Chemical inhibitors of matriptase-2 include a variety of compounds that target the protein's function in different ways. Silexan operates by inhibiting voltage-gated calcium channels, leading to a decrease in intracellular calcium, which is crucial for the activation of proteases, including matriptase-2. This results in an indirect inhibition of matriptase-2's protease activity. Marimastat and Ilomastat, while primarily matrix metalloprotease (MMP) inhibitors, may also bind to matriptase-2 due to structural similarities between the enzyme's substrates and MMP substrates. This binding inhibits matriptase-2's active site, thus inhibiting its function. Similarly, Gabexate Mesylate and Nafamostat Mesylate inhibit serine proteases by binding to their active sites. This interaction would block matriptase-2's active site, preventing substrate access and thereby inhibiting its proteolytic activity.
Camostat Mesylate also functions as a serine protease inhibitor and could inhibit matriptase-2 by preventing substrate cleavage through active site binding. Aprotinin, another serine protease inhibitor, may inhibit matriptase-2 by a similar mechanism of action. Leupeptin's inhibitory effect on serine proteases could involve binding to matriptase-2's active site and preventing substrate access. E-64, though a specific inhibitor of cysteine proteases, works by irreversible binding to the active site, which could inhibit matriptase-2 if a similar binding occurs. Pepstatin A, an aspartyl protease inhibitor, might exhibit inhibition of matriptase-2 through a structural analogy in binding to the active site. AEBSF, known to covalently modify the serine residue in the active site of serine proteases, can inhibit matriptase-2 by forming a covalent bond with its active site, which would inhibit its proteolytic function. Lastly, Phosphoramidon, although a metalloprotease inhibitor, interacts with the metalloprotease-like domain of matriptase-2, thereby interfering with its function.
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| 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 metalloprotease (MMP) inhibitor. Matriptase-2 is a serine protease that shares some substrate similarities with MMPs. Although Marimastat is not a direct inhibitor of matriptase-2, its structural similarity to MMP substrates could theoretically allow it to bind and inhibit matriptase-2's active site. | ||||||
GM 6001 | 142880-36-2 | sc-203979 sc-203979A | 1 mg 5 mg | $77.00 $270.00 | 55 | |
Ilomastat, like Marimastat, is a matrix metalloprotease inhibitor. Its mechanism of inhibiting MMPs through binding to the zinc-binding site could similarly inhibit matriptase-2 if it were to interact with its active site, which also coordinates a metal ion, although in the case of serine proteases like matriptase-2, it is not zinc. | ||||||
Gabexate mesylate | 56974-61-9 | sc-215066 | 5 mg | $100.00 | ||
Gabexate Mesylate is a serine protease inhibitor that functions by binding to the active sites of various serine proteases. Given that matriptase-2 is also a serine protease, Gabexate Mesylate could inhibit its activity by occupying its active site and preventing substrate access. | ||||||
Nafamostat mesylate | 82956-11-4 | sc-201307 sc-201307A | 10 mg 50 mg | $82.00 $306.00 | 4 | |
Nafamostat Mesylate inhibits various serine proteases through a mechanism involving the formation of a stable complex with the enzyme, which could include matriptase-2, leading to the functional inhibition of its proteolytic activity. | ||||||
Camostat mesylate | 59721-29-8 | sc-203867 sc-203867A sc-203867B sc-203867C sc-203867D sc-203867E | 10 mg 50 mg 500 mg 1 g 10 g 100 g | $43.00 $183.00 $312.00 $624.00 $2081.00 $4474.00 | 5 | |
Camostat Mesylate is a known serine protease inhibitor that can inhibit the enzymatic activity of proteases like matriptase-2 by binding to their active sites, thus preventing substrate cleavage. | ||||||
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. It may inhibit matriptase-2 by binding to its active site due to the similarity in the mechanism of action with other serine proteases, thus blocking its proteolytic function. | ||||||
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 is an inhibitor of cysteine, serine, and threonine peptidases. Its inhibitory action on serine proteases like matriptase-2 would involve binding to the active site, thereby preventing access to the substrate. | ||||||
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 cysteine proteases. While it is specific to cysteine proteases, its mechanism involves irreversible binding to the active site, which, if similar in matriptase-2, could inhibit its activity. | ||||||
AEBSF hydrochloride | 30827-99-7 | sc-202041 sc-202041A sc-202041B sc-202041C sc-202041D sc-202041E | 50 mg 100 mg 5 g 10 g 25 g 100 g | $65.00 $122.00 $428.00 $851.00 $1873.00 $4994.00 | 33 | |
AEBSF is an irreversible serine protease inhibitor that covalently modifies the active site serine residue. This chemical can inhibit matriptase-2 by covalently binding to its active site, rendering it inactive. | ||||||
Phosphoramidon | 119942-99-3 | sc-201283 sc-201283A | 5 mg 25 mg | $199.00 $632.00 | 8 | |
Phosphoramidon is a metalloprotease inhibitor that could potentially interact with the metalloprotease-like domain of matriptase-2, thereby interfering with its proteolytic function despite it not being a classic metalloprotease. | ||||||