CLAP Inhibitors
Chemical inhibitors of CLAP can act through various mechanisms to inhibit its proteolytic functions. Marimastat, Batimastat, and Ilomastat, as matrix metalloproteinase inhibitors, can prevent the degradation of the extracellular matrix proteins, which is a necessary step for the proper functioning of CLAP in processes such as cell migration and tissue remodeling. Inhibition by these compounds stabilizes the extracellular matrix, potentially altering the signaling pathways and physical environment where CLAP operates. E-64, targeting cysteine proteases, can interfere with the catalytic activity of enzymes that utilize a cysteine residue in their active site. CLAP activities that depend on the proteolysis mediated by cysteine proteases can be affected by E-64, leading to reduced degradation of protein substrates within the cell. Similarly, Leupeptin's broad-spectrum inhibition of serine and cysteine proteases can lead to a decrease in the proteolytic activity that CLAP is associated with, affecting various biological processes.
O-Phenanthroline, as a metalloprotease inhibitor, can chelate metal ions necessary for the activity of metalloproteases, and this action can indirectly affect CLAP functionality by altering metalloprotease-related pathways. Lactacystin and MG-132, which inhibit the proteasome, prevent the degradation of ubiquitinated proteins that could be involved in regulating CLAP function, thus affecting the proteolytic environment. Aprotinin and Chymostatin, which inhibit serine proteases like trypsin and chymotrypsin, respectively, can modify the proteolytic pathways and impact the stability of protein substrates relevant to CLAP activity. Alloxan, though primarily known for its effects on glucose metabolism, can indirectly influence CLAP by altering the metabolic state of the cell, which can affect protease activity. Each of these inhibitors contributes to the modulation of the proteolytic landscape in which CLAP is involved, resulting in the reduction of its functional activity by stabilizing substrates or disrupting necessary proteolytic cascades.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Marimastat | 154039-60-8 | sc-202223 sc-202223A sc-202223B sc-202223C sc-202223E | 5 mg 10 mg 25 mg 50 mg 400 mg | $168.00 $218.00 $404.00 $629.00 $4900.00 | 19 | |
Marimastat is a broad-spectrum matrix metalloproteinase inhibitor. CLAP is involved in proteolytic processes; by inhibiting matrix metalloproteinases, Marimastat can reduce the proteolytic degradation of the extracellular matrix, which is a pathway necessary for the function of CLAP related to cell migration and tissue remodeling. | ||||||
Batimastat | 130370-60-4 | sc-203833 sc-203833A | 1 mg 10 mg | $179.00 $377.00 | 24 | |
Batimastat is another inhibitor of matrix metalloproteinases. Given CLAP's role in proteolysis, Batimastat can inhibit the breakdown of the extracellular matrix by matrix metalloproteinases, indirectly inhibiting CLAP's associated functions in cell motility and angiogenesis. | ||||||
GM 6001 | 142880-36-2 | sc-203979 sc-203979A | 1 mg 5 mg | $77.00 $270.00 | 55 | |
Ilomastat, also known as GM6001, is a matrix metalloproteinase inhibitor that can inhibit the proteolytic activity of CLAP by stabilizing the extracellular matrix, thus interfering with the protease-mediated signaling required for the functional activity of CLAP. | ||||||
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, irreversible cysteine protease inhibitor. By inhibiting cysteine proteases, E-64 can impede the proteolytic pathways that CLAP is involved in, particularly those related to protein degradation and turnover, leading to the functional inhibition of CLAP. | ||||||
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 | $73.00 $148.00 $316.00 $499.00 $1427.00 $101.00 | 19 | |
Leupeptin inhibits serine and cysteine proteases, which play a critical role in the proteolytic pathways CLAP is involved in. Inhibition of these proteases by Leupeptin would lead to a decrease in protease activity that is necessary for the functional role of CLAP in various biological processes. | ||||||
Lactacystin | 133343-34-7 | sc-3575 sc-3575A | 200 µg 1 mg | $188.00 $575.00 | 60 | |
Lactacystin is a specific inhibitor of the proteasome. CLAP, as a protein involved in proteolysis, may be involved in pathways regulated by the proteasome. Inhibition of the proteasome by Lactacystin can therefore lead to an accumulation of proteins that are supposed to be degraded, indirectly inhibiting the function of CLAP by disrupting the proteolytic balance. | ||||||
MG-132 [Z-Leu- Leu-Leu-CHO] | 133407-82-6 | sc-201270 sc-201270A sc-201270B | 5 mg 25 mg 100 mg | $60.00 $265.00 $1000.00 | 163 | |
MG-132 is an inhibitor of the ubiquitin-proteasome pathway. It can indirectly inhibit CLAP by preventing the degradation of proteins that may regulate the function of CLAP, thus disrupting the proteolytic environment in which CLAP operates. | ||||||
Aprotinin | 9087-70-1 | sc-3595 sc-3595A sc-3595B | 10 mg 100 mg 1 g | $112.00 $408.00 $3000.00 | 51 | |
Aprotinin is a protease inhibitor that primarily inhibits trypsin and plasmin. By inhibiting these proteases, Aprotinin affects the proteolytic pathways, potentially leading to indirect inhibition of CLAP's function by altering the proteolytic balance within the cell. | ||||||
Chymostatin | 9076-44-2 | sc-202541 sc-202541A sc-202541B sc-202541C sc-202541D | 5 mg 10 mg 25 mg 50 mg 100 mg | $156.00 $260.00 $640.00 $1186.00 $2270.00 | 3 | |
Chymostatin is a chymotrypsin inhibitor that can inhibit serine proteases. CLAP's function in proteolytic processing can be indirectly inhibited by Chymostatin through the stabilization of protein substrates and alteration of proteolytic cascades that CLAP may be involved with. | ||||||
Alloxan monohydrate | 2244-11-3 | sc-254940 | 10 g | $54.00 | ||
Alloxan is known to selectively inhibit glucokinase. While not a direct inhibitor of CLAP, it influences glucose metabolism pathways. CLAP, which may interact with or be regulated by proteins involved in these pathways, could be indirectly inhibited by the disruption of metabolic regulation, as protease function can be sensitive to changes in cellular metabolic states. | ||||||