KLKb2 Inhibitors
Chemical inhibitors of KLKb2 include a variety of compounds that impede the protein's function through different mechanisms of action. Aprotinin acts by forming a complex with the protease domain of KLKb2, thereby obstructing the active site and preventing it from engaging with peptide substrates. Similarly, Benzamidine competes with natural substrates for binding to the active site of KLKb2, achieving inhibition by mimicking substrate structure. AEBSF inhibits KLKb2 irreversibly by covalently attaching to the serine residue within the active site, which is crucial for the enzyme's proteolytic activity. Leupeptin, on the other hand, reversibly binds to the active site and blocks the hydrolysis of peptide bonds, thus inhibiting KLKb2 activity.
Gabexate and Camostat both mimic the transition state of peptide bond hydrolysis to occupy the active site of KLKb2, resulting in the prevention of the protein's interaction with its substrates and subsequent inhibition of its function. Nafamostat also binds to the active site in a similar fashion to Camostat, preventing substrate cleavage and subsequently inhibiting the enzymatic activity of KLKb2. Chymostatin operates by occupying the active site to prevent the proteolytic activity of KLKb2. Soybean trypsin inhibitor (SBTI) directly targets KLKb2 by binding to its active site, inhibiting the enzyme's ability to process substrates. E-64, although typically inhibiting cysteine proteases, can inhibit KLKb2 by irreversibly binding to its active site due to the broad specificity of the protease, leading to inhibited catalytic function. Pepstatin A, which is generally an aspartic protease inhibitor, can inhibit KLKb2 by binding to its active site. Finally, Phosphoramidon may inhibit KLKb2 by chelating metal ions essential for the structural integrity of the protease or for substrate binding, thereby inhibiting the proteolytic function of the protein. Each of these chemicals targets the proteolytic activity of KLKb2 through specific interactions with the active site or essential structural components of the enzyme, leading to functional inhibition.
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Items 1 to 10 of 11 total
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Aprotinin | 9087-70-1 | sc-3595 sc-3595A sc-3595B | 10 mg 100 mg 1 g | $110.00 $400.00 $1615.00 | 51 | |
Aprotinin is a protease inhibitor that can inhibit KLKb2 by forming a stable complex with the protease domain of the protein, thereby blocking access to the active site and preventing the cleavage of peptide substrates. | ||||||
Benzamidine | 618-39-3 | sc-233933 | 10 g | $286.00 | 1 | |
Benzamidine acts as a competitive inhibitor of KLKb2 by mimicking the structure of the substrates and binding to the active site, which inhibits the protein's enzymatic activity in cleaving its natural peptide substrates. | ||||||
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 | $50.00 $120.00 $420.00 $834.00 $1836.00 $4896.00 | 33 | |
AEBSF irreversibly inhibits KLKb2 by covalently binding to the serine residue in the active site of the enzyme, which is essential for its protease activity, thereby leading to a loss of 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 | $72.00 $145.00 $265.00 $489.00 $1399.00 $99.00 | 19 | |
Leupeptin inhibits KLKb2 by reversibly binding to its active site and preventing the hydrolysis of peptide bonds in substrates, thus inhibiting the proteolytic activity of the protein. | ||||||
Gabexate mesylate | 56974-61-9 | sc-215066 | 5 mg | $100.00 | ||
Gabexate mimics the transition state of peptide bond hydrolysis, allowing it to bind to the active site of KLKb2, which prevents the protein from interacting with its natural substrates and inhibits its function. | ||||||
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 | $42.00 $179.00 $306.00 $612.00 $2040.00 $4386.00 | 5 | |
Camostat inhibits KLKb2 by binding to its active site, therefore blocking substrate access and inhibiting the proteolytic activity of the enzyme, which is critical for its function. | ||||||
Nafamostat mesylate | 82956-11-4 | sc-201307 sc-201307A | 10 mg 50 mg | $80.00 $300.00 | 4 | |
Nafamostat, like Camostat, binds to the active site of KLKb2, thereby preventing substrate cleavage and inhibiting the enzymatic activity of the protein. | ||||||
Chymostatin | 9076-44-2 | sc-202541 sc-202541A sc-202541B sc-202541C sc-202541D | 5 mg 10 mg 25 mg 50 mg 100 mg | $153.00 $255.00 $627.00 $1163.00 $2225.00 | 3 | |
Chymostatin inhibits KLKb2 by binding to its active site, which effectively prevents the enzyme from catalyzing the hydrolysis of peptide bonds in its substrates, thus inhibiting the protein's function. | ||||||
Trypsin Inhibitor, soybean | 9035-81-8 | sc-29129 sc-29129A sc-29129B sc-29129C sc-29129D sc-29129F sc-29129E | 50 mg 250 mg 1 g 5 g 10 g 25 g 100 g | $36.00 $129.00 $262.00 $940.00 $1499.00 $2580.00 $10200.00 | 14 | |
Soybean trypsin inhibitor (SBTI) targets KLKb2 directly by occupying the active site and blocking the entry of substrates, which in turn inhibits the proteolytic activity of the enzyme. | ||||||
E-64 | 66701-25-5 | sc-201276 sc-201276A sc-201276B | 5 mg 25 mg 250 mg | $275.00 $928.00 $1543.00 | 14 | |
E-64 can inhibit KLKb2 activity by irreversibly binding to the active site, despite being a cysteine protease inhibitor, due to the protease's broad specificity, resulting in a decrease in the protein's catalytic function. | ||||||