Date published: 2025-9-12

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CCP4 Inhibitors

Chemical inhibitors of CCP4 can exert their inhibitory effects through various mechanisms that interfere with the protein's function or the signaling pathways it is involved with. Marimastat, a broad-spectrum metalloproteinase inhibitor, can inhibit metalloproteinases that CCP4 may rely on for its functional interactions, thus impeding CCP4's role in proteolytic processes. Similarly, O-Phenanthroline can disrupt CCP4-related activities by chelating metal ions essential for the enzymatic activity of metalloproteinases. Inhibition of enzyme activities that are upstream or in the same pathway as CCP4 can lead to a reduction in the functional activity of CCP4 itself. For example, Captopril, primarily known as an angiotensin-converting enzyme (ACE) inhibitor, can reduce the activity of ACE and its related pathways, thereby possibly reducing interactions and functions of CCP4 linked to this system.

Further, the MAPK/ERK pathway, which is crucial for cell proliferation and survival, can be inhibited by PD98059 and U0126, both of which target MEK, potentially leading to decreased CCP4 activity related to this pathway. LY294002 and Wortmannin are PI3K inhibitors and can inhibit the PI3K/Akt pathway, which may be vital for CCP4's role in cellular signaling processes. SP600125, a JNK inhibitor, and SB203580, a p38 MAPK inhibitor, can reduce CCP4 activity connected to stress response pathways by inhibiting these kinases. Rapamycin, by inhibiting mTOR, can affect CCP4's functionality within mTOR signaling pathways, which are key in cell growth and metabolism. GF109203X, a PKC inhibitor, can alter CCP4 activity related to PKC-mediated signaling pathways. Lastly, Trichostatin A, by inhibiting histone deacetylase, can disrupt gene expression patterns, potentially leading to a decrease in CCP4 activity if CCP4's function is closely tied to gene expression regulated by acetylation. Each of these inhibitors targets specific enzymes or pathways, leading to a reduction in the functional activity of CCP4 by either directly inhibiting its action or by altering signaling pathways that CCP4 is known to be involved with.

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