Items 1 to 10 of 12 total
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
CK 666 | 442633-00-3 | sc-361151 sc-361151A | 10 mg 50 mg | $315.00 $1020.00 | 5 | |
CK666 is a small molecule inhibitor of the Arp2/3 complex, which regulates actin polymerization. By inhibiting Arp2/3, CK666 disrupts the actin cytoskeleton dynamics. Neurabin-II interacts with actin filaments, and modulation of actin dynamics can indirectly affect Neurabin-II localization and function. | ||||||
Latrunculin A, Latrunculia magnifica | 76343-93-6 | sc-202691 sc-202691B | 100 µg 500 µg | $260.00 $799.00 | 36 | |
Latrunculin A is a marine toxin that disrupts actin polymerization by sequestering monomeric actin. Since Neurabin-II interacts with actin, inhibition of actin polymerization by Latrunculin A can impact the organization of the actin cytoskeleton, indirectly influencing Neurabin-II function and localization. | ||||||
Jasplakinolide | 102396-24-7 | sc-202191 sc-202191A | 50 µg 100 µg | $180.00 $299.00 | 59 | |
Jasplakinolide is a natural product that stabilizes actin filaments, preventing depolymerization. As Neurabin-II is associated with actin filaments, the stabilization of actin by Jasplakinolide can indirectly modulate Neurabin-II localization and function by affecting the dynamic rearrangement of the actin cytoskeleton. | ||||||
(±)-Blebbistatin | 674289-55-5 | sc-203532B sc-203532 sc-203532A sc-203532C sc-203532D | 5 mg 10 mg 25 mg 50 mg 100 mg | $179.00 $307.00 $455.00 $924.00 $1689.00 | 7 | |
Blebbistatin is a selective inhibitor of myosin II ATPase activity, leading to the inhibition of myosin-mediated contractility. Since Neurabin-II interacts with myosin II and regulates its activity, the inhibition of myosin II by Blebbistatin can influence the interactions between Neurabin-II and myosin II, indirectly modulating Neurabin-II function. | ||||||
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 a potent inhibitor of protein phosphatases, particularly PP1 and PP2A. Neurabin-II is known to interact with and be regulated by protein phosphatases. Inhibition of these phosphatases by Calyculin A can lead to hyperphosphorylation of Neurabin-II, potentially affecting its localization and interactions with other proteins. | ||||||
Okadaic Acid | 78111-17-8 | sc-3513 sc-3513A sc-3513B | 25 µg 100 µg 1 mg | $285.00 $520.00 $1300.00 | 78 | |
Okadaic Acid is another potent inhibitor of protein phosphatases, particularly PP1 and PP2A. Similar to Calyculin A, Okadaic Acid can lead to hyperphosphorylation of Neurabin-II by inhibiting protein phosphatases, impacting the localization and functional interactions of Neurabin-II within the cell. | ||||||
CK-869 | 388592-44-7 | sc-507274 | 5 mg | $160.00 | ||
CK869 is a small molecule that inhibits the Arp2/3 complex, similar to CK666. By targeting Arp2/3, CK869 disrupts actin polymerization, which can indirectly influence Neurabin-II function and localization due to its association with actin filaments. | ||||||
SMIFH2 | 340316-62-3 | sc-507273 | 5 mg | $140.00 | ||
SMIFH2 is a small molecule inhibitor that disrupts formin-mediated actin polymerization. Since Neurabin-II interacts with actin, the inhibition of actin polymerization by SMIFH2 can indirectly affect Neurabin-II localization and function by altering the dynamics of the actin cytoskeleton. | ||||||
Cytochalasin D | 22144-77-0 | sc-201442 sc-201442A | 1 mg 5 mg | $145.00 $442.00 | 64 | |
Cytochalasin D is a mycotoxin that disrupts actin polymerization by capping the growing ends of actin filaments. As Neurabin-II is associated with actin filaments, the disturbance of actin dynamics by Cytochalasin D can indirectly modulate Neurabin-II localization and function by impacting actin filament rearrangement. | ||||||
Phalloidin | 17466-45-4 | sc-202763 | 1 mg | $229.00 | 33 | |
Phalloidin is a toxin that stabilizes F-actin filaments, preventing their depolymerization. Since Neurabin-II is associated with actin filaments, the stabilization of actin by Phalloidin can indirectly influence Neurabin-II localization and function by affecting the dynamic rearrangement of the actin cytoskeleton. | ||||||