Date published: 2025-9-21

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1700027N10Rik Inhibitors

Chemical inhibitors of 1700027N10Rik include a range of compounds that function by disrupting specific signaling pathways integral to the protein's activity. Staurosporine is known for its broad kinase inhibition profile and can interfere with kinase-driven signaling pathways upon which 1700027N10Rik relies for its functional activity. Similarly, Bisindolylmaleimide I, by inhibiting protein kinase C, can impede downstream signaling processes essential for the correct functioning of 1700027N10Rik. Additionally, the inhibition of JNK by SP600125 removes a key regulatory step, potentially leading to a decreased functional activity of 1700027N10Rik. In the same vein, SB203580 targets p38 MAP kinase, a pivotal molecule in a cascade of events that could be crucial for the regulatory mechanisms of 1700027N10Rik.

Moreover, the activity of 1700027N10Rik can be indirectly influenced by chemicals like PD98059 and U0126, which inhibit MEK enzymes, thereby disrupting the ERK pathway signaling that may be essential for 1700027N10Rik's role within the cell. LY294002 and Wortmannin, both inhibitors of PI3K, can attenuate Akt pathway signaling, which can be critical for the mediation of 1700027N10Rik's cellular effects. The inhibitory action of Rapamycin on mTOR signaling pathways can also result in a reduction of 1700027N10Rik's activity due to the close connectivity of mTOR with numerous cellular functions. Src family kinases, targeted by PP2, are another group of enzymes whose inhibition can lead to a decrease in the functional activity of 1700027N10Rik, as they are frequently involved in complex signaling networks within the cell. AG490 exerts its effects by inhibiting JAK2 kinase, thereby impacting the JAK-STAT signaling pathway, which can be of particular significance to the regulatory control of 1700027N10Rik. Lastly, PD173074 targets FGFR, which can perturb the signaling pathways in which 1700027N10Rik is involved, further influencing its activity within the cellular context.

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