Forskolin and IBMX elevate the levels of cyclic nucleotides within the cell, fostering an environment where protein kinases are activated; these kinases can then target and activate LOC729132. Similarly, PMA and ionomycin act on protein kinase C and calcium-dependent kinases, respectively, both of which are capable of modifying the activity of various proteins through phosphorylation. Inhibition of protein phosphatases by compounds such as okadaic acid shifts the phosphorylation equilibrium towards a more phosphorylated and active proteome, which could include LOC729132.
Other compounds like lithium chloride, U0126, SB203580, and SP600125 exert their effects via inhibition of specific kinases within major signaling pathways, such as the Wnt, MAPK/ERK, p38 MAP kinase, and JNK pathways. These pathways are intricately linked to numerous cellular processes and can lead to changes in the phosphorylation status of LOC729132. Metabolic stressors such as 2-deoxy-D-glucose create a cellular environment that can trigger stress response pathways, potentially affecting the activation state of proteins like LOC729132. Similarly, the accumulation of ubiquitinated proteins induced by proteasome inhibitors like MG132 can lead to cellular responses that may indirectly activate LOC729132. All-trans retinoic acid exemplifies a compound that alters gene expression profiles and can modulate signaling pathways, thereby affecting the phosphorylation and activation of diverse proteins, including LOC729132.
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