Date published: 2025-9-17

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TATI Inhibitors

TATI inhibitors, as conceptualized here, focus on the broader spectrum of protease inhibitors that can indirectly influence TATI's biological activity. These compounds are generally classified based on the type of protease they inhibit, including serine, cysteine, aspartyl, and metalloproteases. Since TATI itself is a protease inhibitor, the use of synthetic or naturally occurring protease inhibitors may affect the biological context in which TATI operates, altering its activity or expression levels. The inhibitors listed, such as aprotinin and gabexate mesilate, primarily target serine proteases, which are the types of proteases that TATI might naturally inhibit. By providing these inhibitors, the functional necessity for TATI could be modulated, thereby impacting its biological role. Other inhibitors, like E-64 and pepstatin A, target different classes of proteases (cysteine and aspartyl proteases, respectively), and their use can change the proteolytic balance within the cell, possibly affecting pathways wherein TATI is a participant.

Metalloprotease inhibitors such as phosphoramidon, marimastat, and batimastat represent another class of compounds that can have an indirect impact on TATI's regulatory functions. These inhibitors could modulate the extracellular matrix turnover and cell signaling, which may indirectly influence the activity and significance of TATI in various physiological and pathological processes.

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