FBLIM1 Inhibitors
Chemical inhibitors of FBLIM1 can disrupt the protein's functionality through various mechanisms, each related to the actin cytoskeleton which FBLIM1 is known to stabilize and organize. Y-27632, for example, targets the Rho-associated protein kinase (ROCK), a key regulator of actin cytoskeleton dynamics. By inhibiting ROCK, Y-27632 disrupts the downstream actin filament organization, thus indirectly inhibiting the stabilizing role of FBLIM1 on these structures. Similarly, ML-7 disrupts actin-myosin interactions by inhibiting myosin light chain kinase (MLCK), which phosphorylates myosin light chains, a process vital for actin filament tension and integrity that FBLIM1 supports. Cytochalasin D and Latrunculin A directly bind to actin filaments and monomers respectively, preventing polymerization and elongation, processes crucial for the maintenance of actin structures that FBLIM1 is a part of. This disruption leads to a functional inhibition of FBLIM1's role in actin stability.
Further inhibitory actions come from chemicals like Blebbistatin and Jasplakinolide, which affect myosin II and actin filaments, respectively. Blebbistatin inhibits myosin II ATPase activity, which is essential for actin filament contractility, a dynamic that FBLIM1 is involved in. Jasplakinolide, on the other hand, stabilizes actin filaments to such an extent that it paradoxically inhibits the dynamic role that FBLIM1 plays in modulating the actin cytoskeleton. Additionally, CK-666 and SMIFH2 target the Arp2/3 complex and formin-mediated actin nucleation, both essential for the formation of actin filaments, thereby inhibiting the structural organization that FBLIM1 helps facilitate. CCG-1423 disrupts RhoA signaling, which is intricately linked to actin cytoskeleton organization, affecting FBLIM1's role. Chelerythrine and Wiskostatin inhibit protein kinase C and the N-WASP-Arp2/3 complex interaction, which are crucial for maintaining actin dynamics and thus, the stability of actin filaments that FBLIM1 is associated with. Lastly, Thapsigargin raises cytosolic calcium levels, which indirectly affects actin dynamics, creating a cellular environment that is not conducive to the stabilizing function of FBLIM1 on the actin cytoskeleton.
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Items 1 to 10 of 12 total
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Y-27632, free base | 146986-50-7 | sc-3536 sc-3536A | 5 mg 50 mg | $186.00 $707.00 | 88 | |
A selective inhibitor of ROCK (Rho-associated protein kinase), which is involved in actin cytoskeleton organization. FBLIM1 interacts with actin filaments and is implicated in the stabilization of the actin cytoskeleton. By inhibiting ROCK, Y-27632 can disrupt actin cytoskeleton dynamics, thereby functionally inhibiting the stabilizing role of FBLIM1. | ||||||
(S)-(−)-Blebbistatin | 856925-71-8 | sc-204253 sc-204253A sc-204253B sc-204253C | 1 mg 5 mg 10 mg 25 mg | $72.00 $265.00 $495.00 $968.00 | ||
An inhibitor of myosin II ATPase activity. Since FBLIM1 is associated with actin filaments, its function is closely related to the contractility and dynamics regulated by myosin II. Blebbistatin, by inhibiting myosin II, can interfere with this process, potentially disrupting the interaction between FBLIM1 and actin, leading to its functional inhibition. | ||||||
ML-7 hydrochloride | 110448-33-4 | sc-200557 sc-200557A | 10 mg 50 mg | $91.00 $267.00 | 13 | |
An inhibitor of myosin light chain kinase (MLCK), which phosphorylates myosin light chains to promote actin-myosin interactions. FBLIM1, being associated with the actin cytoskeleton, can be functionally inhibited if MLCK is inhibited, as this would disrupt the tension and structure of actin filaments that FBLIM1 is involved with. | ||||||
Cytochalasin D | 22144-77-0 | sc-201442 sc-201442A | 1 mg 5 mg | $165.00 $486.00 | 64 | |
Binds to the barbed ends of actin filaments, preventing elongation and promoting depolymerization. As FBLIM1 is involved in actin filament organization, the disruption of actin polymerization by Cytochalasin D would disrupt the structural integrity that FBLIM1 helps to maintain. | ||||||
Latrunculin A, Latrunculia magnifica | 76343-93-6 | sc-202691 sc-202691B | 100 µg 500 µg | $265.00 $815.00 | 36 | |
Binds to actin monomers and prevents their polymerization. FBLIM1's role in actin filament formation and maintenance would be compromised by the prevention of actin polymerization, functionally inhibiting FBLIM1's ability to stabilize actin structures. | ||||||
Jasplakinolide | 102396-24-7 | sc-202191 sc-202191A | 50 µg 100 µg | $184.00 $305.00 | 59 | |
Stabilizes actin filaments and prevents their disassembly. By locking actin filaments in a stable state, Jasplakinolide can paradoxically inhibit the dynamic function of FBLIM1, which is to modulate the actin cytoskeleton structure. | ||||||
CK 666 | 442633-00-3 | sc-361151 sc-361151A | 10 mg 50 mg | $321.00 $1040.00 | 5 | |
An inhibitor of the Arp2/3 complex, which is involved in the nucleation of new actin filaments. The inhibition of Arp2/3-mediated actin polymerization could impair the organization of actin structures that FBLIM1 is involved in, thereby functionally inhibiting its action. | ||||||
SMIFH2 | 340316-62-3 | sc-507273 | 5 mg | $140.00 | ||
An inhibitor of formin-mediated actin nucleation and elongation. Since FBLIM1 is involved in actin filament organization, inhibiting formin function can interfere with FBLIM1's role in actin dynamics, leading to its functional inhibition. | ||||||
CCG-1423 | 285986-88-1 | sc-205241 sc-205241A | 1 mg 5 mg | $30.00 $90.00 | 8 | |
An inhibitor of RhoA transcriptional signaling, which impacts actin cytoskeleton organization. By disrupting RhoA signaling, FBLIM1's associated actin dynamics and structures can be disrupted, leading to functional inhibition of the protein's role in actin cytoskeleton stabilization. | ||||||
Chelerythrine chloride | 3895-92-9 | sc-3547 sc-3547A | 5 mg 25 mg | $90.00 $317.00 | 17 | |
A protein kinase C inhibitor, which can modulate actin dynamics indirectly. Since FBLIM1's function is closely related to actin filament stabilization, the inhibition of protein kinase C can disrupt this balance, functionally inhibiting FBLIM1. | ||||||