Calpain Inhibitors
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Items 11 to 19 of 19 total
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
E-64-c | 76684-89-4 | sc-201278 sc-201278A | 1 mg 5 mg | $101.00 $392.00 | 3 | |
E-64-c is a potent inhibitor of calpain, a calcium-dependent cysteine protease, characterized by its ability to form covalent bonds with the active site cysteine residue. This selective interaction alters the enzyme's conformation, effectively blocking substrate access and modulating proteolytic activity. The compound's unique structure allows for specific targeting of calpain, influencing cellular signaling pathways and protein turnover, thereby impacting various physiological processes. | ||||||
PD 145305 | 90536-15-5 | sc-222131 | 5 mg | $255.00 | 1 | |
PD 145305 is a selective calpain inhibitor that operates through a unique mechanism of action, engaging with the enzyme's active site to disrupt its proteolytic function. This compound exhibits a high affinity for calpain, leading to a significant alteration in enzyme kinetics. By stabilizing the inactive form of calpain, PD 145305 effectively modulates intracellular calcium signaling and influences the degradation of specific substrates, thereby impacting cellular homeostasis and protein regulation. | ||||||
Aureusimine B | 170713-71-0 | sc-362711 | 1 mg | $204.00 | 1 | |
Aureusimine B functions as a calpain modulator, exhibiting a distinctive interaction with the enzyme's regulatory domains. This compound alters calpain's conformational dynamics, enhancing its selectivity for specific substrates. Its unique binding affinity influences the enzyme's proteolytic activity, leading to altered reaction kinetics. By selectively engaging with calpain, Aureusimine B plays a role in fine-tuning cellular signaling pathways and protein turnover, showcasing its intricate biochemical behavior. | ||||||
Penicillide | 55303-92-9 | sc-391044 | 1 mg | $160.00 | ||
Penicillide acts as a calpain modulator, characterized by its ability to disrupt the enzyme's active site through specific non-covalent interactions. This compound influences calpain's substrate recognition and catalytic efficiency, resulting in modified proteolytic rates. Its unique structural features facilitate selective binding, which can lead to differential regulation of cellular processes. The compound's impact on calpain dynamics highlights its role in modulating protease activity and cellular homeostasis. | ||||||
Calpeptin | 117591-20-5 | sc-202516 sc-202516A | 10 mg 50 mg | $119.00 $447.00 | 28 | |
Calpeptin is a potent inhibitor of calpain, exhibiting a unique mechanism of action that involves the stabilization of the enzyme's inactive conformation. By binding to the calpain catalytic domain, it alters the enzyme's conformational dynamics, effectively reducing its proteolytic activity. This selective inhibition can influence various signaling pathways, as calpain is involved in numerous cellular processes. The compound's specificity and binding affinity underscore its role in regulating protease function and maintaining cellular integrity. | ||||||
ALLM (Calpain Inhibitor) | 136632-32-1 | sc-201268 sc-201268A | 5 mg 25 mg | $140.00 $380.00 | 23 | |
ALLM is a selective calpain inhibitor that operates through a distinct mechanism, engaging with the enzyme's active site to prevent substrate access. This interaction leads to a conformational shift that diminishes calpain's proteolytic function. The compound's unique structure allows for high binding affinity, influencing calpain's kinetic properties and modulating its role in cellular signaling pathways. Its specificity highlights the intricate balance of protease regulation within cellular environments. | ||||||
ALLN | 110044-82-1 | sc-221236 | 5 mg | $134.00 | 20 | |
ALLN is a potent calpain inhibitor characterized by its ability to form stable interactions with the enzyme's catalytic domain. This compound disrupts the enzyme's normal activity by inducing a conformational change that alters substrate recognition. The unique steric and electronic properties of ALLN enhance its selectivity, allowing it to finely tune calpain-mediated proteolysis. Its influence on reaction kinetics underscores the complexity of protease regulation in various biological contexts. | ||||||
MDL-28170 | 88191-84-8 | sc-201301 sc-201301A sc-201301B sc-201301C | 10 mg 50 mg 100 mg 500 mg | $68.00 $236.00 $438.00 $2152.00 | 20 | |
MDL-28170 is a selective calpain inhibitor that exhibits unique binding dynamics with the enzyme's active site. Its structure facilitates the formation of hydrogen bonds and hydrophobic interactions, leading to a significant alteration in calpain's substrate affinity. This compound's kinetic profile reveals a competitive inhibition mechanism, highlighting its role in modulating proteolytic pathways. The distinct molecular interactions of MDL-28170 contribute to its specificity in targeting calpain isoforms, showcasing its intricate influence on protease activity. | ||||||
EDTA, disodium salt, dihydrate, for molecular biology | 6381-92-6 | sc-359904 sc-359904B sc-359904A sc-359904C sc-359904D sc-359904E | 50 g 100 g 250 g 500 g 1 kg 5 kg | $56.00 $87.00 $143.00 $194.00 $255.00 $969.00 | 1 | |
EDTA, disodium salt, dihydrate, is a chelating agent that effectively sequesters divalent metal ions, influencing various biochemical pathways. Its ability to form stable complexes with calcium and magnesium ions alters enzyme activity and stabilizes protein structures. This compound exhibits unique solubility properties, enhancing its interaction with biomolecules. By modulating metal ion availability, EDTA plays a crucial role in regulating enzymatic reactions and cellular processes, impacting overall molecular dynamics. | ||||||