β1-Syntrophin Inhibitors
Chemical inhibitors of β1-Syntrophin act by various mechanisms to modulate the cytoskeletal infrastructure with which this protein interacts. Phalloidin and Jasplakinolide both enhance actin filament stability; the former by binding to F-actin and preventing depolymerization, and the latter by promoting actin polymerization. Their action can lead to an overly rigid actin cytoskeleton, which can interfere with the dynamic interactions required for β1-Syntrophin to perform its cellular functions. Conversely, Latrunculin A and Cytochalasin D disrupt the actin cytoskeleton, albeit through different approaches – Latrunculin A by sequestering G-actin monomers and Cytochalasin D by capping the growing ends of actin filaments. These disruptions can hinder the ability of β1-Syntrophin to bind to actin, which is essential for its role in signal transduction and molecular organization.
Other inhibitors target ancillary pathways that indirectly affect β1-Syntrophin function. ML-7, by inhibiting myosin light chain kinase, and Blebbistatin, by targeting myosin II ATPase, can alter actin-myosin interactions and thus the mechanical stability of the cytoskeleton, which can reduce the structural support necessary for β1-Syntrophin's operations. Y-27632 and Wiskostatin, which inhibit Rho-associated protein kinase and neural Wiskott-Aldrich syndrome protein respectively, alter the organization and nucleation of actin filaments, potentially disrupting β1-Syntrophin's ability to facilitate cellular signaling. CK-636 and SMIFH2 target the actin nucleation and elongation processes by inhibiting the Arp2/3 complex and formin-mediated actin assembly, respectively. This inhibition can lead to a less organized actin framework, affecting the β1-Syntrophin's scaffolding capabilities. Finally, Chelerythrine and Gö6976, as inhibitors of protein kinase C, can influence the phosphorylation state of proteins involved in the actin cytoskeleton dynamics, which is crucial for maintaining β1-Syntrophin's functional interactions within the cell.
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Items 1 to 10 of 11 total
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Phalloidin | 17466-45-4 | sc-202763 | 1 mg | $229.00 | 33 | |
Phalloidin binds to F-actin, stabilizing it and preventing its depolymerization, which is crucial for maintaining the cytoskeleton integrity. Since β1-Syntrophin is associated with actin cytoskeleton, phalloidin's stabilization of F-actin could hinder the dynamic interactions required for β1-Syntrophin to function properly in cell signaling and molecular scaffolding. | ||||||
Latrunculin A, Latrunculia magnifica | 76343-93-6 | sc-202691 sc-202691B | 100 µg 500 µg | $260.00 $799.00 | 36 | |
Latrunculin A binds to G-actin monomers, preventing their polymerization into F-actin. By disrupting the actin cytoskeleton, this compound indirectly inhibits β1-Syntrophin's ability to interact with actin and perform its scaffolding functions within the dystrophin-glycoprotein complex. | ||||||
Jasplakinolide | 102396-24-7 | sc-202191 sc-202191A | 50 µg 100 µg | $180.00 $299.00 | 59 | |
Jasplakinolide promotes actin polymerization and also stabilizes actin filaments. By altering actin dynamics, it affects the structural framework necessary for β1-Syntrophin to anchor and interact with signaling molecules, thus impairing its role in signal transduction processes. | ||||||
Cytochalasin D | 22144-77-0 | sc-201442 sc-201442A | 1 mg 5 mg | $145.00 $442.00 | 64 | |
Cytochalasin D disrupts actin polymerization by capping the barbed ends of actin filaments, ultimately leading to cytoskeleton disassembly. This disruption can inhibit β1-Syntrophin's ability to bind to the actin cytoskeleton, impairing its cellular functions. | ||||||
ML-7 hydrochloride | 110448-33-4 | sc-200557 sc-200557A | 10 mg 50 mg | $89.00 $262.00 | 13 | |
ML-7 is an inhibitor of myosin light chain kinase (MLCK), which is involved in myosin-actin interaction. By inhibiting MLCK, ML-7 may reduce actin-myosin contractility, potentially disrupting the mechanical stability of the cytoskeleton and the associated function of β1-Syntrophin in cellular signaling. | ||||||
Y-27632, free base | 146986-50-7 | sc-3536 sc-3536A | 5 mg 50 mg | $182.00 $693.00 | 88 | |
Y-27632 is an inhibitor of Rho-associated protein kinase (ROCK), which plays a role in actin cytoskeleton organization. Inhibition of ROCK may lead to a less organized cytoskeleton, affecting the ability of β1-Syntrophin to properly engage with its binding partners and carry out its scaffolding role. | ||||||
Wiskostatin | 253449-04-6 | sc-204399 sc-204399A sc-204399B sc-204399C | 1 mg 5 mg 25 mg 50 mg | $48.00 $122.00 $432.00 $812.00 | 4 | |
Wiskostatin is a selective inhibitor of the neural Wiskott-Aldrich syndrome protein (N-WASP), an actin-nucleation promoting factor. Since β1-Syntrophin's function is related to actin dynamics, inhibiting N-WASP may interfere with the actin remodeling necessary for β1-Syntrophin's activities. | ||||||
(±)-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 an inhibitor of myosin II ATPase activity. By inhibiting myosin II, Blebbistatin impairs actin-myosin interactions and can disturb cytoskeletal integrity. This may compromise the structural and signaling mechanisms involving β1-Syntrophin. | ||||||
SMIFH2 | 340316-62-3 | sc-507273 | 5 mg | $140.00 | ||
SMIFH2 is an inhibitor of formin-mediated actin assembly. Formins are important for the elongation of actin filaments. By inhibiting formin activity, SMIFH2 might disrupt actin polymerization and subsequently β1-Syntrophin's scaffolding and signaling roles that depend on actin structures. | ||||||
Chelerythrine chloride | 3895-92-9 | sc-3547 sc-3547A | 5 mg 25 mg | $88.00 $311.00 | 17 | |
Chelerythrine is a potent inhibitor of protein kinase C (PKC). PKC is implicated in a wide range of cellular functions, including roles in cytoskeletal organization. Inhibiting PKC can lead to altered actin dynamics, which could hinder the operational framework required for β1-Syntrophin function. | ||||||