Chemerin-9 (149-157), the nonapeptide (149)YFPGQFAFS(157) (chemerin-9), corresponding to the C terminus of processed chemerin, retains most of the activity of the full-size protein, with regard to agonism toward the chemerinR.
CAT No: R1289
CAS No:676367-27-4
Synonyms/Alias:chemerin C-terminal peptide;676367-27-4;Chemerin-9 (149-157);chemerin-9;chemerin 149-157;CHEMBL5081975;(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-5-amino-2-[[2-[[(2S)-1-[(2S)-2-[[(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]-3-phenylpropanoyl]pyrrolidine-2-carbonyl]amino]acetyl]amino]-5-oxopentanoyl]amino]-3-phenylpropanoyl]amino]propanoyl]amino]-3-phenylpropanoyl]amino]-3-hydroxypropanoic acid;chemerin 9;Chemerin-9 (human);bioactive chemerin peptide;GTPL3422;SCHEMBL26342858;BCB36727;HY-P1844;BDBM50581650;DA-62262;CS-0096567;
Chemerin-9 149-157 is a synthetic peptide fragment derived from the C-terminal region of the human chemerin protein, specifically encompassing amino acids 149 to 157. As a bioactive peptide, it represents the minimal sequence required for high-affinity activation of chemerin receptors, such as ChemR23 (CMKLR1). Its selective receptor agonism and stability make it a valuable tool for probing chemerin-mediated signaling pathways. Researchers utilize this peptide to dissect the physiological and biochemical roles of chemerin, particularly in the context of immune modulation, adipogenesis, and inflammatory responses. The precise sequence and defined activity of Chemerin-9 149-157 enable targeted investigation of chemerin receptor functions in diverse experimental systems.
Receptor Activation Studies: Chemerin-9 149-157 is widely employed in receptor pharmacology to study the activation and downstream signaling of the ChemR23 receptor. Its high specificity and potency as a ChemR23 agonist allow researchers to delineate ligand-receptor interactions, characterize G protein-coupled receptor (GPCR) signaling cascades, and quantify receptor responsiveness in cellular and molecular assays. By applying this peptide to receptor-expressing cell lines or primary cells, investigators can map signaling events and evaluate receptor selectivity without interference from full-length chemerin or other endogenous ligands.
Inflammation and Immunomodulation Research: The peptide serves as a powerful probe for investigating the role of chemerin signaling in immune cell recruitment, migration, and activation. It is used in in vitro and ex vivo models to assess how chemerin-derived peptides modulate the chemotaxis of macrophages, dendritic cells, and natural killer cells. These studies facilitate a deeper understanding of the molecular mechanisms underlying inflammatory processes and immune surveillance, offering insights into the regulation of leukocyte trafficking and the resolution of inflammation at the cellular level.
Adipocyte Biology and Metabolic Studies: Chemerin-9 149-157 is instrumental in exploring the influence of chemerin signaling on adipogenesis and metabolic regulation. Researchers employ the peptide to examine its effects on preadipocyte differentiation, lipid accumulation, and metabolic gene expression in adipose tissue models. Such studies help clarify the contribution of chemerin and its receptor to energy homeostasis, adipose tissue remodeling, and metabolic syndrome-related pathways, providing a mechanistic basis for further investigation of adipokine signaling.
Peptide Structure-Activity Relationship (SAR) Analysis: As a well-characterized minimal active sequence, Chemerin-9 149-157 is frequently utilized in SAR studies to identify key residues responsible for receptor binding and activation. Systematic substitution or truncation of amino acids within the peptide enables researchers to map structural determinants of bioactivity and optimize peptide analogs for enhanced potency, selectivity, or stability. These investigations are crucial for the rational design of novel peptide-based probes or modulators targeting chemerin receptors.
Analytical and Quantitative Assays: The defined sequence and receptor specificity of this peptide make it suitable as a standard or positive control in various biochemical and analytical assays. It is used to calibrate receptor binding assays, monitor peptide-receptor interactions via fluorescence or radioligand techniques, and validate the performance of ligand detection platforms. Employing Chemerin-9 149-157 in these contexts ensures reproducibility and reliability in quantitative analyses of chemerin receptor activity, supporting robust experimental design in peptide research and receptor pharmacology.
3. Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes
5. Cationic cell-penetrating peptides are potent furin inhibitors
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