Date published: 2025-9-14

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EGL-15 Inhibitors

EGL-15 is a protein kinase involved in the regulation of various cellular processes, including cell migration, axon guidance, and synaptic plasticity. It belongs to the Eph receptor family, which plays crucial roles in cell-cell communication and tissue development. To inhibit EGL-15, several chemical inhibitors can be used. Staurosporine is a potent protein kinase inhibitor that can directly inhibit EGL-15 by binding to its active site and preventing the phosphorylation of its target substrates. Similarly, Genistein, a tyrosine kinase inhibitor, can inhibit EGL-15 by blocking the phosphorylation of downstream signaling molecules, disrupting the signaling cascade. In addition to direct inhibitors, several chemicals can indirectly inhibit EGL-15 by influencing related signaling pathways. U0126, PD 98059, and SB 203580 are inhibitors of upstream kinases in the MAPK signaling pathway. By blocking the activation of these kinases, they can disrupt the downstream signaling events involving EGL-15. LY 294002 is a specific inhibitor of phosphatidylinositol 3-kinase (PI3K), a key regulator of the PI3K/AKT signaling pathway. By inhibiting PI3K, LY 294002 can indirectly inhibit EGL-15 by disrupting the activation of downstream targets in the pathway. Furthermore, AG1478 is an EGFR inhibitor that can inhibit EGL-15 by blocking the activation of EGFR and subsequent downstream signaling events. Rapamycin, a known mTOR inhibitor, can inhibit EGL-15 by blocking the activation of mTOR and downstream signalingpathways involved in protein synthesis and cell growth. Curcumin, a natural compound with anti-inflammatory and antioxidant properties, can inhibit EGL-15 by suppressing the activation of NF-κB, a transcription factor involved in inflammatory responses and cell survival. Resveratrol, another natural compound found in grapes and red wine, can inhibit EGL-15 by activating SIRT1, a protein deacetylase that can modulate the activity of various signaling pathways involved in cell proliferation and survival. Tyrphostin B42 is a JAK2 inhibitor that can inhibit EGL-15 by blocking the activation of JAK2 and subsequent downstream signaling events. Lastly, bortezomib is a proteasome inhibitor that can inhibit EGL-15 by preventing the degradation of its target proteins, leading to their accumulation and subsequent disruption of signaling pathways. In summary, EGL-15 inhibitors can directly target the protein kinase activity of EGL-15 or indirectly inhibit its function by influencing related signaling pathways. These inhibitors can disrupt the phosphorylation of downstream targets, block the activation of upstream kinases, inhibit receptor activation, modulate transcription factor activity, or prevent protein degradation. By targeting these crucial steps in the signaling pathways involving EGL-15, these inhibitors can effectively inhibit its function and potentially impact cellular processes such as cell migration, axon guidance, and synaptic plasticity.

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