MMP Inhibitors
Items 11 to 20 of 33 total
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
GM 6001, Negative Control | 877381-76-5 | sc-295025 sc-295025A | 1 mg 5 mg | $125.00 $440.00 | ||
GM 6001, a negative control for matrix metalloproteinases (MMPs), is characterized by its unique ability to disrupt enzyme-substrate interactions without forming stable complexes. This compound exhibits a rapid dissociation rate, which limits its inhibitory potential, making it an ideal reference for assessing MMP activity. Its structural properties allow for minimal steric hindrance, ensuring that it does not interfere with the catalytic mechanisms of MMPs, thus serving as a baseline in experimental settings. | ||||||
Lactobionic acid | 96-82-2 | sc-221826 sc-221826A | 100 g 500 g | $235.00 $369.00 | ||
Lactobionic acid functions as a matrix metalloproteinase (MMP) modulator, exhibiting unique interactions with the enzyme's active site. Its structural features promote specific hydrogen bonding and electrostatic interactions, enhancing selectivity. The compound's ability to stabilize transition states influences reaction kinetics, allowing for nuanced regulation of MMP activity. Additionally, its hydrophilic nature facilitates solubility, impacting its distribution in biological systems. | ||||||
o-Phenanthroline monohydrate | 5144-89-8 | sc-202256 sc-202256A | 1 g 25 g | $42.00 $184.00 | 1 | |
o-Phenanthroline monohydrate acts as a matrix metalloproteinase (MMP) modulator through its chelating properties, forming stable complexes with metal ions essential for MMP function. This interaction alters the enzyme's conformation, affecting substrate binding and catalytic efficiency. The compound's planar structure enhances π-π stacking interactions, influencing molecular recognition. Its solubility characteristics also play a role in modulating local concentrations, further impacting MMP activity. | ||||||
Ecotin, E. coli | 87928-05-0 | sc-221575 | 100 µg | $259.00 | ||
Ecotin, derived from E. coli, functions as a matrix metalloproteinase (MMP) modulator by specifically binding to the active sites of MMPs, inhibiting their enzymatic activity. Its unique structure allows for selective interactions with zinc ions, crucial for MMP function, thereby stabilizing the enzyme in an inactive form. The presence of hydrophobic regions enhances its affinity for target proteins, influencing the dynamics of protein-protein interactions and altering reaction kinetics. | ||||||
4-epi-Chlortetracycline Hydrochloride | 101342-45-4 | sc-206875 sc-206875A sc-206875B | 1 mg 5 mg 10 mg | $475.00 $562.00 $1132.00 | ||
4-epi-Chlortetracycline Hydrochloride acts as a matrix metalloproteinase (MMP) modulator through its ability to chelate metal ions, particularly zinc, which are essential for MMP activity. Its unique tetracycline backbone facilitates specific interactions with the enzyme's active site, leading to conformational changes that reduce enzymatic function. Additionally, its amphipathic nature promotes interactions with lipid membranes, potentially influencing cellular signaling pathways and modulating protein interactions. | ||||||
N-Dansyl-D-phenylalanine | 56176-31-9 | sc-391601 | 250 mg | $337.00 | ||
N-Dansyl-D-phenylalanine functions as a matrix metalloproteinase (MMP) modulator by engaging in selective interactions with the enzyme's active site. The dansyl group enhances hydrophobic interactions, promoting conformational alterations that inhibit MMP activity. Its unique structure allows for specific binding to metal ions, disrupting the catalytic mechanism. Furthermore, the compound's fluorescence properties enable real-time monitoring of MMP activity, providing insights into reaction kinetics and enzyme dynamics. | ||||||
20(R)-Ginsenoside Rh2 | 112246-15-8 | sc-396791 | 1 mg | $168.00 | ||
20(R)-Ginsenoside Rh2 acts as a matrix metalloproteinase (MMP) modulator through its unique stereochemistry, which facilitates specific interactions with the enzyme's substrate-binding site. This compound exhibits a distinctive ability to stabilize the enzyme's inactive conformation, effectively reducing its catalytic efficiency. Additionally, its hydrophilic regions enhance solubility, influencing the diffusion kinetics and overall bioavailability in biochemical environments. | ||||||
Pro-Leu-Gly hydroxamate hydrochloride | 120928-08-7 | sc-215748 sc-215748A | 50 mg 250 mg | $199.00 $793.00 | ||
Pro-Leu-Gly hydroxamate hydrochloride functions as a matrix metalloproteinase (MMP) inhibitor by forming strong chelation complexes with the zinc ion in the enzyme's active site. This interaction disrupts the enzyme's catalytic mechanism, leading to a decrease in proteolytic activity. Its hydroxamate group enhances binding affinity, while the peptide backbone contributes to conformational stability, influencing the kinetics of enzyme-substrate interactions and modulating proteolytic pathways. | ||||||
GM 6001 | 142880-36-2 | sc-203979 sc-203979A | 1 mg 5 mg | $75.00 $265.00 | 55 | |
GM 6001 acts as a matrix metalloproteinase (MMP) inhibitor through its unique ability to form stable complexes with the zinc ion in the enzyme's active site. This interaction alters the enzyme's conformation, effectively hindering its catalytic function. The compound's structural features promote selective binding, influencing the reaction kinetics and modulating the activity of various MMPs, thereby impacting extracellular matrix remodeling processes. | ||||||
Actinonin | 13434-13-4 | sc-201289 sc-201289B | 5 mg 10 mg | $160.00 $319.00 | 3 | |
Actinonin functions as a matrix metalloproteinase (MMP) inhibitor by selectively targeting the enzyme's active site, where it engages in specific interactions with the catalytic zinc ion. This binding stabilizes the enzyme's structure, leading to a significant reduction in its proteolytic activity. The compound's unique molecular architecture enhances its affinity for MMPs, influencing substrate accessibility and altering the dynamics of extracellular matrix turnover. | ||||||