MARCKS Peptide(151-175), Phosphorylated is a phosphorylated peptide corresponding to the basic effector domain of myristoylated alanine-rich protein kinase C substrate protein (MARCKS). Phosphorylation of MARCKS Peptide (151-175) reverses its inhibition of phospholipase C (PLC)-catalyzed hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2).
CAT No: R1503
MARCKS Peptide(151-175), Phosphorylated is a synthetic phosphopeptide corresponding to amino acids 151 through 175 of the Myristoylated Alanine-Rich C Kinase Substrate (MARCKS) protein, with phosphorylation at specific serine residues. As a member of the MARCKS family, this peptide plays a significant role in the regulation of actin cytoskeletal dynamics and cellular signaling pathways, particularly those mediated by protein kinase C (PKC). The phosphorylated form serves as a critical molecular tool for dissecting the functional consequences of MARCKS phosphorylation in various biochemical and cell biology contexts, making it a valuable resource for research focused on signal transduction, cytoskeletal regulation, and membrane interactions.
Phosphorylation studies: As a well-defined phosphopeptide, the MARCKS (151-175) fragment is widely used in phosphorylation research to elucidate the role of site-specific phosphorylation events on MARCKS function. Its sequence and phosphorylation state allow researchers to model the effects of PKC-mediated phosphorylation, providing a controlled substrate for in vitro kinase assays and phosphatase studies. This enables detailed investigation into the regulation of MARCKS by kinases and phosphatases, advancing understanding of phosphorylation-dependent signaling mechanisms.
Protein-protein interaction analysis: The phosphorylated peptide serves as a valuable probe for studying protein-protein interactions involving MARCKS and its binding partners. By mimicking the native phosphorylation state, it facilitates the identification and characterization of proteins that specifically recognize or are regulated by phosphorylated MARCKS motifs. Such analyses are central to mapping interaction networks that govern cytoskeletal remodeling, vesicle trafficking, and cellular adhesion processes.
Signal transduction research: Utilization of this phosphopeptide in cell-free systems or cell-based assays enables researchers to investigate the downstream effects of MARCKS phosphorylation within signal transduction pathways. The peptide can be applied to model the dynamic regulation of actin-binding and membrane association properties, providing mechanistic insight into how phosphorylation modulates MARCKS activity during cellular responses to external stimuli.
Antibody validation and epitope mapping: The defined sequence and phosphorylation status of the MARCKS (151-175) peptide make it an ideal standard for validating the specificity and sensitivity of phospho-specific antibodies. It is routinely employed in immunoassays such as Western blotting, ELISA, and immunoprecipitation to confirm antibody recognition of phosphorylated epitopes, supporting the development and quality control of research-grade immunoreagents.
Functional assays in cytoskeletal studies: The phosphorylated MARCKS peptide is instrumental in functional assays designed to probe the role of MARCKS in actin filament organization and membrane-cytoskeleton interactions. By introducing the peptide into biochemical or cell-based systems, investigators can assess how phosphorylation influences actin binding, membrane localization, and the overall architecture of the cytoskeleton, thus providing a direct link between post-translational modification and cellular structural dynamics.
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