Hexa-D-arginine (Furin Inhibitor II) is a stable furin inhibitor with Ki values 106 nM, 580 nM and 13.2 μM for furin, PACE4 and prohormone convertase-1 (PC1), respectively. Hexa-D-arginine blocks Pseudomonas exotoxin A and anthrax toxins toxicity in vitro and in vivo.
CAT No: R1834
CAS No:673202-67-0
Synonyms/Alias:Hexa-D-arginine;673202-67-0;Furin Inhibitor II;D-Argininamide D-arginyl-D-arginyl-D-arginyl-D-arginyl-D-arginyl-D-alanine;Furin Inhibitor II trifluoroacetate salt;D-Argininamide, D-arginyl-D-arginyl-D-arginyl-D-arginyl-D-arginyl-;hexa-D-arginine amide;SCHEMBL19267519;DTXSID90724127;CHEBI:231111;HY-P1028;AKOS024458307;Furin Inhibitor II(Hexa-D-arginine)?;CS-7595;NCGC00505008-01;BS-17319;DA-53444;FF111121;D71119;D-ArgininamideD-arginyl-D-arginyl-D-arginyl-D-arginyl-D-arginyl-D-alanine;H-D-Arg-D-Arg-D-Arg-D-Arg-D-Arg-D-Arg-NH2; H-(dR)(dR)(dR)(dR)(dR)(dR)-NH2;(2R)-2-[(2R)-2-[(2R)-2-[(2R)-2-[(2R)-2-[(2R)-2-amino-5-carbamimidamidopentanamido]-5-carbamimidamidopentanamido]-5-carbamimidamidopentanamido]-5-[(diaminomethylidene)amino]pentanamido]-5-[(diaminomethylidene)amino]pentanamido]-5-carbamimidamidopentanamide;(2R)-2-[(2R)-2-[(2R)-2-[(2R)-2-[(2R)-2-[(2R)-2-amino-5-carbamimidamidopentanamido]-5-carbamimidamidopentanamido]-5-carbamimidamidopentanamido]-5-carbamimidamidopentanamido]-5-carbamimidamidopentanamido]-5-carbamimidamidopentanamide;N~5~-(Diaminomethylidene)-D-ornithyl-N~5~-(diaminomethylidene)-D-ornithyl-N~5~-(diaminomethylidene)-D-ornithyl-N~5~-(diaminomethylidene)-D-ornithyl-N~5~-(diaminomethylidene)-D-ornithyl-N~5~-(diaminomethylidene)-D-ornithinamide;
Furin Inhibitor II is a specialized small molecule compound designed to selectively inhibit the activity of furin, a proprotein convertase enzyme involved in the proteolytic processing of a wide array of precursor proteins. As a critical regulator of protein maturation, furin mediates the cleavage of proproteins into their biologically active forms, impacting numerous physiological and pathological processes. The targeted inhibition of furin has emerged as an important tool in biochemical research, enabling scientists to dissect the roles of proprotein convertases in cellular signaling, protein trafficking, and disease mechanisms. Furin Inhibitor II offers high specificity and potency, making it an essential reagent for studies requiring precise modulation of proteolytic pathways.
Protease activity studies: Researchers employ Furin Inhibitor II to investigate the functional significance of furin-mediated cleavage events in diverse cellular systems. By selectively blocking furin activity, scientists can delineate the downstream effects of impaired proprotein processing, shedding light on the enzyme's role in maturation of growth factors, hormones, and membrane-bound receptors. This approach provides valuable mechanistic insights into the regulation of proteolytic networks and their influence on cell signaling and homeostasis.
Pathogen-host interaction research: In the context of infectious disease studies, Furin Inhibitor II is widely utilized to probe the involvement of furin in the activation of viral and bacterial proteins. Many pathogens exploit host furin to process their envelope or surface proteins, facilitating entry, replication, or virulence. By inhibiting furin, researchers can assess the impact of proteolytic processing on pathogen infectivity, host cell susceptibility, and cross-species transmission, thereby advancing understanding of host-pathogen dynamics at the molecular level.
Protein trafficking and secretion analysis: The compound serves as a valuable tool for exploring the influence of furin-dependent cleavage on the intracellular trafficking and secretion of proteins. Inhibition of furin enables detailed studies of how unprocessed precursor proteins are retained, mislocalized, or secreted in aberrant forms, affecting cellular communication and extracellular matrix composition. Such investigations are critical for unraveling the molecular basis of protein sorting disorders and secretory pathway regulation.
Biomarker validation and assay development: Furin Inhibitor II is frequently integrated into biochemical assay platforms to validate candidate biomarkers or to develop furin-specific activity assays. By providing a means to selectively suppress furin activity in vitro, it enables the establishment of robust, reproducible assays that can distinguish furin-dependent cleavage from other proteolytic events. This is particularly important in the context of high-throughput screening, diagnostic research, and the characterization of novel substrates or inhibitors.
Functional genomics and pathway mapping: The inhibitor is also employed in functional genomics experiments aimed at mapping the broader biological pathways governed by proprotein convertases. When used alongside genetic knockdown or overexpression strategies, Furin Inhibitor II facilitates the dissection of redundant or compensatory mechanisms among the convertase family. This integrative approach enhances the precision of pathway analysis and supports the identification of novel regulatory nodes within complex proteolytic cascades, contributing to a deeper understanding of cellular physiology and disease etiology.
3. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function
4. Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes
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