MYH9 Activators
MYH9 activators constitute a diverse array of chemicals that either directly or indirectly influence the function of MYH9, a non-muscle myosin II motor protein involved in various cellular processes, including cell motility, adhesion, and cytokinesis. While direct activators specific to MYH9 are limited, several compounds indirectly modulate MYH9 by targeting key regulators within the cellular machinery. Among the indirect activators, Blebbistatin stands out as a myosin II inhibitor that indirectly impacts MYH9 by inhibiting myosin II ATPase activity. This disruption of myosin II function leads to altered actin-myosin contractility, indirectly influencing MYH9-mediated cellular dynamics. Similarly, Y-27632, a ROCK inhibitor, indirectly modulates MYH9 through RhoA/ROCK signaling. Inhibition of ROCK disrupts downstream pathways involved in myosin II regulation, indirectly affecting MYH9's role in cytoskeletal dynamics and cellular contractility.
ML-7, a myosin light chain kinase (MLCK) inhibitor, indirectly regulates MYH9 by disrupting the phosphorylation of myosin regulatory light chain. Inhibition of MLCK results in reduced myosin II activation, indirectly affecting MYH9-mediated cellular processes dependent on actomyosin dynamics. Calyculin A, a protein phosphatase inhibitor, indirectly influences MYH9 by preventing dephosphorylation of myosin II regulatory light chain. This sustains myosin II activation, impacting MYH9-mediated cellular processes related to actomyosin contractility. The actin cytoskeleton plays a pivotal role in MYH9 regulation, and chemicals like Jasplakinolide, Latrunculin B, CK-666, and SMIFH2 indirectly modulate MYH9 by influencing actin dynamics. Jasplakinolide promotes actin polymerization, indirectly affecting the interaction between actin and myosin II. In contrast, Latrunculin B depolymerizes actin filaments, disrupting the actin-myosin interaction. CK-666 and SMIFH2 target the Arp2/3 complex and formin, respectively, impacting actin nucleation and polymerization, indirectly influencing MYH9-mediated cellular processes related to cytoskeletal organization and motility. Brefeldin A, an ADP-ribosylation factor (ARF) activator, indirectly regulates MYH9 through Golgi apparatus dynamics. Disruption of ARF-dependent vesicular trafficking by Brefeldin A influences the localization of MYH9, potentially altering its functions related to membrane trafficking and cytoskeletal organization.
| 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 | |
Y-27632, a ROCK inhibitor, indirectly influences MYH9 through RhoA/ROCK signaling. By inhibiting ROCK, Y-27632 disrupts the downstream pathways involved in myosin II regulation. This disruption can indirectly modulate MYH9 activity, impacting its cellular functions related to cytoskeletal dynamics and contractility. | ||||||
ML-7 hydrochloride | 110448-33-4 | sc-200557 sc-200557A | 10 mg 50 mg | $91.00 $267.00 | 13 | |
ML-7, a myosin light chain kinase (MLCK) inhibitor, indirectly regulates MYH9 by disrupting the phosphorylation of myosin regulatory light chain. Inhibition of MLCK by ML-7 results in reduced myosin II activation and altered contractile activity, indirectly affecting MYH9-mediated cellular processes dependent on actomyosin dynamics. | ||||||
Calyculin A | 101932-71-2 | sc-24000 sc-24000A | 10 µg 100 µg | $163.00 $800.00 | 59 | |
Calyculin A, a protein phosphatase inhibitor, indirectly influences MYH9 by preventing dephosphorylation of myosin II regulatory light chain. By maintaining phosphorylation, calyculin A sustains myosin II activation, indirectly impacting MYH9-mediated cellular processes dependent on actomyosin contractility and cytoskeletal dynamics. | ||||||
Jasplakinolide | 102396-24-7 | sc-202191 sc-202191A | 50 µg 100 µg | $184.00 $305.00 | 59 | |
Jasplakinolide, an actin polymerization enhancer, indirectly modulates MYH9 by influencing actin dynamics. By promoting actin polymerization, jasplakinolide indirectly affects the interaction between actin and myosin II, potentially altering MYH9-mediated processes related to cytoskeletal organization and cellular motility. | ||||||
Latrunculin A, Latrunculia magnifica | 76343-93-6 | sc-202691 sc-202691B | 100 µg 500 µg | $265.00 $815.00 | 36 | |
Latrunculin B, an actin depolymerizing agent, indirectly regulates MYH9 by disrupting actin filaments. By inhibiting actin polymerization, latrunculin B indirectly affects the interaction between actin and myosin II, potentially altering MYH9-mediated cellular processes related to cytoskeletal dynamics and cellular motility. | ||||||
CK 666 | 442633-00-3 | sc-361151 sc-361151A | 10 mg 50 mg | $321.00 $1040.00 | 5 | |
CK-666, an Arp2/3 complex inhibitor, indirectly influences MYH9 through actin cytoskeleton modulation. By inhibiting the Arp2/3 complex, CK-666 disrupts actin nucleation and branching, indirectly impacting the interaction between actin and myosin II. This can alter MYH9-mediated cellular processes related to cytoskeletal organization and motility. | ||||||
SMIFH2 | 340316-62-3 | sc-507273 | 5 mg | $140.00 | ||
SMIFH2, a formin inhibitor, indirectly modulates MYH9 by impacting actin dynamics. By inhibiting formin-mediated actin polymerization, SMIFH2 indirectly affects the interaction between actin and myosin II, potentially altering MYH9-mediated cellular processes related to cytoskeletal organization and cellular motility. | ||||||
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, an ADP-ribosylation factor (ARF) activator, indirectly regulates MYH9 through Golgi apparatus dynamics. By disrupting ARF-dependent vesicular trafficking, brefeldin A indirectly influences the localization of MYH9, potentially altering its cellular functions related to membrane trafficking and cytoskeletal organization. | ||||||
Cytochalasin D | 22144-77-0 | sc-201442 sc-201442A | 1 mg 5 mg | $165.00 $486.00 | 64 | |
Cytochalasin D, an actin polymerization inhibitor, indirectly regulates MYH9 by disrupting actin filament formation. By inhibiting actin polymerization, cytochalasin D indirectly affects the interaction between actin and myosin II, potentially altering MYH9-mediated cellular processes related to cytoskeletal organization and cellular motility. | ||||||