Receptor for advanced glycation end products (RAGE) antagonist. Blocks S100P, S100A4 and HMGB-1 mediated RAGE activation in vitro and in vivo. Inhibits growth and metastasis of rat glioma tumors. Reduces cell growth and RAGE-mediated NF-κB activity in human PDAC cell lines. Inhibits effects of TDI exposure in BALB/c mice.
CAT No: R0852
CAS No:1092460-91-7
Synonyms/Alias:RAGE antagonist peptide;1092460-91-7;RAGE antagonist peptide TFA;AKOS032947195;AS-85200;PD080324;
RAGE antagonist peptide is a synthetic peptide compound designed to selectively inhibit the activity of the Receptor for Advanced Glycation End-products (RAGE), a cell surface receptor implicated in a wide range of physiological and pathological processes. As a peptide-based inhibitor, it offers a targeted approach for modulating RAGE-mediated signaling pathways, which are known to play crucial roles in cellular stress responses, inflammation, and metabolic regulation. The unique sequence and structure of this peptide enable it to interact specifically with the ligand-binding domain of RAGE, thereby preventing the downstream activation of signaling cascades associated with this receptor. Its use in research settings has become increasingly significant for elucidating the molecular mechanisms underlying RAGE-related pathways and for developing new experimental models of cellular dysfunction.
Signal transduction research: The peptide serves as a valuable molecular tool for dissecting RAGE-dependent signaling mechanisms in vitro and in cell-based assays. By competitively inhibiting ligand binding to RAGE, it allows researchers to selectively block the activation of downstream effectors, such as NF-κB and MAP kinases, which are central to inflammatory and stress response pathways. This targeted inhibition enables the study of RAGE's specific contributions to cellular signaling networks, facilitating the identification of key regulatory nodes and potential intervention points within these pathways.
Inflammation studies: Due to its capacity to inhibit RAGE-ligand interactions, the antagonist peptide is extensively used in experimental models investigating the biochemical basis of inflammation. RAGE is recognized for its involvement in amplifying inflammatory responses through the recognition of diverse ligands, including advanced glycation end-products, S100 proteins, and HMGB1. Application of the peptide in cell culture or ex vivo tissue systems permits the assessment of how RAGE blockade modulates cytokine production, adhesion molecule expression, and other pro-inflammatory mediators, thereby providing mechanistic insights into the receptor's role in inflammatory cascades.
Oxidative stress investigation: The RAGE pathway is closely linked to the generation of reactive oxygen species and the perpetuation of oxidative stress in various cell types. Utilizing the antagonist peptide in biochemical assays or cellular models allows researchers to evaluate the impact of RAGE inhibition on oxidative stress markers, antioxidant defense mechanisms, and redox-sensitive signaling events. Such studies are instrumental for understanding the interplay between RAGE activity and cellular oxidative homeostasis, supporting the development of new strategies for mitigating oxidative damage in research contexts.
Peptide-protein interaction analysis: As a well-characterized inhibitor, the peptide is frequently employed in studies focused on characterizing the molecular determinants of RAGE-ligand binding. By serving as a competitive antagonist, it enables detailed mapping of the receptor's ligand-binding interface and the identification of critical residues involved in high-affinity interactions. These analyses are essential for guiding rational design of next-generation RAGE inhibitors and for advancing structural biology research related to peptide-receptor recognition.
Peptide-based assay development: The antagonist peptide is also utilized in the development and validation of novel biochemical and cell-based assays for screening RAGE modulators. Its defined inhibitory activity provides a reliable reference for benchmarking assay sensitivity and specificity, as well as for calibrating experimental conditions. Incorporation of the peptide into assay platforms supports high-throughput screening efforts and the quantitative assessment of candidate compounds, thereby accelerating discovery workflows in the context of RAGE-targeted research.
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