CALP3 is a cell-permeable calmodulin (CaM) agonist that binds to the EF-hand/Ca2+-binding site. Activates phosphodiesterase in the absence of Ca2+ and inhibits Ca2+-mediated cytotoxicity and apoptosis (IC50 = 33 μM).
CAT No: 10-101-306
CAS No:261969-05-5
Synonyms/Alias:CALP3;261969-05-5;(2S)-6-amino-2-[[(2S)-2-[[2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-amino-3-methylbutanoyl]amino]hexanoyl]amino]-3-phenylpropanoyl]amino]acetyl]amino]-3-methylbutanoyl]amino]acetyl]amino]-3-phenylpropanoyl]amino]hexanoic acid;VKFGVGFK;CALP3 TFA;CALP-3;HY-P1075;AKOS024457051;DA-71886;FC110060;MS-31632;Calcium-Like Peptide 3 trifluoroacetate salt;CS-0027558;G13351;H-Val-Lys-Phe-Gly-Val-Gly-Phe-Lys-OH; H-VKFGVGFK-OH;
Chemical Name:(2S)-6-amino-2-[[(2S)-2-[[2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-amino-3-methylbutanoyl]amino]hexanoyl]amino]-3-phenylpropanoyl]amino]acetyl]amino]-3-methylbutanoyl]amino]acetyl]amino]-3-phenylpropanoyl]amino]hexanoic acid
CALP3 is a synthetic peptide compound designed to emulate or modulate specific protein-protein interactions within cellular signaling pathways. As a peptide-based reagent, CALP3 is characterized by its defined amino acid sequence, which enables selective binding or interference with target proteins. Its biochemical properties make it highly relevant for research focused on elucidating molecular mechanisms of cellular regulation, particularly in contexts where peptide-mediated modulation of signaling events is of interest. The compound's structural specificity and functional mimicry position it as a valuable tool for probing the roles of endogenous peptides and their interacting partners in diverse biological systems.
Signal Transduction Research: CALP3 is widely utilized in studies investigating the molecular underpinnings of intracellular signaling cascades. By mimicking or disrupting native peptide motifs, it facilitates the dissection of signaling pathways, allowing researchers to delineate the contributions of specific protein domains or interaction sites. Its application is especially pertinent in experiments aimed at understanding how transient peptide-protein interactions govern the transmission of signals from membrane receptors to downstream effectors, thereby providing insights into the dynamic regulation of cellular responses.
Protein-Protein Interaction Studies: The defined sequence of CALP3 enables its use as a probe in mapping interaction networks between proteins. In vitro binding assays, co-immunoprecipitation experiments, and surface plasmon resonance analyses often employ such synthetic peptides to quantify binding affinities and identify critical contact residues. By serving as a competitive inhibitor or molecular mimic, this peptide assists in validating the specificity and functional relevance of protein-protein contacts, supporting the development of models for complex assembly and regulation.
Peptide-Based Assay Development: CALP3 is frequently incorporated into custom assay platforms designed to monitor enzyme activity, receptor engagement, or post-translational modifications. Its sequence can be tailored to include recognition sites for kinases, phosphatases, or proteases, enabling the creation of sensitive and selective assays for high-throughput screening or mechanistic studies. The utility of this peptide in assay development extends to the optimization of detection protocols and the calibration of analytical instruments, ensuring robust and reproducible measurement of biochemical activities.
Structural Biology Applications: The use of CALP3 in structural biology is instrumental for elucidating conformational changes associated with peptide binding. Crystallographic studies, NMR spectroscopy, and molecular modeling approaches benefit from the availability of well-defined synthetic peptides, which can stabilize transient complexes or highlight dynamic regions within target proteins. Such applications are essential for mapping interaction interfaces, guiding mutagenesis experiments, and informing the rational design of peptide-based modulators.
Peptide Therapeutic Research: Although not intended for clinical or therapeutic use, CALP3 serves as a research tool in the early stages of peptide therapeutic development. Its role includes enabling the assessment of peptide stability, bioavailability, and target engagement in preclinical models. By providing a platform for structure-activity relationship studies, it contributes to the identification and optimization of lead compounds with desirable pharmacological profiles, ultimately supporting the advancement of peptide-based strategies in drug discovery pipelines.
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