Date published: 2025-9-19

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HEATR8 Activators

HEATR8 activators are a class of chemical compounds that modulate the activity of HEAT Repeat-containing protein 8 (HEATR8), a part of the intricate network of proteins that regulate various cellular functions. These activators work through diverse mechanisms to influence the phosphorylation state and conformation of HEATR8, thereby altering its activity. The modulation of HEATR8 by these activators is achieved through the manipulation of intracellular signaling pathways and biochemical processes. For example, compounds like Forskolin exert their effect by directly stimulating adenylate cyclase, which increases the levels of cyclic AMP (cAMP) within the cell. The elevated cAMP in turn activates protein kinase A (PKA), a key player in the phosphorylation of proteins, including HEATR8. This phosphorylation can lead to conformational changes in HEATR8, potentially enhancing its activity. Similarly, IBMX works by inhibiting phosphodiesterases, enzymes that break down cAMP, which results in the indirect increase of cAMP levels and subsequent activation of PKA, following a pathway parallel to that of Forskolin.

Other molecules within the HEATR8 activators class operate through different cellular mechanisms. PMA, for instance, directly activates protein kinase C (PKC), which is involved in a plethora of signaling cascades, and its activation can lead to the phosphorylation and activation of HEATR8 as part of downstream signaling. Ionomycin increases intracellular calcium levels, which can also activate calcium-dependent protein kinases, including PKC, potentially affecting the activity of HEATR8. Additionally, Okadaic Acid, by inhibiting protein phosphatases PP1 and PP2A, prevents the dephosphorylation of proteins, which can result in the enhanced activity of HEATR8 due to sustained phosphorylation. Lithium Chloride, on another front, inhibits glycogen synthase kinase-3 (GSK-3), a negative regulator in many signaling pathways, and its inhibition might indirectly result in the upregulation of HEATR8 activity.

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