Kallikrein Inhibitor is a synthetic peptide. The synthetic kallikrein inhibitor can attenuate breast cancer cell invasion.
CAT No: R1462
CAS No:97145-43-2
Synonyms/Alias:KKI 5;97145-43-2;KKI-5;Kallikrein Inhibitor;Ac-Pro-phe-arg-ser-val-gln-NH2;1-ACETYL-L-PROLYL-L-PHENYLALANYL-L-ARGINYL-L-SERYL-L-VALYL-L-GLUTAMAMIDE;CHEMBL104915;(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-1-acetylpyrrolidine-2-carbonyl]amino]-3-phenylpropanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]-3-hydroxypropanoyl]amino]-3-methylbutanoyl]amino]pentanediamide;(S)-2-((3S,6S,9S,12S)-1-((S)-1-acetylpyrrolidin-2-yl)-3-benzyl-6-(3-guanidinopropyl)-9-(hydroxymethyl)-12-isopropyl-1,4,7,10-tetraoxo-2,5,8,11-tetraazatridecan-13-amido)pentanediamide;L-Glutamamide, 1-acetyl-L-prolyl-L-phenylalanyl-L-arginyl-L-seryl-L-valyl-;Ac-PFRSVQ-NH2;DTXSID90914102;HY-P0237;BDBM50004609;DB-250260;(S)-2-((3S,6S,9S,12S)-1-((S)-1-acetylpyrrolidin-2-yl)-3-benzyl-6-(3-guanidinopropyl)-9-(hydroxymethyl)-12-isopropyl-1,4,7,10-tetraoxo-2,5,8,11-tetraazatridecanamido)pentanediamide;2-{[13-(1-Acetylpyrrolidin-2-yl)-11-benzyl-8-(3-carbamimidamidopropyl)-1,4,7,10,13-pentahydroxy-5-(hydroxymethyl)-2-(propan-2-yl)-3,6,9,12-tetraazatrideca-3,6,9,12-tetraen-1-ylidene]amino}pentanediimidic acid;2-{2-[2-(2-{2-[(1-Acetyl-pyrrolidine-2-carbonyl)-amino]-3-phenyl-propionylamino}-5-guanidino-pentanoylamino)-3-hydroxy-propionylamino]-3-methyl-butyrylamino}-pentanedioic acid diamide;L-glutamamide, 1-acetyl-L-prolyl-L-phenylalanyl-N5-(diaminomethylene)-L-ornithyl-L-seryl-L-valyl-;
Chemical Name:(S)-2-((3S,6S,9S,12S)-1-((S)-1-acetylpyrrolidin-2-yl)-3-benzyl-6-(3-guanidinopropyl)-9-(hydroxymethyl)-12-isopropyl-1,4,7,10-tetraoxo-2,5,8,11-tetraazatridecan-13-amido)pentanediamide
Kallikrein Inhibitor is a specialized biochemical compound designed to modulate the activity of kallikrein enzymes, which are serine proteases involved in the regulation of key physiological processes such as blood coagulation, inflammation, and the kallikrein-kinin system. As a potent modulator of proteolytic cascades, this inhibitor serves as a valuable research tool for dissecting the functional roles of kallikreins in various biological contexts. Its ability to selectively block kallikrein activity enables researchers to investigate complex signaling pathways, elucidate enzyme-substrate relationships, and explore the broader implications of protease regulation in health and disease. The compound's specificity and functional relevance make it an indispensable reagent for biochemical, cellular, and molecular studies targeting protease-mediated mechanisms.
Enzyme Mechanism Studies: Kallikrein inhibitors are widely employed in biochemical research to probe the catalytic mechanisms of serine proteases, particularly those in the kallikrein family. By selectively suppressing enzyme activity, they allow for the detailed characterization of active sites, substrate specificity, and kinetic parameters. Researchers utilize these inhibitors to map proteolytic cleavage events, determine enzyme-substrate affinities, and validate hypotheses regarding catalytic residues. Such mechanistic insights are instrumental for advancing the understanding of protease function and regulation in both physiological and pathological settings.
Signal Transduction Research: The kallikrein-kinin system plays a pivotal role in mediating signal transduction pathways related to vascular tone, inflammation, and cellular communication. Inhibition of kallikrein activity enables the dissection of downstream signaling events, such as bradykinin generation and receptor activation. Scientists leverage kallikrein inhibitors to study the modulation of intracellular signaling cascades, analyze cross-talk between proteolytic and receptor-mediated pathways, and elucidate the molecular determinants of inflammatory responses. This application is particularly valuable for unraveling the complex interplay between proteases and cellular signaling networks.
Protease Inhibitor Screening: In drug discovery and biochemical assay development, kallikrein inhibitors serve as essential reference compounds or positive controls for high-throughput screening platforms. Their well-characterized inhibitory profiles facilitate the benchmarking of novel small molecules, peptides, or biologics targeting serine proteases. By providing a reliable standard, these inhibitors help validate assay performance, optimize screening conditions, and ensure reproducibility in the identification of new protease modulators. This approach is critical for the early-stage evaluation of candidate compounds in pharmaceutical and academic research settings.
Pathway Elucidation: Understanding the broader biological consequences of protease inhibition requires precise experimental controls. Kallikrein inhibitors are utilized to delineate the contribution of kallikrein-mediated proteolysis within complex biological systems, including plasma, tissue extracts, or cell culture models. By selectively blocking kallikrein activity, researchers can attribute observed phenotypic or biochemical changes to specific proteolytic events, thereby clarifying the functional roles of these enzymes in diverse physiological and experimental contexts. This strategy is fundamental for constructing accurate models of protease-driven pathways and for identifying potential regulatory nodes.
Analytical Biochemistry: In analytical workflows, kallikrein inhibitors are incorporated to preserve sample integrity during the preparation and analysis of biological specimens. Proteolytic degradation by endogenous enzymes can compromise the quantification of sensitive analytes, such as peptides, proteins, or metabolites. The inclusion of specific inhibitors minimizes unwanted protease activity, ensuring accurate measurement and reproducibility in downstream analytical techniques, including mass spectrometry, immunoassays, and enzymatic profiling. This application supports high-quality data acquisition and is essential for rigorous biochemical and molecular analyses.
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