Fap-IN-2 features a peptide-based framework designed to investigate conformational determinants and binding equilibria. Hydrophobic and polar residues govern solubility and folding patterns. Researchers evaluate its stability and structural transitions. Applications include ligand modeling, peptide optimization, and structural biology.
CAT No: R2488
CAS No:2471983-20-5
Synonyms/Alias:FAP-IN-2;2471983-20-5;(S)-N-(2-(2-Cyano-4,4-difluoropyrrolidin-1-yl)-2-oxoethyl)-6-(3-(piperazin-1-yl)propoxy)quinoline-4-carboxamide;SCHEMBL23754367;EX-A11457;FC183427;HY-47979;CS-0617809;(S)-N-(2-(2-Cyano-4,4-difluoropyrrolidin-1-yl)-2-oxoethyl)-6-(3-(piperazine-1-yl)propoxy)quinoline-4-carboxamide;N-[2-[(2S)-2-cyano-4,4-difluoropyrrolidin-1-yl]-2-oxoethyl]-6-(3-piperazin-1-ylpropoxy)quinoline-4-carboxamide;
Fap-IN-2 is a specialized carbohydrate compound designed for advanced research applications in the field of glycobiology and enzymology. Characterized by its unique molecular structure, Fap-IN-2 is recognized for its high specificity and ability to interact with fibroblast activation protein (FAP), a serine protease implicated in diverse physiological and pathological processes. The compound serves as a valuable tool for scientists exploring the intricate mechanisms of carbohydrate-protein interactions, signal transduction pathways, and the modulation of extracellular matrix components. Its chemical stability and compatibility with a wide range of biological assays make it a preferred choice for laboratories seeking reliable and reproducible results in experimental settings.
Enzyme Inhibition Studies: Fap-IN-2 is extensively utilized in enzyme inhibition assays to probe the functional dynamics of fibroblast activation protein. By acting as a selective inhibitor, it allows researchers to dissect the enzymatic activity of FAP in vitro, facilitating the identification of substrate preferences and catalytic mechanisms. This application is crucial for elucidating the role of FAP in tissue remodeling and fibrotic processes, as well as for the validation of potential therapeutic targets in preclinical research. The compound's specificity enables the differentiation between FAP and closely related proteases, supporting the development of highly selective inhibitors for downstream applications.
Cancer Biology Research: In the context of cancer biology, Fap-IN-2 serves as a powerful investigative tool for understanding the involvement of FAP in tumor microenvironment modulation. Researchers employ this compound to study how FAP-mediated proteolysis contributes to tumor progression, angiogenesis, and immune cell infiltration. By selectively inhibiting FAP activity, scientists can assess changes in cellular behavior, extracellular matrix degradation, and signal transduction pathways associated with malignancy. These insights are instrumental in identifying novel intervention points for cancer therapy and in evaluating the efficacy of combination treatments in experimental models.
Fibrosis and Tissue Remodeling: Fap-IN-2 is also applied in studies focused on fibrosis and tissue remodeling, where FAP plays a pivotal role in the regulation of extracellular matrix turnover. The compound's inhibitory properties enable the assessment of FAP's contribution to collagen degradation, fibroblast activation, and scar tissue formation. Researchers utilize it to delineate the molecular events underlying fibrotic diseases and to screen candidate molecules that may attenuate pathological tissue remodeling. This application is particularly relevant for the investigation of chronic inflammatory conditions and the development of anti-fibrotic strategies in basic research settings.
Biomarker Discovery: The use of Fap-IN-2 extends to biomarker discovery, where it aids in the identification and validation of FAP-related molecular signatures in various biological samples. By modulating FAP activity in controlled experiments, scientists can correlate specific biochemical changes with disease states, tissue injury, or regenerative processes. This approach supports the development of diagnostic assays and the refinement of prognostic indicators based on FAP expression and activity profiles. The compound's reliability and reproducibility in experimental workflows enhance the robustness of biomarker studies and facilitate the translation of findings to broader research applications.
High-Throughput Screening: In pharmaceutical and academic laboratories, Fap-IN-2 is integrated into high-throughput screening platforms to evaluate the potency and selectivity of novel FAP inhibitors. Its use in automated assay systems accelerates the identification of lead compounds with desirable pharmacological properties, streamlining the early stages of drug discovery. The compound's compatibility with diverse assay formats, including fluorescence-based and colorimetric readouts, ensures its versatility in screening campaigns. As a result, Fap-IN-2 contributes significantly to the advancement of chemical biology and the discovery of next-generation modulators targeting fibroblast activation protein.
Glycobiology Research: Beyond its role in enzyme inhibition and disease modeling, Fap-IN-2 is valuable for fundamental glycobiology research. Scientists employ it to investigate the structural and functional aspects of carbohydrate-protein interactions, shedding light on the molecular basis of cell signaling, adhesion, and migration. The compound's defined structure and inhibitory activity make it an ideal probe for dissecting the complex interplay between glycans and proteases in physiological and pathological contexts. By enabling precise manipulation of FAP activity, Fap-IN-2 supports a deeper understanding of glycan-mediated regulatory networks and their implications in health and disease.
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