| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Camostat mesylate | 59721-29-8 | sc-203867 sc-203867A sc-203867B sc-203867C sc-203867D sc-203867E | 10 mg 50 mg 500 mg 1 g 10 g 100 g | $43.00 $183.00 $312.00 $624.00 $2081.00 $4474.00 | 5 | |
Camostat mesylate acts as a potent serine protease inhibitor, exhibiting a unique mechanism of action through its reversible binding to the active site of target enzymes. This interaction alters the enzyme's conformation, impacting substrate accessibility and catalytic efficiency. Its specificity for certain proteases allows for selective modulation of proteolytic pathways, influencing various biological processes. The compound's kinetic profile reveals a rapid association and slower dissociation, underscoring its potential for sustained enzymatic regulation. | ||||||
Nafamostat mesylate | 82956-11-4 | sc-201307 sc-201307A | 10 mg 50 mg | $82.00 $306.00 | 4 | |
Nafamostat mesylate functions as a selective inhibitor of serine proteases, characterized by its ability to form stable complexes with target enzymes. This compound exhibits a unique affinity for the active site, leading to conformational changes that hinder substrate binding. Its rapid kinetics facilitate quick inhibition, while the prolonged dissociation rate allows for extended regulatory effects on proteolytic activity. The compound's specificity enhances its role in modulating intricate biochemical pathways. | ||||||
Gabexate mesylate | 56974-61-9 | sc-215066 | 5 mg | $100.00 | ||
Gabexate mesylate acts as a potent inhibitor of serine proteases, distinguished by its unique ability to interact with the enzyme's active site through hydrogen bonding and hydrophobic interactions. This compound demonstrates a rapid onset of action, effectively altering enzyme conformation and disrupting substrate access. Its selective binding profile allows for targeted modulation of proteolytic processes, influencing various physiological pathways with precision and efficiency. | ||||||