Date published: 2025-9-15

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OR1L8 Activators

Forskolin raises cAMP levels, thereby activating protein kinase A. This activation can lead to phosphorylation events within the cell that may affect OR1L8. Similarly, A-23187 acts as a calcium ionophore, increasing the intracellular concentration of calcium ions, which are pivotal in numerous signaling cascades, thus potentially affecting OR1L8's state of activity. Compounds that inhibit specific kinases or phosphatases, such as PD98059 and U0126, which are MEK inhibitors, and SB 203580, a p38 MAP kinase inhibitor. These inhibitors can alter the activity of proteins in the MAPK/ERK pathway, which is closely related to the regulation of numerous proteins, possibly including OR1L8. The presence of kinase inhibitors like KN-62 and Gö 6983, which target Ca2+/calmodulin-dependent protein kinases and PKC isozymes, respectively, suggests that OR1L8 may be regulated through pathways associated with these kinases.

Protein phosphatase inhibitors like Calyculin A and Okadaic Acid also feature in this class, preserving the phosphorylation state of proteins, which is a crucial aspect of protein function and signaling. Phosphorylation status can significantly influence protein interactions and signaling pathways that OR1L8 may be a part of. Meanwhile, compounds like Genistein exert their effects by inhibiting protein tyrosine kinases, thereby influencing tyrosine phosphorylation within cells. Zn2+ serve as signaling molecules, having the capacity to interact with a variety of molecular pathways, including those that govern the activity of proteins like OR1L8.

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