ALX 40-4C is a small peptide inhibitor of the chemokine receptor CXCR4, inhibits SDF-1 from binding CXCR4 with a Ki of 1 μM, and suppresses the replication of X4 strains of HIV-1; ALX 40-4C Trifluoroacetate also acts as an antagonist of the APJ receptor, with an IC50 of 2.9 μM.
CAT No: R1182
CAS No:143413-49-4
Synonyms/Alias:9025-49-4;Aspergillus acid protease;RUWHAENIXFIHPU-UHFFFAOYSA-N;DA-50747;143413-49-4;
ALX 40-4C is a synthetic peptide compound widely recognized for its role as a CXCR4 antagonist in biochemical and cell signaling research. Structurally, it is derived from a series of rationally designed peptides that specifically target the CXC chemokine receptor 4 (CXCR4), a G-protein-coupled receptor implicated in diverse physiological and pathological processes. By competitively inhibiting the interaction between CXCR4 and its natural ligand, stromal cell-derived factor-1 (SDF-1 or CXCL12), ALX 40-4C enables researchers to dissect the molecular mechanisms underlying chemokine-mediated signaling pathways. Its high specificity and affinity for CXCR4 make it a valuable tool for investigating receptor-ligand interactions, cellular migration, and downstream signal transduction events in various experimental systems.
Receptor pharmacology: ALX 40-4C is extensively utilized in studies focused on CXCR4 receptor pharmacology. By acting as a selective antagonist, it allows for the characterization of CXCR4-mediated signaling cascades and helps delineate receptor function in response to chemokine stimulation. Researchers employ this peptide to block SDF-1 binding, thereby enabling precise evaluation of receptor activation, desensitization, and downstream effects in cell-based assays. Its application is instrumental for elucidating the specificity and dynamics of chemokine receptor interactions in both primary cells and established cell lines.
Cell migration and chemotaxis assays: The peptide serves as a critical reagent in cell migration and chemotaxis studies, particularly in the context of leukocyte trafficking, stem cell homing, and cancer cell invasion. By inhibiting the CXCR4/CXCL12 axis, ALX 40-4C allows investigators to assess the contribution of this pathway to directed cell movement under physiological and experimental conditions. Its use facilitates the development of robust in vitro and ex vivo models that simulate tissue-specific migration, offering insights into the regulatory mechanisms governing cellular localization and microenvironmental responses.
Signal transduction research: ALX 40-4C is applied in the investigation of intracellular signaling events downstream of CXCR4 engagement. Researchers utilize the compound to interrupt receptor-mediated activation of pathways such as MAPK/ERK, PI3K/AKT, and other G-protein-dependent cascades. By providing a means to selectively block CXCR4, the peptide enables detailed analysis of how chemokine receptor signaling influences gene expression, cell survival, proliferation, and differentiation in various biological contexts.
Peptide-based screening and assay development: The specificity and reproducibility of ALX 40-4C make it a preferred standard in the development and optimization of high-throughput screening assays targeting chemokine receptors. Its use as a reference antagonist supports the validation of assay systems designed to identify novel modulators of CXCR4 activity. Additionally, the peptide aids in benchmarking assay sensitivity and selectivity, ensuring reliable detection of functional receptor antagonism in drug discovery and basic research applications.
Functional studies in immunology and oncology: The ability of ALX 40-4C to modulate CXCR4 signaling has established it as a valuable tool in studies exploring immune cell dynamics and tumor biology. In immunological research, the peptide is used to investigate the regulation of lymphocyte trafficking, tissue retention, and immune surveillance. In oncology, it supports mechanistic studies of tumor cell migration, metastasis, and microenvironmental interactions driven by the CXCR4/CXCL12 axis. Its application provides critical insights into the molecular basis of immune and cancer cell behavior, informing the design of experimental models and the interpretation of chemokine-driven processes.
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