An antagonist of 14.3.3 proteins (KD ≈80 nM) that induces apoptosis. Competitively inhibits 14-3-3-ligand interactions without requiring phosphorylation, thereby blocks the ability of 14-3-3 binding to target proteins such as Raf-1, Bad, ASK1 and exoenzyme S.
CAT No: R1015
CAS No:211364-78-2
Synonyms/Alias:R18 peptide;211364-78-2;CHEMBL3814675;R18 TFA;BDBM50177028;DA-67086;
R18 is a synthetic peptide derived from the amino acid sequence of the Kunitz-type protease inhibitor domain, widely recognized for its role in modulating protein-protein interactions and influencing various cellular signaling pathways. As a research-grade peptide, R18 offers a precise tool for investigating the molecular mechanisms underlying protease inhibition and cell regulation. Its unique sequence and structural properties have made it a valuable asset in the study of neuroprotection, cellular signaling, and peptide-receptor interactions, supporting a range of advanced experimental designs in biochemistry and molecular biology.
Neuroprotection research: R18 is frequently employed in experimental models to examine its capacity to shield neural cells from excitotoxic and oxidative stress-induced damage. Researchers utilize this peptide to dissect the pathways involved in neuronal survival and death, particularly focusing on the inhibition of protease-mediated cell injury. By serving as a modulator of protease activity, it enables the exploration of neuroprotective strategies and the identification of molecular targets that may mitigate neurodegenerative processes in vitro or in ex vivo systems.
Cell signaling studies: The peptide is a powerful tool for elucidating the mechanisms of cellular communication, particularly those involving serine proteases and their downstream signaling cascades. Its ability to interact with specific protease targets allows investigators to probe the modulation of intracellular pathways, such as those regulating apoptosis, inflammation, and synaptic plasticity. Through controlled application in cell-based assays, R18 facilitates the mapping of complex signaling networks and the assessment of peptide-mediated regulatory effects.
Protein interaction analysis: Due to its defined sequence and affinity for protease domains, R18 is well-suited for use in protein-protein interaction studies. It can be incorporated into binding assays, co-immunoprecipitation experiments, and surface plasmon resonance analyses to quantify and characterize interactions between protease inhibitors and their enzyme counterparts. Such applications provide critical insights into the structural determinants of binding specificity and the dynamics of inhibitor-enzyme complexes.
Peptide structure-function relationship investigations: R18 serves as a model system for examining the relationship between peptide sequence, three-dimensional conformation, and biological activity. By subjecting it to mutagenesis, truncation, or labeling, researchers can systematically assess how structural modifications influence its inhibitory properties and functional efficacy. These studies inform the rational design of novel peptides with tailored bioactivity for research purposes.
Peptide synthesis and methodological validation: The reliable synthesis and characterization of R18 make it an ideal standard for validating peptide synthesis protocols and analytical techniques. Laboratories frequently use this peptide to optimize purification strategies, assess chromatographic performance, and calibrate mass spectrometry instrumentation. Its well-characterized nature ensures reproducibility and consistency in method development, supporting quality assurance in peptide chemistry workflows.
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