MMP-12 Inhibitors
Santa Cruz Biotechnology now offers a broad range of MMP-12 Inhibitors. The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, Fibronectin, Laminin and proteoglycan. MMP-12 Inhibitors offered by Santa Cruz inhibit MMP-12 and, in some cases, other metalloproteinase and zinc-dependent endopeptidase related proteins. View detailed MMP-12 Inhibitor specifications, including MMP-12 Inhibitor CAS number, molecular weight, molecular formula and chemical structure, by clicking on the product name.
Items 1 to 10 of 11 total
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
GM 6001 | 142880-36-2 | sc-203979 sc-203979A | 1 mg 5 mg | $75.00 $265.00 | 55 | |
GM 6001 (CAS 142880-36-2) is a chemical compound that acts as an effective inhibitor of MMP-12, a proteolytic enzyme. It modulates MMP-12 activity by binding to its active site, thereby regulating its function in various biological processes. | ||||||
Actinonin | 13434-13-4 | sc-201289 sc-201289B | 5 mg 10 mg | $160.00 $319.00 | 3 | |
Actinonin (CAS 13434-13-4) is a bioactive compound recognized for its significant role as an inhibitor of MMP-12, an enzyme belonging to the matrix metalloproteinase family. MMP-12 plays a crucial role in tissue remodeling, particularly in processes associated with inflammation. By targeting MMP-12, actinonin modulates its enzymatic activity, potentially influencing pathways related to tissue homeostasis and cellular responses. | ||||||
Prinomastat | 192329-42-3 | sc-507449 | 5 mg | $190.00 | ||
Prinomastat is a synthetic inhibitor that targets multiple MMPs, including MMP-It has been studied for its potential anti-inflammatory and anti-metastatic properties. | ||||||
PF-356231 | 766536-21-4 | sc-222151 sc-222151A | 1 mg 5 mg | $150.00 $395.00 | 1 | |
PF-356231 (CAS 766536-21-4) functions as a potent inhibitor of MMP-12, a proteolytic enzyme involved in tissue remodeling and inflammation control. | ||||||
WAY 170523 | 307002-73-9 | sc-361402 sc-361402A | 1 mg 10 mg | $275.00 $595.00 | 1 | |
This is a selective inhibitor of MMP-12 that has shown promise in research on diseases involving tissue destruction and inflammation. | ||||||
Ageladine A, TFA | 643020-13-7 | sc-396549 | 200 µg | $364.00 | ||
Ageladine A, TFA (CAS 643020-13-7) is recognized for its role as an MMP-12 inhibitor, crucial in modulating tissue remodeling and inflammation pathways. | ||||||
NNGH | 161314-17-6 | sc-222075 | 5 mg | $95.00 | 2 | |
NNGH functions as a potent modulator of MMP-12, exhibiting a unique ability to stabilize enzyme conformations through specific electrostatic interactions and steric hindrance. This compound alters the dynamics of substrate binding, leading to a notable decrease in catalytic efficiency. Its distinct reaction kinetics reveal a non-competitive inhibition profile, where NNGH effectively reduces the overall enzymatic activity without directly competing with substrate molecules, thereby impacting extracellular matrix remodeling processes. | ||||||
ARP 100 | 704888-90-4 | sc-203522 | 5 mg | $121.00 | 26 | |
ARP-100 is a synthetic MMP inhibitor that has demonstrated efficacy against MMP-It has been explored for its research potential to attenuate tissue damage in lung diseases. | ||||||
MMP-3 Inhibitor VIII | 208663-26-7 | sc-311435 | 5 mg | $400.00 | ||
MMP-3 Inhibitor VIII demonstrates a remarkable capacity to selectively interact with MMP-12, influencing its enzymatic behavior through unique allosteric modulation. This compound alters the enzyme's active site accessibility, resulting in a significant reduction in proteolytic activity. Its kinetic profile indicates a mixed inhibition mechanism, where it affects both substrate affinity and turnover rate, thereby reshaping the enzymatic landscape and influencing cellular signaling pathways. | ||||||
MMP Inhibitor V | 223472-31-9 | sc-203139 | 2 mg | $216.00 | 2 | |
MMP Inhibitor V exhibits a distinctive ability to bind to MMP-12, leading to conformational changes that hinder substrate recognition. This compound engages in specific hydrogen bonding and hydrophobic interactions, stabilizing an inactive enzyme state. Its reaction kinetics reveal a competitive inhibition pattern, effectively altering the enzyme's catalytic efficiency. Additionally, MMP Inhibitor V's unique structural features contribute to its selectivity, enhancing its interaction dynamics with MMP-12. | ||||||