Elastase Inhibitors
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
MeOSuc-AAPV-AMC | 72252-90-5 | sc-201163 | 5 mg | $185.00 | 19 | |
MeOSuc-AAPV-AMC serves as a substrate for elastase, showcasing a unique cleavage pattern that highlights its specificity for serine proteases. The compound's design incorporates a fluorogenic moiety, enabling real-time monitoring of enzymatic activity. Its interactions with the active site of elastase facilitate a rapid hydrolysis reaction, characterized by distinct kinetic parameters. This specificity and efficiency in substrate recognition underscore its role in proteolytic pathways. | ||||||
Elastase Inhibitor I | sc-221584 | 1 mg | $171.00 | |||
Elastase Inhibitor I functions by selectively binding to the active site of elastase, disrupting its proteolytic activity. This inhibitor exhibits a unique affinity for the enzyme, leading to a significant alteration in the reaction kinetics, effectively slowing down the hydrolysis of peptide bonds. Its structural conformation allows for specific molecular interactions that stabilize the enzyme-inhibitor complex, thereby modulating elastase's role in various biological processes. | ||||||
Elastase Inhibitor II | sc-294466 sc-294466A | 5 mg 10 mg | $327.00 $629.00 | |||
Elastase Inhibitor II operates through a distinct mechanism that involves competitive inhibition at the elastase active site. Its unique molecular structure facilitates strong hydrogen bonding and hydrophobic interactions, enhancing binding affinity. This inhibitor alters the enzyme's conformational dynamics, resulting in a marked decrease in substrate turnover rates. The intricate balance of steric and electronic factors in its design allows for precise modulation of elastase activity, influencing downstream proteolytic pathways. | ||||||
Ecotin, E. coli | 87928-05-0 | sc-221575 | 100 µg | $264.00 | ||
Ecotin, derived from E. coli, exhibits a remarkable ability to bind elastase with high specificity, utilizing a unique combination of electrostatic and hydrophobic interactions. Its structure features a flexible loop that adapts to the enzyme's active site, effectively blocking substrate access. This adaptability enhances its inhibitory potency, leading to a significant reduction in elastase activity. The kinetic profile of Ecotin reveals a slow dissociation rate, ensuring prolonged inhibition and stability in various environments. | ||||||
SSR 69071 | 344930-95-6 | sc-203702 | 10 mg | $202.00 | 1 | |
SSR 69071 is a potent elastase inhibitor characterized by its unique binding affinity and specificity. It engages elastase through a series of intricate hydrogen bonds and van der Waals interactions, stabilizing the enzyme-inhibitor complex. The compound's rigid structure allows for precise alignment within the active site, effectively obstructing substrate entry. Kinetic studies indicate a rapid association rate, contributing to its effectiveness in modulating elastase activity under diverse conditions. | ||||||
Elasnin | 68112-21-0 | sc-280684 sc-280684A | 1 mg 5 mg | $196.00 $930.00 | ||
Elasnin is a selective elastase modulator that exhibits remarkable interaction dynamics with the enzyme's active site. Its unique conformation facilitates the formation of multiple hydrophobic contacts, enhancing binding stability. The compound's ability to induce conformational changes in elastase promotes a distinct inhibition pathway, characterized by a slow dissociation rate. This kinetic profile allows for sustained modulation of elastase activity, making it a subject of interest in enzymatic regulation studies. | ||||||
Sivelestat sodium salt | 150374-95-1 | sc-361359 sc-361359A | 10 mg 50 mg | $104.00 $427.00 | 1 | |
Sivelestat sodium salt acts as a potent elastase inhibitor, characterized by its ability to form specific hydrogen bonds with key residues in the enzyme's active site. This interaction not only stabilizes the enzyme-inhibitor complex but also alters the enzyme's catalytic conformation, leading to a significant reduction in enzymatic activity. The compound's unique structural features contribute to its selective binding, influencing reaction kinetics and providing insights into elastase regulation mechanisms. | ||||||
Glutaryl-Ala-Ala-Phe-4-methoxy-β-naphthylamide | 79642-99-2 | sc-488720 | 10 mg | $440.00 | ||
Glutaryl-Ala-Ala-Phe-4-methoxy-β-naphthylamide exhibits remarkable specificity as an elastase inhibitor through its unique peptide backbone and aromatic moiety. The compound engages in hydrophobic interactions and π-π stacking with the enzyme, enhancing binding affinity. Its design allows for a conformational fit that disrupts substrate access, effectively modulating the enzyme's activity. This selective interaction provides a deeper understanding of elastase's role in proteolytic pathways. | ||||||