Date published: 2025-10-31

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LOC728379 Activators

LOC728379 Activators encompass a spectrum of chemical compounds that indirectly stimulate the functional activity of the deubiquitinating enzyme LOC728379 through diverse signaling pathways. Forskolin, by increasing cAMP concentrations, indirectly influences LOC728379 by activating PKA, which can impact proteins that modulate LOC728379's activity. Similarly, PMA, by activating PKC, could lead to phosphorylation of proteins that interact with LOC728379, potentially enhancing its deubiquitination function. Ionomycin raises intracellular Ca2+ levels, which could activate calcium-dependent proteases and protein interactions, indirectly affecting LOC728379 activity. LY294002 and U0126, by inhibiting PI3K and MEK1/2 respectively, modulate pathways that could shift cellular proteostasis and indirectly augment the functional activity ofLOC728379. Additionally, Epigallocatechin gallate (EGCG), acting as a tyrosine kinase inhibitor, may reduce competitive signaling, possibly leading to an enhanced role for LOC728379 in protein stability regulation.

LOC728379's activity is further influenced by compounds that affect various cellular signaling processes. MG132, by inhibiting the proteasome, could increase the pool of ubiquitinated proteins, potentially raising the functional demand for LOC728379's deubiquitinating activity. The nitric oxide donor, S-Nitroso-N-acetylpenicillamine (SNAP), may indirectly promote LOC728379's activity by affecting protein modification pathways. Okadaic acid's inhibition of protein phosphatases PP1 and PP2A could indirectly enhance LOC728379 activity by affecting the phosphorylation state of proteins that interact with it. Thapsigargin, by inhibiting SERCA pumps, increases cytosolic calcium levels, which may influence LOC728379 activity through calcium-dependent signaling pathways. Staurosporine, despite being a broad kinase inhibitor, might selectively activate pathways related to LOC728379 by altering the phosphorylation landscape. Lastly, 5-Azacytidine could lead to changes in gene expression that indirectly increase LOC728379 activity by affecting the cellular levels of interacting or regulatory proteins, highlighting a complex network of intracellular signals that collectively facilitate the enhancement of LOC728379's functional role in deubiquitination without the need for direct activation or upregulation of its expression.

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