Date published: 2025-9-12

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TTC23L Activators

TTC23L activators encompass a diverse array of compounds that exert their effects through various signaling pathways, ultimately leading to the enhanced functional activity of TTC23L. For instance, some activators work by directly stimulating enzymes like adenylate cyclase, thereby increasing the levels of intracellular second messengers such as cAMP. This rise in cAMP levels activates protein kinase A, a kinase that could phosphorylate and activate proteins within the pathways that TTC23L is a part of, thereby potentially enhancing its activity. Other activators function by inhibiting phosphodiesterases, resulting in sustained cAMP levels and similar enhancement of PKA activity. Additionally, there are activators that target protein kinase C, which can phosphorylate substrates that interact with TTC23L, thereby influencing its activity. There are also compounds that modulate intracellular calcium levels, which could activate calcium-dependent kinases that have the potential to impact TTC23L function.

Some TTC23L activators operate by altering the phosphorylation state of proteins within TTC23L's associated pathways. For example, inhibitors of protein phosphatases such as PP1 and PP2A result in an increased phosphorylation of proteins, which could subsequently enhance the activity of TTC23L. Certain ionophores raise intracellular calcium levels, potentially affecting the activity of calcium-dependent kinases that may interact with TTC23L. Furthermore, modulation of energy balance signaling by AMPK activators could have implications for TTC23L activity. Other activators include cAMP analogs that permeate cells and directly activate PKA, as well as compounds that influence gene expression through receptor activation, potentially leading to the activation of proteins that enhance TTC23L function.

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