CEF4 is a peptide that corresponds to aa 342-351 of the influenza A virus nucleocapsid protein.
CEF4, also known as C-C motif chemokine ligand 18 (CCL18) derived peptide, is a synthetic peptide compound designed for research applications in immunology, cell signaling, and chemokine biology. As a functional fragment or analog related to the chemokine family, it is valued for its role in mimicking or modulating the activity of endogenous chemokines, which are critical regulators of immune cell trafficking and inflammatory responses. The peptide's biochemical properties enable precise interrogation of chemokine-mediated pathways, making it a valuable tool for researchers investigating mechanisms of immune communication, cellular migration, and signal transduction. Its defined sequence and controlled synthesis support reproducible studies in a variety of experimental contexts, from basic cell biology to advanced translational research.
Immunology research: In the field of immunology, CEF4-related peptides are frequently utilized to dissect the molecular mechanisms underlying chemokine signaling and leukocyte recruitment. By serving as a functional ligand for specific chemokine receptors, the peptide enables detailed study of receptor-ligand interactions, downstream signaling cascades, and the regulation of immune cell migration. Such investigations are fundamental to understanding the orchestration of immune responses in both physiological and pathological settings, including inflammation, infection, and tissue homeostasis.
Cell migration assays: CEF4 peptide is widely employed in in vitro and ex vivo cell migration and chemotaxis assays. Researchers use it to stimulate or inhibit the directed movement of immune cells, such as monocytes, T cells, and dendritic cells, across biological barriers or within tissue models. These assays help elucidate the molecular cues that govern cell trafficking, providing insights into processes such as immune surveillance, tissue repair, and the development of inflammatory microenvironments.
Receptor profiling: The peptide is instrumental in receptor binding studies, facilitating the characterization of chemokine receptor specificity and affinity. By using labeled or modified forms of the peptide, scientists can map receptor expression patterns on different cell types, quantify binding kinetics, and identify novel receptor-ligand interactions. Such profiling is essential for unraveling the complexity of chemokine networks and for the validation of new targets in immunological research.
Peptide structure-function analysis: CEF4 peptide serves as a model system for structure-activity relationship (SAR) studies within the chemokine family. Researchers employ it to investigate how specific amino acid substitutions or modifications affect biological activity, receptor engagement, and downstream signaling. These structure-function analyses inform the rational design of peptide-based modulators or inhibitors, advancing the development of research tools for probing chemokine function and regulation.
Peptide synthesis validation: As a well-characterized chemokine-derived peptide, CEF4 is also used as a reference compound in peptide synthesis and analytical method validation. Laboratories utilize it to optimize solid-phase peptide synthesis protocols, assess chromatographic separation techniques, and calibrate mass spectrometry instruments. Its defined sequence and predictable behavior make it an ideal standard for ensuring the accuracy and reproducibility of peptide production workflows, supporting broader research and development efforts in peptide chemistry and analytical biochemistry.
1. Emu oil in combination with other active ingredients for treating skin imperfections
2. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists
3. Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes
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