ZNF323 Activators
Chemical activators of ZNF323 can influence its activity through various signaling pathways that lead to its phosphorylation and subsequent functional activation. Phorbol 12-myristate 13-acetate (PMA) is one such activator that targets the protein kinase C (PKC) pathway. Activation of PKC can result in the phosphorylation of proteins that interact with ZNF323, enhancing its DNA-binding capability and transcriptional regulation functions. Similarly, forskolin raises intracellular cAMP levels, which, in turn, activate protein kinase A (PKA). PKA can phosphorylate transcription factors and regulatory proteins associated with ZNF323, potentially increasing its activity. Ionomycin also plays a role in this regulatory network by increasing intracellular calcium concentrations, which activate calcium/calmodulin-dependent protein kinases that can phosphorylate and activate ZNF323.
Further modulation of ZNF323 activity can occur through the inhibition of protein phosphatases by chemicals like okadaic acid and calyculin A. These compounds maintain proteins in a phosphorylated state by inhibiting phosphatases such as PP1 and PP2A, which may enhance the transcriptional activity of ZNF323. In parallel, spermine can enhance kinase activity, which includes kinases responsible for phosphorylating ZNF323 or its associated proteins, leading to its activation. Epidermal Growth Factor (EGF) and insulin are also key players, with EGF activating the MAPK/ERK pathway and insulin activating the PI3K/Akt pathway. Both pathways involve cascades of protein kinases that can lead to ZNF323 phosphorylation and activation. Additionally, dibutyryl-cAMP (db-cAMP), a cAMP analog, activates PKA, further contributing to the phosphorylation and functional activation of ZNF323. Bryostatin 1 and anisomycin activate PKC and the stress-activated protein kinase pathway respectively, both of which can lead to phosphorylation events that enhance the activity of ZNF323. Through these complex signaling networks, ZNF323 becomes an active participant in the regulation of transcription.
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| 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 | |
PMA activates protein kinase C (PKC), which is involved in signaling pathways that lead to activation of certain transcription factors. Given that ZNF323 is a zinc finger protein, which often plays a role in DNA binding and transcriptional regulation, the activation of PKC can lead to phosphorylation events that promote ZNF323's binding affinity or its interaction with other co-regulatory proteins, resulting in functional activation of ZNF323. | ||||||
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 directly stimulates adenylyl cyclase, increasing the levels of cAMP, which in turn activates PKA. Activated PKA can phosphorylate transcription factors and other proteins associated with ZNF323, potentially enhancing ZNF323's DNA-binding capability and its functional activation as a transcription factor. | ||||||
Ionomycin | 56092-82-1 | sc-3592 sc-3592A | 1 mg 5 mg | $76.00 $265.00 | 80 | |
Ionomycin acts as an ionophore for calcium, increasing intracellular calcium concentrations, which can activate calcium/calmodulin-dependent protein kinases (CaMKs). These kinases can phosphorylate and lead to the activation of proteins associated with the regulation of transcription factors such as ZNF323, thereby promoting its functional activation. | ||||||
Okadaic Acid | 78111-17-8 | sc-3513 sc-3513A sc-3513B | 25 µg 100 µg 1 mg | $285.00 $520.00 $1300.00 | 78 | |
By inhibiting protein phosphatases PP1 and PP2A, okadaic acid leads to increased phosphorylation levels of various proteins. This inhibition can result in the hyperphosphorylation of proteins that interact with or regulate ZNF323, which can enhance ZNF323's activity as a transcription factor. | ||||||
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 inhibits serine/threonine phosphatases like PP1 and PP2A. This leads to a sustained phosphorylation state of proteins, which could include transcription factors or co-regulatory proteins that are necessary for ZNF323 activation. | ||||||
Spermine | 71-44-3 | sc-212953A sc-212953 sc-212953B sc-212953C | 1 g 5 g 25 g 100 g | $60.00 $192.00 $272.00 $883.00 | 1 | |
Spermine can potentiate kinase activity, which could include kinases that phosphorylate proteins interacting with ZNF323, resulting in its functional activation. | ||||||
Retinoic Acid, all trans | 302-79-4 | sc-200898 sc-200898A sc-200898B sc-200898C | 500 mg 5 g 10 g 100 g | $65.00 $319.00 $575.00 $998.00 | 28 | |
Retinoic acid influences gene expression and cell differentiation pathways that could include activation of kinases or other signaling molecules that phosphorylate and activate ZNF323. | ||||||
Insulin | 11061-68-0 | sc-29062 sc-29062A sc-29062B | 100 mg 1 g 10 g | $153.00 $1224.00 $12239.00 | 82 | |
Insulin activates the PI3K/Akt signaling pathway which can lead to the phosphorylation and activation of various proteins involved in transcriptional regulation, potentially including ZNF323, thereby promoting its functional activation. | ||||||
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. PKA phosphorylates transcription factors and associated regulatory proteins, which could lead to functional activation of ZNF323 by enhancing its transcriptional activity. | ||||||
Bryostatin 1 | 83314-01-6 | sc-201407 | 10 µg | $240.00 | 9 | |
Bryostatin 1 is a PKC activator that can modulate downstream signaling pathways, leading to the activation of proteins that regulate transcription factors. The activation of PKC by Bryostatin 1 could thus result in the functional activation of ZNF323 via phosphorylation or enhancement of its protein-protein interactions. | ||||||