PPP1R36 activators comprise a diverse group of chemical compounds that modulate the activity of protein phosphatase 1, regulatory subunit 36 (PPP1R36), a component of the protein phosphatase 1 (PP1) complex. This complex plays a crucial role in cellular processes by reversing the phosphorylation of serine and threonine residues on proteins, which is a post-translational modification that can alter the function, localization, and interaction of proteins within the cell. The activators of PPP1R36 do not directly stimulate the regulatory subunit but rather influence the phosphorylation state of proteins that PPP1R36 may bind to or regulate. These compounds achieve this modulation through a variety of mechanisms, each interacting with different molecular pathways to indirectly affect the activity of PPP1R36. Some activators, such as Okadaic Acid and Calyculin A, are known to inhibit PP1, leading to an overall increase in the phosphorylated forms of proteins within the cell. This increase in phosphorylation can, in turn, augment the availability of substrates that PPP1R36 may act upon.
The significance of these activators lies in their ability to alter the dynamics of protein phosphorylation, which is a critical regulatory mechanism in cells. By affecting the enzyme's substrate availability or the interaction between PPP1R36 and its protein targets, these compounds can influence the functional state of PPP1R36. For example, agents that upregulate intracellular cAMP levels, such as Forskolin, indirectly promote PPP1R36 activity by activating protein kinase A (PKA), which can then phosphorylate proteins that are potential substrates for PPP1R36. Other activators work by different mechanisms: Phorbol 12-myristate 13-acetate (PMA) functions by activating protein kinase C (PKC), which phosphorylates a broad range of proteins, potentially altering the substrate recognition by PPP1R36. Ionomycin, a calcium ionophore, can elevate intracellular calcium concentrations, thereby activating calcium-dependent calmodulin kinases (CaMKs) which also phosphorylate numerous cellular proteins.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Okadaic Acid | 78111-17-8 | sc-3513 sc-3513A sc-3513B | 25 µg 100 µg 1 mg | $291.00 $530.00 $1800.00 | 78 | |
Okadaic Acid is a potent inhibitor of protein phosphatases, including PP1. By inhibiting PP1, it indirectly increases the phosphorylation levels of proteins, which may enhance the functional activity of protein phosphatase 1, regulatory subunit 36 (PPP1R36) by increasing its substrate availability. | ||||||
Calyculin A | 101932-71-2 | sc-24000 sc-24000A | 10 µg 100 µg | $163.00 $800.00 | 59 | |
Calyculin A, like Okadaic Acid, is an inhibitor of serine/threonine protein phosphatases, including PP1. Its action leads to an increase in protein phosphorylation by preventing PP1 activity, potentially enhancing PPP1R36 activity as a regulatory subunit by promoting its binding to phosphorylated substrates. | ||||||
PMA | 16561-29-8 | sc-3576 sc-3576A sc-3576B sc-3576C sc-3576D | 1 mg 5 mg 10 mg 25 mg 100 mg | $41.00 $132.00 $214.00 $500.00 $948.00 | 119 | |
PMA activates protein kinase C (PKC), which phosphorylates a wide array of substrates. PKC-mediated phosphorylation can influence the binding affinity of PPP1R36 to its substrates, thereby enhancing its regulatory function. | ||||||
Ionomycin | 56092-82-1 | sc-3592 sc-3592A | 1 mg 5 mg | $78.00 $270.00 | 80 | |
Ionomycin is a calcium ionophore that increases intracellular calcium levels, which can activate calmodulin-dependent protein kinase (CaMK). Activated CaMK can phosphorylate substrates, potentially enhancing the regulatory function of PPP1R36 by modulating its substrate interactions. | ||||||
Lithium | 7439-93-2 | sc-252954 | 50 g | $214.00 | ||
Lithium inhibits glycogen synthase kinase-3 (GSK-3), leading to increased protein phosphorylation. By altering the phosphorylation landscape, lithium can indirectly enhance the regulatory role of PPP1R36. | ||||||
Tunicamycin | 11089-65-9 | sc-3506A sc-3506 | 5 mg 10 mg | $172.00 $305.00 | 66 | |
Tautomycin is another inhibitor of PP1 and PP2A phosphatases, leading to an accumulation of phosphorylated proteins. This increase in phosphorylated substrates may enhance the activity of PPP1R36 by increasing its functional interactions with these proteins. | ||||||
Cantharidin | 56-25-7 | sc-201321 sc-201321A | 25 mg 100 mg | $89.00 $279.00 | 6 | |
Cantharidin inhibits serine/threonine protein phosphatases, including PP1. By preventing PP1-mediated dephosphorylation, cantharidin indirectly enhances the functional activity of PPP1R36 through increased phosphorylated protein interactions. | ||||||
Endothall | 145-73-3 | sc-201325 sc-201325A | 20 mg 100 mg | $49.00 $203.00 | 1 | |
Endothall is a PP1 and PP2A inhibitor, which leads to higher levels of protein phosphorylation. This elevated phosphorylation status can enhance PPP1R36 activity by increasing the regulatory subunit's engagement with phosphorylated targets. | ||||||
Roscovitine | 186692-46-6 | sc-24002 sc-24002A | 1 mg 5 mg | $94.00 $265.00 | 42 | |
Roscovitine is a cyclin-dependent kinase inhibitor (CDKi), leading to altered phosphorylation patterns in the cell. Altered CDK activity can indirectly enhance PPP1R36 activity by affecting the phosphorylation status of proteins that interact with PPP1R36. | ||||||
Zoledronic acid, anhydrous | 118072-93-8 | sc-364663 sc-364663A | 25 mg 100 mg | $92.00 $256.00 | 5 | |
Zoledronic Acid inhibits farnesyl pyrophosphate synthase, leading to altered prenylation of proteins. This can affect the localization and function of proteins, indirectly enhancing PPP1R36 activity by modifying its protein-protein interactions. | ||||||