LOC100130274 Activators
Chemical activators of LOC100130274 can modulate the protein's activity through various intracellular signaling pathways, primarily by altering its phosphorylation state. Forskolin, known for its ability to increase cyclic AMP (cAMP) levels, activates protein kinase A (PKA), which can then target LOC100130274 for phosphorylation, leading to its activation. Similarly, PMA and 1,2-Dioctanoyl-sn-glycerol, both activators of protein kinase C (PKC), stimulate the phosphorylation and consequent activation of LOC100130274, incorporating it into cellular signaling cascades. Ionomycin and A23187, both calcium ionophores, elevate intracellular calcium levels, which can activate calcium-dependent kinases capable of phosphorylating LOC100130274. Thapsigargin also raises cytosolic calcium by inhibiting the SERCA pump, triggering a cascade of calcium-mediated phosphorylation events that can activate LOC100130274.
Okadaic Acid and Calyculin A, inhibitors of protein phosphatases PP1 and PP2A, prevent the dephosphorylation of proteins, thus maintaining LOC100130274 in a phosphorylated and active state. Anisomycin activates stress-activated protein kinases, such as JNK and p38 MAPK, which are involved in the cellular stress response and can lead to the activation of LOC100130274 through phosphorylation. Although KN-93 is known to inhibit calcium/calmodulin-dependent protein kinase II (CaMKII), the inhibition can trigger compensatory cellular responses that activate alternative kinases. These kinases may then participate in phosphorylating and activating LOC100130274. Moreover, H-89, while primarily a PKA inhibitor, may at higher concentrations inhibit other kinases, indirectly leading to the activation of compensatory pathways that can result in the phosphorylation and activation of LOC100130274. Collectively, these chemicals engage a network of kinases and phosphatases that converge on the regulation of LOC100130274 activity through phosphorylation.
| 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 | $41.00 $132.00 $214.00 $500.00 $948.00 | 119 | |
Phorbol 12-myristate 13-acetate (PMA) activates protein kinase C (PKC). Activation of PKC leads to the phosphorylation of proteins that are a part of signal transduction pathways. PKC-mediated phosphorylation of LOC100130274 would result in the protein's functional activation. | ||||||
Ionomycin | 56092-82-1 | sc-3592 sc-3592A | 1 mg 5 mg | $78.00 $270.00 | 80 | |
Ionomycin acts as a calcium ionophore, increasing intracellular calcium levels. The rise in calcium can activate calcium-dependent protein kinases, which in turn can phosphorylate and activate proteins involved in calcium signaling. Through this mechanism, ionomycin can lead to the phosphorylation and subsequent activation of LOC100130274. | ||||||
Thapsigargin | 67526-95-8 | sc-24017 sc-24017A | 1 mg 5 mg | $136.00 $446.00 | 114 | |
Thapsigargin inhibits the SERCA pump, causing an increase in cytosolic calcium levels. This perturbation in calcium homeostasis can activate calcium-dependent enzymes, which are capable of activating downstream proteins. Through the activation of calcium-dependent kinases, thapsigargin can lead to the functional activation of LOC100130274. | ||||||
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 PP1 and PP2A. Inhibition of these phosphatases leads to increased phosphorylation levels of proteins by preventing dephosphorylation. As protein phosphorylation is a common mechanism for functional activation, the inhibition of phosphatases by Okadaic Acid can result in the activation of LOC100130274. | ||||||
Anisomycin | 22862-76-6 | sc-3524 sc-3524A | 5 mg 50 mg | $99.00 $259.00 | 36 | |
Anisomycin is known to activate stress-activated protein kinases such as JNK and p38 MAPK. These kinases can phosphorylate a variety of substrate proteins involved in cellular stress responses. Through the activation of these kinases, anisomycin can lead to the phosphorylation and activation of LOC100130274, as it is part of the cellular response to stress. | ||||||
Calyculin A | 101932-71-2 | sc-24000 sc-24000A | 10 µg 100 µg | $163.00 $800.00 | 59 | |
Calyculin A is another inhibitor of protein phosphatases like PP1 and PP2A. By inhibiting these, there is a sustained phosphorylation of proteins. This can lead to the activation of proteins within signaling pathways that are regulated by phosphorylation. Through this sustained phosphorylation, Calyculin A can cause the activation of LOC100130274. | ||||||
1,2-Dioctanoyl-sn-glycerol | 60514-48-9 | sc-202397 sc-202397A | 10 mg 50 mg | $47.00 $254.00 | 2 | |
1,2-Dioctanoyl-sn-glycerol (DOG) is a synthetic analogue of diacylglycerol (DAG) and can activate protein kinase C (PKC). PKC, once activated, phosphorylates and activates proteins involved in various signaling pathways. The activation of PKC by DOG can thus lead to the phosphorylation and functional activation of LOC100130274. | ||||||
A23187 | 52665-69-7 | sc-3591 sc-3591B sc-3591A sc-3591C | 1 mg 5 mg 10 mg 25 mg | $55.00 $131.00 $203.00 $317.00 | 23 | |
A23187 acts as a calcium ionophore similar to ionomycin, increasing intracellular calcium levels. This elevation in calcium can activate calcium-dependent kinases, which in turn can phosphorylate proteins within calcium signaling pathways. A23187 can thus lead to the phosphorylation and functional activation of LOC100130274 through calcium-dependent signaling pathways. | ||||||
KN-93 | 139298-40-1 | sc-202199 | 1 mg | $182.00 | 25 | |
KN-93 is an inhibitor of calcium/calmodulin-dependent protein kinase II (CaMKII). Inhibition of CaMKII can lead to compensatory cellular effects that activate other kinases or signaling molecules to maintain cellular functions. These compensatory effects can lead to the activation of kinases that phosphorylate and activate LOC100130274 as part of their regulatory function. | ||||||