PRB4 Activators
Chemical activators of PRB4 can initiate a cascade of intracellular processes leading to its phosphorylation and subsequent activation. Phorbol 12-myristate 13-acetate (PMA) is a potent activator of protein kinase C (PKC), a kinase that can directly phosphorylate PRB4. The activation of PKC by PMA is a well-documented pathway for the modulation of proteins through phosphorylation. Similarly, forskolin raises intracellular cAMP levels, which in turn activates protein kinase A (PKA). PKA then phosphorylates PRB4, leading to activation. The cAMP-PKA signaling axis is a classical route for the regulation of protein function within cells. Additionally, ionomycin, by increasing intracellular calcium levels, initiates the activation of calmodulin-dependent kinases (CaMKs), which are then able to phosphorylate PRB4. Elevated calcium levels are a universal signal in cellular activation processes, impacting numerous proteins such as PRB4.
Further chemical influences on PRB4 activation involve a variety of signaling pathways and regulatory mechanisms. The binding of Epidermal Growth Factor (EGF) to its receptor triggers the MAPK/ERK pathway, which can result in the phosphorylation of PRB4, an essential step for many proteins involved in cellular proliferation and differentiation. Thapsigargin, through the inhibition of the sarco/endoplasmic reticulum Ca2+-ATPase (SERCA), indirectly raises cytosolic calcium levels and thus activates kinases that target PRB4. Arachidonic Acid, metabolized into eicosanoids, activates PKA and PKC, both of which can phosphorylate PRB4. Phosphatidic Acid, participating in the mTOR signaling pathway, leads to the activation of proteins by phosphorylation, including PRB4. Inhibitors of protein phosphatases, such as Okadaic Acid and Calyculin A, prevent dephosphorylation, thereby maintaining PRB4 in an activated state. Anisomycin triggers the stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) pathway, which can phosphorylate and activate PRB4 as part of a cellular stress response. Lastly, Cantharidin, by inhibiting protein phosphatases like PP2A, contributes to the sustained activation of PRB4 by preventing its dephosphorylation. These diverse chemical activators, through their unique mechanisms, all converge on the common endpoint of PRB4 activation, exemplifying the intricate web of cellular regulation.
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
PMA | 16561-29-8 | sc-3576 sc-3576A sc-3576B sc-3576C sc-3576D | 1 mg 5 mg 10 mg 25 mg 100 mg | $40.00 $129.00 $210.00 $490.00 $929.00 | 119 | |
Phorbol 12-myristate 13-acetate (PMA) activates protein kinase C (PKC) which can then phosphorylate PRB4, leading to its activation. PKC is a known regulatory kinase for many proteins, and phosphorylation by PKC is a common mechanism for protein activation. | ||||||
Forskolin | 66575-29-9 | sc-3562 sc-3562A sc-3562B sc-3562C sc-3562D | 5 mg 50 mg 1 g 2 g 5 g | $76.00 $150.00 $725.00 $1385.00 $2050.00 | 73 | |
Forskolin increases intracellular cAMP levels, which activates protein kinase A (PKA). PKA can phosphorylate PRB4, which is a regulatory mechanism for its activation. Increased cAMP is a well-established second messenger that activates PKA, leading to downstream protein phosphorylation and activation. | ||||||
Ionomycin | 56092-82-1 | sc-3592 sc-3592A | 1 mg 5 mg | $76.00 $265.00 | 80 | |
Ionomycin functions by increasing intracellular calcium concentrations, leading to the activation of calmodulin-dependent kinases (CaMKs). These kinases can phosphorylate PRB4, thus activating it. Calcium signaling is a universal mechanism by which cellular functions are regulated, and proteins like PRB4 can be activated in response to such signals. | ||||||
Thapsigargin | 67526-95-8 | sc-24017 sc-24017A | 1 mg 5 mg | $94.00 $349.00 | 114 | |
Thapsigargin inhibits the sarco/endoplasmic reticulum Ca2+-ATPase (SERCA), causing a rise in cytosolic calcium levels. The increase in calcium levels can activate kinases that phosphorylate PRB4, leading to its activation. This mechanism is an indirect way to increase the concentration of intracellular calcium, which then activates calcium-responsive proteins and kinases. | ||||||
Arachidonic Acid (20:4, n-6) | 506-32-1 | sc-200770 sc-200770A sc-200770B | 100 mg 1 g 25 g | $90.00 $235.00 $4243.00 | 9 | |
Arachidonic Acid metabolism produces eicosanoids, which activate protein kinase A (PKA) and protein kinase C (PKC). Both PKA and PKC can phosphorylate and thus activate PRB4. Arachidonic Acid serves as a precursor for signaling molecules that are known to activate kinases involved in the phosphorylation of proteins. | ||||||
Phosphatidic Acid, Dipalmitoyl | 169051-60-9 | sc-201057 sc-201057B sc-201057A | 100 mg 250 mg 500 mg | $104.00 $239.00 $409.00 | ||
Phosphatidic Acid is involved in the mTOR signaling pathway, which is known to phosphorylate and activate numerous proteins, including PRB4. The mTOR pathway is integral for cell growth and metabolism and its activation leads to the phosphorylation of downstream proteins. | ||||||
Okadaic Acid | 78111-17-8 | sc-3513 sc-3513A sc-3513B | 25 µg 100 µg 1 mg | $285.00 $520.00 $1300.00 | 78 | |
Okadaic Acid inhibits protein phosphatases PP1 and PP2A, leading to an increase in phosphorylated proteins due to reduced dephosphorylation. As a result, proteins like PRB4 that are regulated by phosphorylation remain activated. The inhibition of phosphatases can result in the sustained activation of proteins that are normally regulated by phosphorylation cycles. | ||||||
Calyculin A | 101932-71-2 | sc-24000 sc-24000A sc-24000B sc-24000C | 10 µg 100 µg 500 µg 1 mg | $160.00 $750.00 $1400.00 $3000.00 | 59 | |
Similar to Okadaic Acid, Calyculin A is an inhibitor of protein phosphatases such as PP1 and PP2A. By inhibiting these phosphatases, Calyculin A induces an increase in the phosphorylation and consequent activation of proteins like PRB4 that are regulated by phosphorylation status. | ||||||
Anisomycin | 22862-76-6 | sc-3524 sc-3524A | 5 mg 50 mg | $97.00 $254.00 | 36 | |
Anisomycin activates the stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) pathway, which can lead to the phosphorylation and activation of various proteins, including PRB4. The activation of this pathway is a response to stress stimuli and can result in the activation of proteins involved in the stress response. | ||||||
Cantharidin | 56-25-7 | sc-201321 sc-201321A | 25 mg 100 mg | $81.00 $260.00 | 6 | |
Cantharidin inhibits protein phosphatases, particularly PP2A, which leads to increased phosphorylation levels of proteins. Proteins like PRB4, when not dephosphorylated due to the inhibition of phosphatases, remain in an activated state. This inhibition of protein phosphatases can result in the functional activation of proteins regulated by phosphorylation. | ||||||