TEX12 Activators
TEX12 can influence its function through various biochemical pathways, primarily by altering the phosphorylation state of proteins that interact with TEX12 or are part of the synaptonemal complex. Dibutyryl-cAMP and Forskolin, for example, both serve to increase intracellular cAMP levels, which in turn activate cAMP-dependent protein kinases. These kinases can phosphorylate substrates that may include proteins associated with TEX12, thereby modulating its activity in maintaining synaptonemal complex structure. Similarly, Phorbol 12-myristate 13-acetate (PMA) activates protein kinase C (PKC), which also has the capacity to phosphorylate and alter proteins that may work in conjunction with TEX12 to promote its stabilizing function.
Calyculin A, Okadaic Acid, and Tautomycin act by preventing the dephosphorylation of proteins. By inhibiting protein phosphatases 1 and 2A, these chemicals help maintain proteins in a phosphorylated state, which is often required for active processes within the cell. This sustained phosphorylation can ensure that proteins interacting with TEX12 remain in a state that supports TEX12's activity in meiotic processes. Complementarily, Ionomycin and Thapsigargin both elevate intracellular calcium levels, which could activate calcium-dependent proteins that are necessary for TEX12 function. Similarly, Bisindolylmaleimide I, despite being a PKC inhibitor, may at low concentrations activate certain PKC isoforms, leading to the phosphorylation of proteins that interact with TEX12, promoting its role in the synaptonemal complex. Lastly, Anisomycin activates stress-activated protein kinases, which could phosphorylate and thereby regulate proteins that enhance TEX12's function in meiotic chromosome dynamics, while Epigallocatechin gallate (EGCG) influences various signaling pathways that may include kinases that phosphorylate proteins associated with TEX12. Zearalenone, through its interaction with estrogenic signaling pathways, can also modify the phosphorylation state of proteins that regulate TEX12 activity during meiosis.
SEE ALSO...
Items 1 to 10 of 11 total
Display:
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Dibutyryl-cAMP | 16980-89-5 | sc-201567 sc-201567A sc-201567B sc-201567C | 20 mg 100 mg 500 mg 10 g | $47.00 $136.00 $492.00 $4552.00 | 74 | |
Dibutyryl-cAMP is a cell-permeable cAMP analog that activates cAMP-dependent protein kinases. TEX12 is known to be involved in meiotic cohesion; thus, activation of protein kinase A by this analog may lead to phosphorylation events that enhance TEX12's role in maintaining synaptonemal complex structure. | ||||||
Ionomycin, free acid | 56092-81-0 | sc-263405 sc-263405A | 1 mg 5 mg | $96.00 $264.00 | 2 | |
Ionomycin is a calcium ionophore that elevates intracellular calcium levels. TEX12 function in meiosis is likely calcium-dependent as many cellular processes are; increased calcium may activate kinases or other proteins that interact directly with TEX12, promoting its stabilizing function in the synaptonemal complex. | ||||||
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 | |
PMA activates protein kinase C (PKC), which can influence multiple pathways, including those involved in meiotic progression. PKC may activate pathways or modify proteins that are directly interacting with TEX12, thereby enhancing its function. | ||||||
Calyculin A | 101932-71-2 | sc-24000 sc-24000A | 10 µg 100 µg | $163.00 $800.00 | 59 | |
Calyculin A is a potent inhibitor of protein phosphatases 1 and 2A. By inhibiting dephosphorylation, it may indirectly maintain the phosphorylation state of proteins that interact with TEX12, thus sustaining TEX12's activation status within the synaptonemal complex. | ||||||
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 another inhibitor of protein phosphatases 1 and 2A. Similar to Calyculin A, by preventing dephosphorylation, it could potentially maintain the activation state of proteins that associate with TEX12, thereby supporting its function in meiosis. | ||||||
(−)-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 | $43.00 $73.00 $126.00 $243.00 $530.00 $1259.00 | 11 | |
EGCG has been shown to influence multiple signaling pathways, including those with kinase activity. These kinase pathways could phosphorylate and thus change the interaction of proteins with TEX12, promoting its activity in the synaptonemal complex. | ||||||
Anisomycin | 22862-76-6 | sc-3524 sc-3524A | 5 mg 50 mg | $99.00 $259.00 | 36 | |
Anisomycin is a protein synthesis inhibitor that also activates stress-activated protein kinases. The activation of these kinases could lead to phosphorylation of proteins that regulate TEX12 activity, thereby enhancing TEX12's role in meiotic chromosome dynamics. | ||||||
Bisindolylmaleimide I (GF 109203X) | 133052-90-1 | sc-24003A sc-24003 | 1 mg 5 mg | $105.00 $242.00 | 36 | |
Bisindolylmaleimide I is a specific inhibitor of PKC, but it may paradoxically activate certain PKC isoforms at low concentrations. This PKC isoform activation may then modulate proteins interacting with TEX12, leading to its activation within its cellular context. | ||||||
Thapsigargin | 67526-95-8 | sc-24017 sc-24017A | 1 mg 5 mg | $136.00 $446.00 | 114 | |
Thapsigargin is a SERCA pump inhibitor that leads to increased cytosolic calcium levels. Elevated calcium levels may activate calcium-dependent proteins that are necessary for the activation of TEX12 function in synaptonemal complex stabilization. | ||||||
Tunicamycin | 11089-65-9 | sc-3506A sc-3506 | 5 mg 10 mg | $172.00 $305.00 | 66 | |
Tautomycin is another potent inhibitor of protein phosphatases 1 and 2A. By hindering protein dephosphorylation, it could indirectly maintain the phosphorylation and thus the activation state of proteins that are crucial for TEX12's function. | ||||||