TRIM43B Activators
Chemical activators of TRIM43B can influence the protein's state through various biochemical mechanisms. Forskolin, for example, directly stimulates adenylate cyclase, increasing intracellular levels of cAMP. This surge in cAMP activates protein kinase A (PKA), which is known to phosphorylate proteins, thereby modifying their functional state. This phosphorylation cascade can lead to the activation of TRIM43B. Similarly, Ionomycin, by acting as a calcium ionophore, elevates intracellular calcium concentrations, which then activate calmodulin-dependent kinase (CaMK). CaMK, in turn, can phosphorylate TRIM43B as part of the calcium signaling pathway.
Other activators such as Phorbol 12-myristate 13-acetate (PMA) target protein kinase C (PKC), which phosphorylates TRIM43B. PKC is involved in a multitude of signaling pathways, and its activation is a common trigger for the regulation of many proteins. Conversely, hydrogen peroxide, a reactive oxygen species, can lead to the oxidative modification of amino acids in proteins, which can alter their function and result in TRIM43B activation. Similarly, inhibitors of protein phosphatases such as Calyculin A and Okadaic Acid can prevent the dephosphorylation of proteins, leading to a sustained phosphorylated state of TRIM43B, thereby maintaining its activated form. Additionally, Anisomycin, by activating stress-activated protein kinases (SAPKs) such as JNK, can also phosphorylate and activate TRIM43B. Thapsigargin, by inhibiting the sarco/endoplasmic reticulum Ca2+-ATPase (SERCA), raises cytosolic calcium levels, which could also lead to the phosphorylation and activation of TRIM43B through calcium-dependent signaling mechanisms. Finally, molecules that alter cellular homeostasis, like Chloroquine, which disrupts lysosomal function, and Lithium Chloride, which inhibits GSK-3β, can lead to altered signaling pathways that culminate in the activation of TRIM43B. Zinc Pyrithione, by chelating zinc ions, may induce conformational alterations that enhance TRIM43B activity. These diverse chemicals, through multiple signaling pathways and molecular mechanisms, can all contribute to the activation of TRIM43B.
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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 directly activates adenylate cyclase, leading to an increase in cyclic AMP (cAMP) levels. Elevated cAMP activates PKA (protein kinase A), which can phosphorylate TRIM43B, leading to its activation. | ||||||
Ionomycin | 56092-82-1 | sc-3592 sc-3592A | 1 mg 5 mg | $76.00 $265.00 | 80 | |
Ionomycin functions as a calcium ionophore, increasing intracellular calcium levels. Calcium can activate calmodulin-dependent kinase (CaMK), which may phosphorylate and activate TRIM43B as part of the calcium signaling pathway. | ||||||
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 can then phosphorylate TRIM43B. PKC-mediated phosphorylation is a common mechanism for the functional activation of many proteins, including those within the TRIM family. | ||||||
Hydrogen Peroxide | 7722-84-1 | sc-203336 sc-203336A sc-203336B | 100 ml 500 ml 3.8 L | $30.00 $60.00 $93.00 | 27 | |
Hydrogen peroxide is a reactive oxygen species that can lead to the oxidation of specific amino acid residues, which can alter protein function. This can lead to the activation of TRIM43B through oxidative modifications. | ||||||
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 | |
Calyculin A is an inhibitor of protein phosphatases 1 (PP1) and 2A (PP2A). By inhibiting these phosphatases, Calyculin A can result in the increased phosphorylation state of proteins, including TRIM43B, leading to its 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 | |
Similar to Calyculin A, Okadaic Acid inhibits PP1 and PP2A, which could lead to a hyperphosphorylated state of TRIM43B, resulting in its activation due to the prevention of dephosphorylation. | ||||||
Anisomycin | 22862-76-6 | sc-3524 sc-3524A | 5 mg 50 mg | $97.00 $254.00 | 36 | |
Anisomycin is known to activate stress-activated protein kinases (SAPKs) like JNK. The activation of JNK can lead to the phosphorylation and activation of various substrate proteins, potentially including TRIM43B. | ||||||
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), leading to increased cytosolic calcium levels. Elevated calcium can activate signaling pathways that phosphorylate and activate TRIM43B. | ||||||
Chloroquine | 54-05-7 | sc-507304 | 250 mg | $68.00 | 2 | |
Chloroquine can lead to the alkalization of lysosomes and inhibition of lysosomal enzymes, which might result in the activation of TRIM43B due to altered protein degradation pathways, specifically those involving ubiquitination and TRIM proteins. | ||||||
Lithium | 7439-93-2 | sc-252954 | 50 g | $214.00 | ||
Lithium Chloride inhibits GSK-3β, leading to activation of Wnt/β-catenin signaling. As part of this pathway, TRIM43B could be activated as a response to changes in signaling that require TRIM43B's role in ubiquitination and proteasomal degradation. | ||||||