Santa Cruz Biotechnology now offers a broad range of cathepsin L Inhibitors. Cathepsin L is a dimer composed of disulfide-linked heavy and light chains, both produced from a single protein precursor. Substrates for Cathepsin L include collagen and elastin, as well as alpha-1 protease inhibitor, a major controlling element of neutrophil elastase activity. cathepsin L Inhibitors offered by Santa Cruz inhibit cathepsin L and, in some cases, other cellular metabolism and protein degradation related proteins. View detailed cathepsin L Inhibitor specifications, including cathepsin L Inhibitor CAS number, molecular weight, molecular formula and chemical structure, by clicking on the product name.
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Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
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Calpeptin | 117591-20-5 | sc-202516 sc-202516A | 10 mg 50 mg | $119.00 $447.00 | 28 | |
Calpeptin acts as a selective inhibitor of cathepsin L, characterized by its ability to form stable interactions with the enzyme's active site. Its unique structure facilitates specific hydrophobic and electrostatic interactions, which can alter the enzyme's conformation. Kinetic analyses reveal that Calpeptin exhibits competitive inhibition, impacting substrate binding dynamics and influencing the overall catalytic efficiency of cathepsin L. This modulation highlights its intricate role in proteolytic pathways. | ||||||
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 | $72.00 $145.00 $265.00 $489.00 $1399.00 $99.00 | 19 | |
Leupeptin hemisulfate is a potent inhibitor of cathepsin L, distinguished by its capacity to engage in specific non-covalent interactions with the enzyme's active site. This compound's unique stereochemistry allows for enhanced binding affinity, influencing the enzyme's conformational stability. Kinetic studies indicate that Leupeptin hemisulfate operates through a mixed inhibition mechanism, affecting both substrate affinity and turnover rates, thereby intricately modulating proteolytic activity. | ||||||
ALLM (Calpain Inhibitor) | 136632-32-1 | sc-201268 sc-201268A | 5 mg 25 mg | $140.00 $380.00 | 23 | |
ALLM, a selective calpain inhibitor, exhibits unique interactions with cathepsin L through its ability to form stable complexes with the enzyme's active site. Its structural conformation promotes a high binding affinity, which alters the enzyme's dynamics and stability. Kinetic analyses reveal that ALLM functions via competitive inhibition, impacting substrate recognition and catalytic efficiency, thus finely tuning proteolytic processes within cellular environments. | ||||||
E-64-d | 88321-09-9 | sc-201280 sc-201280A | 1 mg 5 mg | $70.00 $275.00 | 37 | |
E-64-d is a potent inhibitor of cathepsin L, characterized by its ability to form covalent bonds with the enzyme's active site cysteine residue. This irreversible binding modifies the enzyme's conformation, leading to a significant reduction in proteolytic activity. Kinetic studies indicate that E-64-d exhibits a unique mechanism of action, effectively blocking substrate access and altering the enzyme's catalytic pathway, thereby influencing cellular protein turnover and homeostasis. | ||||||
E-64 | 66701-25-5 | sc-201276 sc-201276A sc-201276B | 5 mg 25 mg 250 mg | $275.00 $928.00 $1543.00 | 14 | |
E-64 acts as a selective inhibitor of cathepsin L, engaging in a unique interaction with the enzyme's active site. By forming a stable covalent bond with the cysteine residue, E-64 induces a conformational change that disrupts the enzyme's normal function. This alteration not only impedes substrate binding but also modifies the enzyme's reaction kinetics, ultimately affecting the proteolytic landscape within cells and influencing various metabolic pathways. | ||||||
ALLN | 110044-82-1 | sc-221236 | 5 mg | $134.00 | 20 | |
ALLN serves as a potent inhibitor of cathepsin L, characterized by its ability to form a reversible complex with the enzyme. This interaction alters the enzyme's substrate specificity and modulates its catalytic efficiency. By influencing the dynamics of proteolytic activity, ALLN can shift the balance of protein turnover and degradation pathways, thereby impacting cellular homeostasis and the regulation of intracellular signaling cascades. | ||||||
Tebufenozide | 112410-23-8 | sc-280110 | 100 mg | $200.00 | ||
Tebufenozide is a non-peptidic, reversible inhibitor that targets cathepsin L by binding to the enzyme's active site, preventing substrate cleavage. | ||||||
Z-FA-FMK | 197855-65-5 | sc-201303 sc-201303A | 1 mg 5 mg | $125.00 $365.00 | 19 | |
Z-FA-FMK is a selective inhibitor of cathepsin L, known for its irreversible binding to the enzyme's active site. This covalent modification disrupts the enzyme's proteolytic function, leading to a significant decrease in its activity. The compound's unique structure allows for specific interactions with the enzyme, influencing the kinetics of substrate processing and altering the overall protease activity within cellular environments. Its mechanism highlights the intricate balance of proteolytic regulation. | ||||||
Chymostatin | 9076-44-2 | sc-202541 sc-202541A sc-202541B sc-202541C sc-202541D | 5 mg 10 mg 25 mg 50 mg 100 mg | $153.00 $255.00 $627.00 $1163.00 $2225.00 | 3 | |
Chymostatin is a potent inhibitor of cathepsin L, characterized by its ability to form non-covalent interactions with the enzyme's active site. This selective binding alters the enzyme's conformation, effectively modulating its proteolytic activity. The compound's unique structural features facilitate specific molecular interactions that influence substrate affinity and reaction kinetics, thereby impacting the dynamics of protein degradation pathways. Its role in protease regulation underscores the complexity of cellular proteolysis. | ||||||
Cathepsin L inhibitor | 167498-29-5 | sc-3132 | 5 mg | $122.00 | 15 | |
Cathepsin L inhibitors exhibit a unique mechanism of action by stabilizing the inactive form of the enzyme through specific hydrophobic and electrostatic interactions. This binding disrupts the enzyme's catalytic triad, leading to a significant decrease in proteolytic activity. The inhibitors can also influence the enzyme's conformational flexibility, affecting substrate recognition and processing. Their distinct molecular architecture allows for selective targeting, highlighting the intricate balance of protease activity in cellular homeostasis. |