SPOPL Activators
SPOPL activators pertain to a class of chemical compounds that target the SPOPL (speckle-type POZ protein-like) protein, which is a part of the ubiquitin-proteasome system (UPS). The UPS is a pivotal pathway in cellular function that regulates the turnover of proteins and maintains cellular homeostasis. Proteins that are earmarked for degradation are tagged with ubiquitin molecules, and this tagging is often mediated by E3 ubiquitin ligases, among which SPOPL can be classified. SPOPL specifically recognizes and binds to substrates via its substrate recognition domain, and subsequently, it facilitates the transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to the target protein, marking it for degradation by the proteasome. Activators of SPOPL enhance its activity, increasing the ubiquitination of its substrate proteins.
The significance of SPOPL activators lies in their ability to modulate protein levels within the cell by increasing the efficiency of the ubiquitination process. By activating SPOPL, these compounds can influence the degradation rate of proteins that are implicated in various cellular pathways. The fine-tuning of protein ubiquitination has profound effects on cellular processes such as signal transduction, cell cycle progression, and gene expression. SPOPL itself has been identified to have specific substrates that, when ubiquitinated, can affect the dynamics of cellular growth and the maintenance of genomic integrity. As such, the study and development of SPOPL activators is an area of interest for biochemical research, focusing on elucidating the underlying mechanisms that govern protein turnover and how these processes can be precisely controlled by targeted activation of key components like SPOPL within the UPS.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
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 is an activator of adenylate cyclase, leading to an increase in cyclic AMP (cAMP) levels. Elevated cAMP activates protein kinase A (PKA), which can phosphorylate target proteins. SPOPL could be activated by PKA-mediated phosphorylation, leading to enhanced ubiquitination of its substrates involved in signal transduction pathways. | ||||||
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 | |
PMA is a potent activator of protein kinase C (PKC), which phosphorylates a variety of protein targets. PKC-mediated phosphorylation may enhance the activity of SPOPL by promoting its interaction with specific substrates or by stabilizing the protein, thereby increasing its functional activity. | ||||||
Ionomycin | 56092-82-1 | sc-3592 sc-3592A | 1 mg 5 mg | $76.00 $265.00 | 80 | |
Ionomycin is a calcium ionophore that increases intracellular calcium concentrations. Elevated calcium levels can activate calmodulin-dependent kinase (CaMK), which potentially could phosphorylate SPOPL or its interacting partners, enhancing SPOPL's functional activity in ubiquitination processes. | ||||||
(−)-Epigallocatechin Gallate | 989-51-5 | sc-200802 sc-200802A sc-200802B sc-200802C sc-200802D sc-200802E | 10 mg 50 mg 100 mg 500 mg 1 g 10 g | $42.00 $72.00 $124.00 $238.00 $520.00 $1234.00 | 11 | |
EGCG is known to inhibit several protein kinases, potentially leading to altered phosphorylation states of proteins within SPOPL's signaling network. By inhibiting upstream kinases, EGCG may enhance SPOPL activity indirectly by reducing negative regulatory phosphorylation events, thus promoting its role in proteasomal degradation. | ||||||
Dibutyryl-cAMP | 16980-89-5 | sc-201567 sc-201567A sc-201567B sc-201567C | 20 mg 100 mg 500 mg 10 g | $45.00 $130.00 $480.00 $4450.00 | 74 | |
db-cAMP is a cell-permeable cAMP analog that activates PKA. By enhancing PKA activity, db-cAMP can improve SPOPL phosphorylation status, leading to increased SPOPL-mediated ubiquitination and proteasomal degradation of specific cellular 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 is a potent inhibitor of protein phosphatases PP1 and PP2A. By preventing dephosphorylation, okadaic acid could maintain SPOPL in a phosphorylated state, thereby enhancing its activity. This could increase the ubiquitination and degradation of certain proteins, contingent on SPOPL's role in the ubiquitin-proteasome pathway. | ||||||
Calyculin A | 101932-71-2 | sc-24000 sc-24000A | 10 µg 100 µg | $160.00 $750.00 | 59 | |
Calyculin A, like okadaic acid, inhibits protein phosphatases. By inhibiting the dephosphorylation process, calyculin A could indirectly enhance SPOPL activity by maintaining its phosphorylation state, promoting the ubiquitination of proteins within SPOPL's functional scope. | ||||||
LY 294002 | 154447-36-6 | sc-201426 sc-201426A | 5 mg 25 mg | $121.00 $392.00 | 148 | |
LY294002 is a PI3K inhibitor that can lead to decreased Akt phosphorylation. Inhibition of the PI3K/Akt pathway might relieve negative feedback on upstream RTK signaling, which can indirectly increase SPOPL activity if SPOPL is involved in the degradation of proteins downstream of these receptors. | ||||||
PF 4708671 | 1255517-76-0 | sc-361288 sc-361288A | 10 mg 50 mg | $175.00 $700.00 | 9 | |
PF-4708671 is a selective inhibitor of the p70 S6 kinase (S6K1). By inhibiting S6K1, this compound could alter the protein synthesis machinery, potentially affecting SPOPL's substrates' stability and enhancing SPOPL-mediated protein degradation. | ||||||
Rapamycin | 53123-88-9 | sc-3504 sc-3504A sc-3504B | 1 mg 5 mg 25 mg | $62.00 $155.00 $320.00 | 233 | |
Rapamycin inhibits mTOR, which plays a central role in regulating protein synthesis and degradation. By inhibiting mTOR, rapamycin could enhance SPOPL's role in the degradation of proteins through the ubiquitin-proteasome system, as SPOPL might be involved in targeting proteins that are regulated by mTOR signaling. | ||||||