Epsilon-V1-2 is a peptidic inhibitor fragment containing diverse residues that support structured folding and ligand-recognition motifs. Researchers use it to examine residue-driven conformational changes, hydrophobic pairing, and protein-interface mapping. The sequence's polarity variations aid biophysical profiling. Its modular design supports mechanistic studies.
CAT No: R2266
CAS No:182683-50-7
Synonyms/Alias:Epsilon-V1-2;182683-50-7;L-alpha-Glutamyl-L-alanyl-L-valyl-L-seryl-L-leucyl-L-lysyl-L-prolyl-L-threonine;(4S)-4-amino-5-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-6-amino-1-[(2S)-2-[[(1S,2R)-1-carboxy-2-hydroxypropyl]carbamoyl]pyrrolidin-1-yl]-1-oxohexan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-1-oxopropan-2-yl]amino]-5-oxopentanoic acid;CHEMBL3261358;Epsilon-V1-2?;HY-P0154;BDBM50012948;AKOS040754861;DA-63243;MS-31563;CS-0019940;G12953;
Epsilon-V1-2 is a synthetic peptide compound characterized by a unique amino acid sequence that enables selective molecular interactions within biological systems. As a research-grade peptide, it is engineered to facilitate the exploration of protein-protein interactions, receptor binding mechanisms, and cellular signaling pathways. Its defined structure and functional groups provide an essential tool for investigating the roles of specific peptide motifs in various biochemical and molecular biology contexts. The compound's versatility and precision make it particularly valuable for studies requiring high specificity and reproducibility in peptide-mediated processes.
Peptide-Protein Interaction Studies: Epsilon-V1-2 is frequently employed in research focused on elucidating the dynamics of peptide-protein interactions. By serving as a model ligand or competitive inhibitor, it allows investigators to probe the binding affinities and specificity of target proteins, such as receptors, enzymes, or scaffolding molecules. These studies are instrumental in mapping interaction domains, characterizing binding kinetics, and understanding the structural basis of molecular recognition events in both in vitro and cell-based assay systems.
Signal Transduction Research: The peptide's defined sequence can be leveraged to interrogate intracellular signaling cascades. Researchers utilize Epsilon-V1-2 to modulate or mimic endogenous signaling motifs, enabling the dissection of downstream effects in pathways such as kinase activation, G protein-coupled receptor signaling, or adaptor protein recruitment. Through such applications, the compound aids in identifying critical nodes within signaling networks and in validating the functional relevance of specific peptide sequences to cellular communication processes.
Peptide-Based Functional Assays: Epsilon-V1-2 is suitable for use in a variety of functional assays designed to measure cellular responses to peptide-mediated stimuli. In these contexts, it can act as a substrate, agonist, or antagonist, depending on the experimental design. Its application in cell-based assays, biochemical reconstitution experiments, or high-throughput screening platforms enables precise quantification of activity changes, facilitating the identification of modulators or effectors associated with the peptide's target pathway.
Structural and Biophysical Characterization: The compound's well-defined structure makes it an excellent candidate for structural biology investigations, including nuclear magnetic resonance (NMR) spectroscopy, X-ray crystallography, and circular dichroism (CD) analysis. Researchers utilize Epsilon-V1-2 to determine conformational preferences, secondary structure elements, and interaction interfaces with target proteins or membranes. These studies provide critical insights into the molecular determinants of peptide function and stability, supporting rational design strategies for related research applications.
Peptide Synthesis and Modification Studies: As a synthetic peptide, Epsilon-V1-2 serves as a reference standard or starting material for the development of novel peptide analogs and derivatives. Its sequence can be modified through site-directed mutagenesis, incorporation of non-natural amino acids, or conjugation with functional moieties, enabling structure-activity relationship (SAR) studies and the creation of tailored research tools. Such applications are fundamental to advancing peptide engineering efforts and optimizing bioactive properties for diverse experimental objectives.
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