cathepsin H Inhibitors
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Leupeptin hemisulfate | 103476-89-7 | sc-295358 sc-295358A sc-295358D sc-295358E sc-295358B sc-295358C | 5 mg 25 mg 50 mg 100 mg 500 mg 10 mg | $73.00 $148.00 $316.00 $499.00 $1427.00 $101.00 | 19 | |
Leupeptin hemisulfate is a potent inhibitor of cathepsin H, characterized by its ability to form stable complexes with the enzyme. This interaction is facilitated by specific hydrogen bonding and hydrophobic contacts, which enhance binding affinity. The compound's structural features allow it to effectively mimic natural substrates, disrupting the enzyme's catalytic activity. Its influence on proteolytic pathways highlights the intricate balance of enzyme regulation and substrate competition in cellular processes. | ||||||
E-64-d | 88321-09-9 | sc-201280 sc-201280A | 1 mg 5 mg | $71.00 $281.00 | 37 | |
E-64-d is a selective inhibitor of cathepsin H, distinguished by its unique ability to engage in covalent interactions with the enzyme's active site. This compound exhibits a high degree of specificity due to its structural conformation, which aligns perfectly with the enzyme's catalytic residues. The kinetics of E-64-d reveal a slow-binding mechanism, allowing for prolonged inhibition. Its interactions can modulate proteolytic activity, influencing cellular homeostasis and protein turnover. | ||||||
E-64 | 66701-25-5 | sc-201276 sc-201276A sc-201276B | 5 mg 25 mg 250 mg | $281.00 $947.00 $1574.00 | 14 | |
E-64 acts as a potent inhibitor of cathepsin H, characterized by its irreversible binding to the enzyme's active site through a nucleophilic attack. This compound's unique electrophilic nature facilitates the formation of a stable covalent bond, effectively blocking substrate access. The inhibition kinetics suggest a time-dependent process, where the rate of inactivation is influenced by the enzyme's conformational dynamics. E-64's selectivity stems from its tailored molecular structure, which enhances its affinity for cathepsin H over other cysteine proteases. | ||||||
Z-FA-FMK | 197855-65-5 | sc-201303 sc-201303A | 1 mg 5 mg | $128.00 $372.00 | 19 | |
Z-FA-FMK is a selective inhibitor of cathepsin H, distinguished by its ability to form a covalent bond with the enzyme via a unique electrophilic mechanism. This compound exhibits a high degree of specificity due to its structural design, which allows for precise interactions with the enzyme's active site. The kinetics of inhibition reveal a rapid onset, with a significant impact on the enzyme's catalytic efficiency, highlighting its role in modulating proteolytic pathways. | ||||||
Chymostatin | 9076-44-2 | sc-202541 sc-202541A sc-202541B sc-202541C sc-202541D | 5 mg 10 mg 25 mg 50 mg 100 mg | $156.00 $260.00 $640.00 $1186.00 $2270.00 | 3 | |
Chymostatin is a potent inhibitor of cathepsin H, characterized by its ability to engage in non-covalent interactions with the enzyme's active site. This compound exhibits unique binding dynamics, leading to a conformational change in the enzyme that alters its substrate affinity. The inhibition kinetics suggest a competitive mechanism, where Chymostatin effectively disrupts the proteolytic activity, influencing various cellular processes and pathways. Its selectivity stems from specific molecular interactions that enhance its efficacy. | ||||||
E-64-c | 76684-89-4 | sc-201278 sc-201278A | 1 mg 5 mg | $103.00 $400.00 | 3 | |
E-64-c is a selective inhibitor of cathepsin H, distinguished by its irreversible binding to the enzyme's active site through covalent modification. This compound forms a stable adduct with the active site cysteine residue, effectively blocking substrate access. The kinetics of E-64-c reveal a time-dependent inhibition profile, highlighting its potency. Its unique structural features facilitate specific interactions that enhance its inhibitory action, impacting proteolytic pathways in cellular environments. | ||||||