Calpain 1 Inhibitors
Santa Cruz Biotechnology now offers a broad range of Calpain 1 Inhibitors. Calpains are a family of cytosolic calcium-regulated cysteine proteases that functions to regulate a wide variety of cellular processes. Calpain cleaves cytoskeletal and submembranous proteins, and is thought to play a role in cytoskeletal reorganization and muscle protein degradation. Calpain 1 Inhibitors offered by Santa Cruz inhibit Calpain 1 and, in some cases, other cell cycle and cytoskeletal related proteins. View detailed Calpain 1 Inhibitor specifications, including Calpain 1 Inhibitor CAS number, molecular weight, molecular formula and chemical structure, by clicking on the product name.
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Calpeptin | 117591-20-5 | sc-202516 sc-202516A | 10 mg 50 mg | $119.00 $447.00 | 28 | |
Calpeptin is a selective inhibitor of calpain 1, characterized by its ability to bind to the enzyme's active site, disrupting substrate access. This interaction alters the enzyme's conformation, leading to a decrease in proteolytic activity. The compound exhibits unique kinetics, with a rapid association and slower dissociation, allowing for sustained inhibition. Its specificity for calpain 1 over other cysteine proteases highlights its potential for targeted modulation of proteolytic pathways in cellular processes. | ||||||
ALLM (Calpain Inhibitor) | 136632-32-1 | sc-201268 sc-201268A | 5 mg 25 mg | $140.00 $380.00 | 23 | |
ALLM is a potent calpain 1 inhibitor that operates through a unique mechanism of action, forming a stable complex with the enzyme. This binding induces a conformational change that effectively blocks substrate recognition and processing. The compound demonstrates distinctive reaction kinetics, characterized by a fast initial binding phase followed by a prolonged inhibitory effect. Its selectivity for calpain 1 underscores its role in modulating specific proteolytic pathways, influencing cellular signaling and homeostasis. | ||||||
ALLN | 110044-82-1 | sc-221236 | 5 mg | $134.00 | 20 | |
ALLN is a selective inhibitor of calpain 1, characterized by its ability to form a covalent bond with the enzyme's active site. This interaction alters the enzyme's conformation, preventing substrate access and subsequent proteolytic activity. The compound exhibits unique reaction kinetics, with a rapid association rate and a sustained inhibitory effect. Its specificity for calpain 1 highlights its role in regulating targeted proteolytic processes, impacting various cellular functions and signaling pathways. | ||||||
PD 150606 | 179528-45-1 | sc-222133 sc-222133A | 5 mg 25 mg | $116.00 $395.00 | 18 | |
Functions as an inhibitor of Calpain 1, a calcium-dependent protease. It may interfere with Calpain 1's activity, affecting its role in cellular processes. | ||||||
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 potent inhibitor of calpain 1, distinguished by its unique ability to interact with the enzyme's catalytic domain through non-covalent interactions. This compound stabilizes an inactive conformation of calpain 1, effectively blocking substrate binding and enzymatic activity. Its kinetic profile reveals a slow dissociation rate, ensuring prolonged inhibition. Additionally, MDL-28170's selectivity underscores its potential to modulate specific proteolytic pathways, influencing cellular dynamics and regulatory mechanisms. | ||||||
Calpain Inhibitor XII | 181769-57-3 | sc-300318 sc-300318A | 1 mg 5 mg | $130.00 $539.00 | ||
Calpain Inhibitor XII is a selective modulator of calpain 1, characterized by its unique binding affinity to the enzyme's active site. This compound disrupts the enzyme's conformational flexibility, preventing substrate access and subsequent proteolytic activity. Its interaction kinetics demonstrate a significant residence time, allowing for sustained inhibition. Furthermore, Calpain Inhibitor XII's specificity highlights its role in fine-tuning cellular signaling pathways, impacting various physiological processes. | ||||||
PD 151746 | 179461-52-0 | sc-222134 | 5 mg | $192.00 | 3 | |
PD 151746 is a selective inhibitor of calpain 1, exhibiting a unique mechanism of action through its interaction with the enzyme's regulatory domain. This compound stabilizes the inactive conformation of calpain 1, effectively blocking substrate binding and enzymatic activity. Its kinetic profile reveals a slow dissociation rate, ensuring prolonged inhibition. Additionally, PD 151746's specificity for calpain 1 underscores its potential to modulate intricate cellular pathways without affecting other proteases. | ||||||
Z-L-Abu-CONH-ethyl | sc-301995 sc-301995A | 1 mg 5 mg | $120.00 $471.00 | 3 | ||
Z-L-Abu-CONH-ethyl acts as a selective inhibitor of calpain 1, characterized by its ability to form stable interactions with the enzyme's active site. This compound alters the enzyme's conformational dynamics, leading to a significant reduction in proteolytic activity. Its unique binding affinity results in a distinct kinetic behavior, allowing for a gradual onset of inhibition. Furthermore, Z-L-Abu-CONH-ethyl's specificity minimizes off-target effects, making it a valuable tool for studying calpain-mediated processes. | ||||||
Z-L-Abu-CONH(CH2)3-morpholine | 145731-49-3 | sc-301996 sc-301996A | 1 mg 5 mg | $145.00 $400.00 | ||
Z-L-Abu-CONH(CH2)3-morpholine exhibits a unique mechanism of action as a calpain 1 inhibitor, engaging in specific hydrogen bonding and hydrophobic interactions within the enzyme's active site. This compound induces conformational changes that disrupt substrate access, effectively modulating enzymatic activity. Its distinct structural features contribute to a slow, sustained inhibition profile, allowing for nuanced exploration of calpain's role in cellular processes without significant interference from other proteases. | ||||||