Selective and cell-permeable antagonist of formyl peptide receptor 2 (FPR2), which selectively inhibits fpr2-mediated nadph oxidase activity, but has no effect on fpr1 signaling in neutrophils.
CAT No: R0987
CAS No:794466-43-6
Synonyms/Alias:PBP 10;794466-43-6;PBP10;AKOS024458252;PD079723;Unk-Gln-Arg-Leu-Phe-Gln-Val-Lys-Gly-Arg-Orn(Unk)-OH;
PBP 10 is a synthetic peptide derived from a segment of the phosphoinositide-binding domain of gelsolin, a multifunctional actin-binding protein. As a research peptide, PBP 10 is recognized for its ability to interact with phosphoinositides, particularly phosphatidylinositol 4,5-bisphosphate (PIP2), and modulate cytoskeletal dynamics. Its sequence is engineered to mimic the natural binding interface, making it a valuable molecular tool in studies of membrane-protein interactions, signal transduction, and cellular motility. The unique biochemical properties of PBP 10 have positioned it as an important reagent for probing the regulation of actin assembly and the functional consequences of phosphoinositide signaling in various biological systems.
Signal Transduction Research: PBP 10 is widely utilized to investigate the mechanisms of phosphoinositide-mediated signal transduction. By selectively binding to PIP2 and related phosphoinositides, the peptide serves as a molecular probe to dissect the spatial and temporal dynamics of lipid signaling within the cell. Researchers use it to map the distribution of key signaling lipids, monitor their interactions with cytoskeletal proteins, and elucidate pathways that govern cellular responses to extracellular stimuli. Its specificity enables detailed analysis of how phosphoinositide signaling orchestrates processes such as cell migration, endocytosis, and exocytosis.
Actin Cytoskeleton Studies: The peptide's affinity for PIP2 makes it an effective modulator of actin filament organization. In vitro and cell-based assays, PBP 10 is employed to perturb the association between phosphoinositides and actin-binding proteins, thereby influencing actin polymerization and network formation. This application is particularly valuable for understanding the molecular underpinnings of cytoskeletal remodeling, cell shape changes, and motility. By introducing the peptide into experimental systems, scientists can delineate the contributions of specific lipid-protein interactions to actin dynamics and cellular architecture.
Membrane Dynamics and Trafficking: PBP 10 is a key reagent for probing membrane-related events such as vesicle trafficking, membrane ruffling, and organelle positioning. Its ability to bind and sequester phosphoinositides allows researchers to manipulate the availability of these lipids at the membrane, thereby affecting processes dependent on localized lipid signaling. Experimental use of the peptide helps clarify the roles of phosphoinositides in membrane curvature generation, vesicle budding, and the coordination of intracellular transport pathways.
Peptide-Protein Interaction Analysis: As a synthetic peptide model, PBP 10 is instrumental in studying the structural and functional aspects of peptide-protein and peptide-lipid interactions. It serves as a template for biophysical assays, including surface plasmon resonance, fluorescence resonance energy transfer, and nuclear magnetic resonance spectroscopy. These studies provide quantitative insights into binding affinities, kinetics, and conformational changes associated with phosphoinositide recognition, supporting the rational design of novel modulators or inhibitors targeting lipid-protein interfaces.
Peptide-Based Assay Development: PBP 10 is also applied in the development of biochemical and cell-based assays that require precise manipulation of phosphoinositide signaling. Its defined sequence and binding characteristics make it suitable for use as a positive control, competitive inhibitor, or functional reporter in assays measuring lipid-protein interactions, actin dynamics, or membrane-associated enzymatic activities. This application is essential for validating experimental platforms, screening small molecules, and characterizing the specificity of lipid-binding domains in a controlled research setting.
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