding the regulatory roles of PKC in cellular processes including proliferation, differentiation, and apoptosis.
Kinase specificity profiling: Researchers employ Malantide to assess the substrate selectivity of various PKC isoforms and to distinguish PKC activity from other kinases in complex biological samples. Its sequence specificity aids in validating the selectivity of novel kinase inhibitors or in mapping the substrate preferences of PKC family members. Such applications are particularly valuable for elucidating isoform-specific signaling events and for refining the design of selective kinase modulators.
Peptide-based assay development: The well-characterized nature of Malantide makes it an ideal standard for developing and validating peptide-based phosphorylation assays. Its use streamlines the calibration of analytical methods such as radiometric, colorimetric, or fluorescence-based detection systems. Reliable assay performance is crucial for high-throughput screening, mechanistic enzymology, and quantitative studies of phosphorylation dynamics.
Biochemical tool for mechanistic studies: As a synthetic peptide substrate, Malantide is frequently incorporated into mechanistic studies aiming to unravel the detailed kinetics and regulatory mechanisms of PKC catalysis. Its defined structure allows for systematic modification or labeling, enabling structure-activity relationship (SAR) studies, mapping of phosphorylation sites, and the exploration of conformational influences on substrate recognition. These applications provide foundational knowledge for advancing the understanding of kinase regulation and the design of next-generation biochemical probes.
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