CaBP7 is a calcium-binding protein that negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. To inhibit CaBP7, several chemicals can be used. Wortmannin irreversibly binds to the active site of PI4KB, preventing its activity and inhibiting the function of CaBP7. LY 294002 is a selective inhibitor of PI3K, a downstream effector of PI4KB, indirectly inhibiting CaBP7 by competing with ATP for the ATP-binding site of PI3K. Brefeldin A and Nocodazole disrupt the Golgi apparatus and vesicle trafficking, indirectly inhibiting CaBP7 by disrupting the overall trafficking pathway. Latrunculin A, Latrunculia magnifica inhibits actin polymerization, disrupting the actin cytoskeleton and vesicle trafficking. BAPTA/AM and Thapsigargin reduce intracellular calcium levels, indirectlyinhibiting CaBP7, which requires calcium binding for its activity. U-73122 inhibits phospholipase C, indirectly inhibiting CaBP7, which is regulated by calcium signaling. 2-APB and EGTA reduce extracellular and intracellular calcium levels, respectively, indirectly inhibiting CaBP7. Cyclopiazonic acid inhibits the SERCA pump, depleting intracellular calcium stores and inhibiting CaBP7. Tunicamycin disrupts protein folding and trafficking, indirectly inhibiting CaBP7 in Golgi-to-plasma membrane trafficking.
The class of chemicals known as CaBP7 inhibitors target the regulation of Golgi-to-plasma membrane trafficking by interfering with the interaction between CaBP7 and PI4KB. These inhibitors act through various mechanisms, including direct inhibition of PI4KB activity, disruption of vesicle trafficking pathways, modulation of calcium signaling, and interference with protein folding and trafficking processes. Wortmannin and LY 294002 directly target PI4KB, preventing its activity and subsequently inhibiting CaBP7 function. Brefeldin A and Nocodazole disrupt the overall Golgi-to-plasma membrane trafficking pathway, indirectly inhibiting CaBP7 by preventing the interaction between CaBP7 and PI4KB. Latrunculin A, Latrunculia magnifica disrupts actin polymerization, leading to the inhibition of vesicle trafficking and indirectly inhibiting CaBP7. BAPTA/AM, Thapsigargin, U-73122, 2-APB, EGTA, Cyclopiazonic acid, and Tunicamycin all interfere with calcium signaling or protein folding/trafficking processes, indirectly inhibiting CaBP7 by disrupting the cellular processes necessary for its function. Overall, these CaBP7 inhibitors provide valuable tools for studying the regulation of Golgi-to-plasma membrane trafficking and the role of CaBP7 in this process.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Wortmannin | 19545-26-7 | sc-3505 sc-3505A sc-3505B | 1 mg 5 mg 20 mg | $67.00 $223.00 $425.00 | 97 | |
Wortmannin is a potent inhibitor of PI4KB, the protein that CaBP7 interacts with to inhibit Golgi-to-plasma membrane trafficking. It irreversibly binds to the active site of PI4KB, preventing its activity and inhibiting the function of CaBP7. | ||||||
LY 294002 | 154447-36-6 | sc-201426 sc-201426A | 5 mg 25 mg | $123.00 $400.00 | 148 | |
LY 294002 is a selective inhibitor of PI3K, a downstream effector of PI4KB. By inhibiting PI3K, LY 294002 indirectly inhibits the function of CaBP7 in Golgi-to-plasma membrane trafficking. It competes with ATP for the ATP-binding site of PI3K. | ||||||
Brefeldin A | 20350-15-6 | sc-200861C sc-200861 sc-200861A sc-200861B | 1 mg 5 mg 25 mg 100 mg | $31.00 $53.00 $124.00 $374.00 | 25 | |
Brefeldin A disrupts the Golgi apparatus and inhibits vesicle trafficking between the Golgi and the plasma membrane. It indirectly inhibits the function of CaBP7 by disrupting the overall Golgi-to-plasma membrane trafficking pathway. | ||||||
Nocodazole | 31430-18-9 | sc-3518B sc-3518 sc-3518C sc-3518A | 5 mg 10 mg 25 mg 50 mg | $59.00 $85.00 $143.00 $247.00 | 38 | |
Nocodazole disrupts microtubule polymerization, leading to the disorganization of the Golgi apparatus and inhibition of vesicle trafficking. It indirectly inhibits the function of CaBP7 in regulating this process. | ||||||
Latrunculin A, Latrunculia magnifica | 76343-93-6 | sc-202691 sc-202691B | 100 µg 500 µg | $265.00 $815.00 | 36 | |
Latrunculin A, Latrunculia magnifica inhibits actin polymerization, leading to the disruption of the actin cytoskeleton and inhibition of vesicle trafficking. It indirectly inhibits the function of CaBP7 by disrupting the overall Golgi-to-plasma membrane trafficking pathway. | ||||||
BAPTA/AM | 126150-97-8 | sc-202488 sc-202488A | 25 mg 100 mg | $138.00 $458.00 | 61 | |
BAPTA/AM is a calcium chelator that can sequester intracellular calcium ions. By reducing intracellular calcium levels, it can indirectly inhibit the function of CaBP7, which requires calcium binding for its activity in regulating Golgi-to-plasma membrane trafficking. | ||||||
Thapsigargin | 67526-95-8 | sc-24017 sc-24017A | 1 mg 5 mg | $136.00 $446.00 | 114 | |
Thapsigargin inhibits the SERCA pump, which is responsible for calcium uptake into the endoplasmic reticulum. By depleting intracellular calcium stores, it can indirectly inhibit the function of CaBP7, which relies on calcium binding for its activity. | ||||||
2-APB | 524-95-8 | sc-201487 sc-201487A | 20 mg 100 mg | $28.00 $53.00 | 37 | |
2-APB is a blocker of IP3 receptors, which are responsible for releasing calcium from intracellular stores. By inhibiting IP3 receptor-mediated calcium release, it can indirectly inhibit the function of CaBP7, which relies on calcium binding for its activity. | ||||||
EGTA | 67-42-5 | sc-3593 sc-3593A sc-3593B sc-3593C sc-3593D | 1 g 10 g 100 g 250 g 1 kg | $21.00 $65.00 $120.00 $251.00 $815.00 | 23 | |
EGTA is a calcium chelator that can sequester extracellular calcium ions. By reducing extracellular calcium levels, it can indirectly inhibit the function of CaBP7, which requires calcium binding for its activity in regulating Golgi-to-plasma membrane trafficking. | ||||||
Cyclopiazonic Acid | 18172-33-3 | sc-201510 sc-201510A | 10 mg 50 mg | $176.00 $624.00 | 3 | |
Cyclopiazonic acid inhibits the SERCA pump, which is responsible for calcium uptake into the endoplasmic reticulum. By depleting intracellular calcium stores, it can indirectly inhibit the function of CaBP7, which relies on calcium binding for its activity. | ||||||