ELA-21 (human) is a peptide containing hydrophobic, aromatic, and polar residues arranged for helix-associated conformational dynamics. Researchers use it to explore ligand-binding interfaces, folding transitions, and solvent-sensitive structure formation. The sequence supports mapping of functional epitopes. Its length allows high-resolution structural investigation.
CAT No: R2417
CAS No:2245073-05-4
Synonyms/Alias:ELA-21 (human);2245073-05-4;DA-52848;
ELA-21 (human) is a synthetic peptide corresponding to the endogenous human peptide, elafin-derived peptide ELA-21. As a member of the serine protease inhibitor family, ELA-21 is characterized by its ability to modulate proteolytic activity, particularly in the context of inflammation and tissue remodeling. Its structure and sequence are derived from the human elafin protein, which is known for its regulatory role in controlling neutrophil elastase and proteinase 3 activity. Due to its high specificity and defined biochemical properties, ELA-21 serves as a valuable molecular tool in peptide research, protease inhibition studies, and the exploration of innate immune mechanisms.
Protease inhibition studies: ELA-21 is widely used in research focused on understanding the regulation of serine proteases, especially those involved in inflammatory processes. By mimicking the natural inhibitory domain of human elafin, the peptide enables researchers to dissect the molecular interactions between protease inhibitors and their target enzymes. Its application in in vitro assays facilitates the characterization of enzyme kinetics, substrate specificity, and the identification of key binding residues, providing insight into the biological control of proteolytic cascades.
Inflammation and immune response research: The peptide is instrumental in investigating the molecular mechanisms underlying innate immune defense, particularly the modulation of neutrophil-derived proteases during inflammation. By serving as a functional analog of endogenous elafin fragments, ELA-21 allows for the study of protease-mediated tissue damage, cytokine regulation, and the resolution of inflammatory responses. Its use in cellular models supports the elucidation of signaling pathways involved in immune cell recruitment and activation.
Peptide structure-function analysis: ELA-21 offers a robust platform for structure-activity relationship (SAR) studies aimed at understanding how specific amino acid sequences and conformational features contribute to protease inhibition. Researchers employ the peptide in mutagenesis experiments, biophysical assays, and computational modeling to map critical residues and structural motifs essential for biological activity. These insights inform the rational design of next-generation protease inhibitors and therapeutic peptide candidates.
Biomarker discovery and validation: The sequence specificity and functional relevance of ELA-21 make it a suitable reference standard in biomarker research related to tissue injury, inflammation, and protease activity. Analytical laboratories utilize the peptide in mass spectrometry-based assays, immunoassays, and bioanalytical method development to quantify endogenous elafin fragments or monitor proteolytic processing events in biological samples. Its defined properties facilitate assay calibration and the generation of reliable quantitative data.
Peptide synthesis and assay development: ELA-21 serves as a model peptide for optimizing solid-phase peptide synthesis protocols and validating peptide purification techniques. Its use in method development supports the establishment of high-yield, high-fidelity synthesis procedures for serine protease inhibitor peptides. Additionally, the peptide is employed in the development and optimization of biochemical assays, including enzyme inhibition screens and peptide-protein interaction studies, thereby advancing peptide-based research and analytical capabilities.
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