674289-55-5

Bright Yellow Solid

Blebbistatin blocked myosin II-dependent cell processes. It blocks cell blebbing rapidly and reversibly. Also rapidly disrupted directed cell migration and cytokinesis in vertebrate cell. It blocks both blebbing and cytokinesis at 50-100. A ne

Blebbistatin blocked myosin II-dependent cell processes. It blocks cell blebbing rapidly and reversibly. Also rapidly disrupted directed cell migration and cytokinesis in vertebrate cell. It blocks both blebbing and cytokinesis at 50-100. [a]D

Blebbistatin blocked myosin II-dependent cell processes. It blocks cell blebbing rapidly and reversibly. Also rapidly disrupted directed cell migration and cytokinesis in vertebrate cell. It blocks both blebbing and cytokinesis at 50-100μM. (±)-1-Phenyl-1,2,3,4-tetrahydro-4-hydroxypyrrolo[2,3-b]-7-methylquinolin-4-one Selective inhibitor of nonmuscle myosin II; inhibits contraction of the cleavage furrow without disrupting mitosis or contractile ring assembly. Rapidly and reversibly blocks cell blebbing, and disrupts directed cell migration and cytokinesis in vertebrate cells.

ChEBI: A pyrroloquinoline that is 1,2,3,3a-tetrahydro-H-pyrrolo[2,3-b]quinolin-4-one substituted by a hydroxy group at position 3a, a methyl group at position 6 and a phenyl group at position 1. It acts as an inhibitor of ATPase ac ivity of non-muscle myosin II.

(±)-Blebbistatin is a selective cell-permeable inhibitor of non-muscle myosin II ATPases. It rapidly and reversibly inhibits Mg-ATPase activity and in vitro motility of non-muscle myosin IIA and IIB for several species (IC50 = 0.5-5.0 μM), while poorly inhibiting smooth muscle myosin (IC50 = 80 μM). Through these effects, blebbistatin blocks apoptosis-related bleb formation, directed cell migration and cytokinesis in vertebrate cells. Blebbistatin is inactivated by UV light, which may be particularly important in fluorescent cell imaging applications. Purified enantiomers of Blebbistatin are also available from Cayman ((?)-Blebbistatin - ).

Selective inhibitor of myosin II ATPase activity; inhibits contraction of the cleavage furrow without disrupting mitosis or contractile ring assembly. Rapidly and reversibly blocks cell blebbing, and disrupts directed cell migration and cytokinesis in vertebrate cells.

(±)-Blebbistatin is a racemic mixture of (–)-blebbistatin and (+)-blebbistatin , the active and inactive forms, respectively. (–)-Blebbistatin is a selective cell-permeable inhibitor of non-muscle myosin II ATPases. (–)-Blebbistatin rapidly and reversibly inhibits Mg-ATPase activity and in vitro motility of non-muscle myosin IIA and IIB for several species (IC₅₀s = 0.5-5 μM), while poorly inhibiting smooth muscle myosin (IC₅₀ = 8 μM). Through these effects, (–)-blebbistatin blocks apoptosis-related bleb formation, directed cell migration, and cytokinesis in vertebrate cells. However, prolonged exposure to blue light (450-490 nm) results in degradation of blebbistatin to an inactive product via cytotoxic intermediates, which may be problematic for its use in fluorescent live cell imaging applications. (S)-nitro-Blebbistatin and (R)-nitro-blebbistatin are more stable forms of (–)-blebbistatin and (+)-blebbistatin, respectively. The addition of a nitro group stabilizes the molecules to circumvent their degradation by prolonged blue light exposure. (S)-nitro-Blebbistatin and (R)-nitro-blebbistatin have the same stereochemistry of the active and inactive enantiomers, respectively.

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[1] AARON F. STRAIGHT. Dissecting Temporal and Spatial Control of Cytokinesis with a Myosin II Inhibitor[J]. Science, 2003, 299 5613. DOI: 10.1126/science.1081412
[2] MIHáLY KOVáCS. Mechanism of blebbistatin inhibition of myosin II.[J]. The Journal of Biological Chemistry, 2004, 279 34: 35557-35563. DOI: 10.1074/jbc.m405319200
[3] JOHN LIMOUZE. Specificity of blebbistatin, an inhibitor of myosin II.[J]. Journal of Muscle Research and Cell Motility, 2004, 25 4-5: 337-341. DOI: 10.1007/s10974-004-6060-7
[4] KOLEGA J. Phototoxicity and photoinactivation of blebbistatin in UV and visible light[J]. Biochemical and biophysical research communications, 2004, 320 3: Pages 1020-1025. DOI: 10.1016/j.bbrc.2004.06.045
[5] TAKESHI SAKAMOTO. Blebbistatin, a Myosin II Inhibitor, Is Photoinactivated by Blue Light[J]. Biochemistry Biochemistry, 2004, 44 2: 584-588. DOI: 10.1021/bi0483357
[6] CRISTINA LUCAS-LOPEZ. Absolute Stereochemical Assignment and Fluorescence Tuning of the Small Molecule Tool, (–)-Blebbistatin[J]. European Journal of Organic Chemistry, 2005, 2005 9: 1736-1740. DOI: 10.1002/ejoc.200500103