cathepsin K Inhibitors
Santa Cruz Biotechnology now offers a broad range of cathepsin K Inhibitors. The cathepsin family of proteolytic enzymes contains several diverse classes of proteases. Cathepsin K is a cystine protease involved in bone resorption. Cathepsin K inhibitors, such as odanacatib, show great potential in the treatment of osteoporosis. Cathepsin K expression is highest in bone, cartilage and skeletal muscle. cathepsin K Inhibitors offered by Santa Cruz inhibit cathepsin K and, in some cases, other cellular metabolism and protein degradation related proteins. View detailed cathepsin K Inhibitor specifications, including cathepsin K 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 | $121.00 $456.00 | 28 | |
Calpeptin is a selective inhibitor of cathepsin K, distinguished by its ability to form stable complexes with the enzyme's active site. Its unique structure facilitates specific interactions that disrupt substrate binding, effectively modulating proteolytic activity. The compound's kinetic properties reveal a slow-onset inhibition, allowing for prolonged effects on enzyme function. Additionally, its conformational flexibility enhances its interaction with the enzyme, providing insights into protease regulation and specificity. | ||||||
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 is a potent inhibitor of cathepsin K, characterized by its ability to covalently modify the enzyme's active site through a unique electrophilic mechanism. This interaction leads to irreversible inhibition, significantly altering the enzyme's catalytic efficiency. The compound's structural features promote selective binding, influencing the conformational dynamics of cathepsin K. Its reaction kinetics demonstrate a rapid onset of inhibition, providing a distinct profile in enzyme regulation studies. | ||||||
Odanacatib | 603139-19-1 | sc-364675 sc-364675A sc-364675B | 5 mg 25 mg 250 mg | $218.00 $993.00 $1982.00 | 2 | |
Odanacatib functions as a selective inhibitor of cathepsin K, exhibiting a unique binding affinity that stabilizes the enzyme in an inactive conformation. Its molecular structure facilitates specific interactions with the enzyme's active site, disrupting substrate access and altering the enzyme's natural turnover rate. The compound's kinetic profile reveals a slow, time-dependent inhibition, highlighting its potential for nuanced modulation of proteolytic activity in biochemical pathways. | ||||||
BML-244 | 104062-70-6 | sc-221370 sc-221370A | 5 mg 25 mg | $81.00 $239.00 | ||
BML-244 acts as a potent inhibitor of cathepsin K, characterized by its ability to form stable complexes with the enzyme. This compound engages in specific non-covalent interactions, effectively blocking substrate binding and altering the enzyme's catalytic efficiency. Its unique structural features promote a distinct conformational change in cathepsin K, leading to a significant reduction in proteolytic activity. The compound's inhibition kinetics suggest a complex mechanism that may involve allosteric modulation. | ||||||
L 006235 | 294623-49-7 | sc-361220 sc-361220A | 10 mg 50 mg | $209.00 $882.00 | 1 | |
L 006235 is a selective inhibitor of cathepsin K, distinguished by its unique ability to disrupt the enzyme's active site through specific steric hindrance. This compound exhibits a high affinity for the enzyme, facilitating a unique binding mode that alters the enzyme's conformational dynamics. The interaction kinetics reveal a slow-onset inhibition, suggesting a potential for prolonged effects on cathepsin K activity. Its distinct molecular architecture enhances specificity, minimizing off-target interactions. | ||||||
WAY 170523 | 307002-73-9 | sc-361402 sc-361402A | 1 mg 10 mg | $275.00 $595.00 | 1 | |
Acts as a selective inhibitor of Cathepsin K, disrupting its proteolytic activity involved in bone matrix breakdown. | ||||||
2-cyano-Pyrimidine | 14080-23-0 | sc-205083 sc-205083A | 1 g 10 g | $28.00 $224.00 | ||
2-Cyano-Pyrimidine acts as a potent modulator of cathepsin K, characterized by its ability to form stable interactions with the enzyme's catalytic residues. This compound engages in unique hydrogen bonding and π-π stacking, influencing the enzyme's structural integrity. The reaction kinetics indicate a competitive inhibition mechanism, where the presence of 2-cyano-Pyrimidine effectively alters substrate accessibility, leading to a nuanced regulation of enzymatic activity. Its distinct electronic properties further enhance binding affinity, promoting selective engagement with cathepsin K. | ||||||
N-Boc-L-phenylalaninal | 72155-45-4 | sc-206062 sc-206062A | 250 mg 1 g | $46.00 $150.00 | ||
N-Boc-L-phenylalaninal exhibits intriguing interactions with cathepsin K, primarily through its electrophilic carbonyl group, which facilitates covalent bonding with the enzyme's active site residues. This compound's unique steric hindrance, due to the bulky Boc group, modulates the enzyme's conformation, impacting substrate orientation. The reaction kinetics reveal a non-competitive inhibition profile, where N-Boc-L-phenylalaninal alters the enzyme's dynamics, enhancing selectivity and specificity in substrate processing. | ||||||
5,5-Dimethyl-2,4-oxazolidinedione | 695-53-4 | sc-254861 | 5 g | $120.00 | ||
5,5-Dimethyl-2,4-oxazolidinedione engages with cathepsin K through its cyclic structure, which allows for unique hydrogen bonding interactions with the enzyme's active site. This compound's distinctive ring strain influences the enzyme's catalytic efficiency, promoting a conformational shift that enhances substrate accessibility. Kinetic studies indicate a mixed inhibition mechanism, where 5,5-Dimethyl-2,4-oxazolidinedione modulates enzyme activity, affecting both binding affinity and turnover rates. | ||||||