Date published: 2025-9-13

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TMPRSS11F Inhibitors

TMPRSS11F inhibitors encompass a variety of chemical compounds that target the proteolytic functionality of TMPRSS11F, ultimately leading to its functional inhibition. Camostat Mesylate, Nafamostat Mesylate, and Gabexate Mesylate work by directly inhibiting the serine protease activity, which is central to TMPRSS11F's role in proteolytic cleavage processes. These inhibitors share a mechanism that involves the obstruction of TMPRSS11F's active site, restraining its ability to engage in proteolytic degradation of substrates. AEBSF Hydrochloride operates by irreversibly binding to serine residues within the active site, while Aprotinin and Leupeptin Hemisulfate provide reversible inhibition, forming complexes with TMPRSS11F that prevent substrate access. The inhibition of TMPRSS11F by these compounds is crucial as it impedes the protein's normal function and can affect the protease network within which TMPRSS11F operates.

In addition to direct inhibitors, there are compounds that influence TMPRSS11F activity indirectly by modulating the wider proteolytic environment. Pepstatin A, although primarily an aspartic protease inhibitor, and E-64, a cysteine protease inhibitor, contribute to the overall protease balance and can impact TMPRSS11F function indirectly. Marimastat and Ilomastat, known for their inhibition of matrix metalloproteases, may affect TMPRSS11F indirectly by altering the extracellular matrix, which could influence TMPRSS11F's accessibility or substrate availability. Similarly, Chymostatin acts on chymotrypsin-like serine proteases, which may indirectly reduce TMPRSS11F activity by altering the dynamic equilibrium of the protease network. Phosphoramidon, through its metalloprotease inhibition, could also lead to an indirect downregulation of TMPRSS11F's activity by changing the interactions within the protease cascade. These indirect mechanisms reflect the complex interplay between different protease families and how their inhibition can lead to a cascading effect, ultimately diminishing TMPRSS11F's activity.

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