Date published: 2025-9-18

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SUHW4 Activators

SUHW4 activators encompass a variety of chemical compounds that indirectly facilitate the functional activity of SUHW4 through their influence on cellular signaling pathways and transcriptional regulation mechanisms. Forskolin, by increasing cAMP levels and consequently activating PKA, primes the phosphorylation landscape to potentially favor SUHW4's role in gene expression modulation. Similarly, PMA activates PKC, which may enhance SUHW4's activity through phosphorylation or alterations in the cellular milieu. Sphingosine-1-phosphate can initiate signaling cascades that enhance the activity of nuclear receptors, potentially including SUHW4, while Ionomycin, by increasing intracellular calcium, activates calcium-dependent pathways that could augment SUHW4's transcriptional regulation functions. The cAMP analog 8-Bromo-cAMP also activates PKA, implying a similar potential for enhancing SUHW4 activity, and Oligomycin, by inhibiting mitochondrial ATP synthase, indirectly activates AMPK, which may modulate SUHW4 activity in response to the cellular energy state.

Further, activators such as EGCG can influence various signaling pathways and affect SUHW4's interaction with other molecular players or its phosphorylation status. LY294002, by inhibiting PI3K, can alter the AKT signaling pathway, impacting the transcriptional context in which SUHW4 operates. Rapamycin, through mTOR inhibition, affects cellular growth signals,potentially leading to enhanced SUHW4 activity through altered gene expression networks. SB203580 and U0126, which inhibit p38 MAPK and MEK1/2 respectively, could shift the balance of intracellular signaling to pathways that favor the activation of SUHW4. Furthermore, Trichostatin A, by inhibiting HDACs, could increase chromatin accessibility for SUHW4, enhancing its capacity to regulate gene expression. Collectively, these compounds contribute to the creation of a cellular environment conducive to the activation and potentiation of SUHW4's role in the regulation of gene expression, without directly increasing its expression or requiring direct activation of the protein.

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