(-)-BlebbistatinNon muscle myosin II ATPase inhibitor CAS# 856925-71-8 |
- Sodium Orthovanadate
Catalog No.:BCC3856
CAS No.:13721-39-6
- Brefeldin A
Catalog No.:BCC4387
CAS No.:20350-15-6
- BTB06584
Catalog No.:BCC5106
CAS No.:219793-45-0
- Istaroxime hydrochloride
Catalog No.:BCC1661
CAS No.:374559-48-5
- Oligomycin A
Catalog No.:BCC2530
CAS No.:579-13-5
- Omecamtiv mecarbil
Catalog No.:BCC3710
CAS No.:873697-71-3
Quality Control & MSDS
Number of papers citing our products
Chemical structure
3D structure
Cas No. | 856925-71-8 | SDF | Download SDF |
PubChem ID | 5287792 | Appearance | Powder |
Formula | C18H16N2O2 | M.Wt | 292.33 |
Type of Compound | N/A | Storage | Desiccate at -20°C |
Synonyms | (S)-(-)-Blebbistatin | ||
Solubility | DMSO : 10 mg/mL (34.21 mM; Need ultrasonic) H2O : < 0.1 mg/mL (insoluble) | ||
Chemical Name | (3aS)-3a-hydroxy-6-methyl-1-phenyl-2,3-dihydropyrrolo[2,3-b]quinolin-4-one | ||
SMILES | CC1=CC2=C(C=C1)N=C3C(C2=O)(CCN3C4=CC=CC=C4)O | ||
Standard InChIKey | LZAXPYOBKSJSEX-GOSISDBHSA-N | ||
Standard InChI | InChI=1S/C18H16N2O2/c1-12-7-8-15-14(11-12)16(21)18(22)9-10-20(17(18)19-15)13-5-3-2-4-6-13/h2-8,11,22H,9-10H2,1H3/t18-/m1/s1 | ||
General tips | For obtaining a higher solubility , please warm the tube at 37 ℃ and shake it in the ultrasonic bath for a while.Stock solution can be stored below -20℃ for several months. We recommend that you prepare and use the solution on the same day. However, if the test schedule requires, the stock solutions can be prepared in advance, and the stock solution must be sealed and stored below -20℃. In general, the stock solution can be kept for several months. Before use, we recommend that you leave the vial at room temperature for at least an hour before opening it. |
||
About Packaging | 1. The packaging of the product may be reversed during transportation, cause the high purity compounds to adhere to the neck or cap of the vial.Take the vail out of its packaging and shake gently until the compounds fall to the bottom of the vial. 2. For liquid products, please centrifuge at 500xg to gather the liquid to the bottom of the vial. 3. Try to avoid loss or contamination during the experiment. |
||
Shipping Condition | Packaging according to customer requirements(5mg, 10mg, 20mg and more). Ship via FedEx, DHL, UPS, EMS or other couriers with RT, or blue ice upon request. |
Description | Selective inhibitor of myosin II ATPase activity (IC50 ~0.5 - 5 μM); active enantiomer of (±)-blebbistatin. 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 Dilution Calculator
(-)-Blebbistatin Molarity Calculator
1 mg | 5 mg | 10 mg | 20 mg | 25 mg | |
1 mM | 3.4208 mL | 17.104 mL | 34.2079 mL | 68.4158 mL | 85.5198 mL |
5 mM | 0.6842 mL | 3.4208 mL | 6.8416 mL | 13.6832 mL | 17.104 mL |
10 mM | 0.3421 mL | 1.7104 mL | 3.4208 mL | 6.8416 mL | 8.552 mL |
50 mM | 0.0684 mL | 0.3421 mL | 0.6842 mL | 1.3683 mL | 1.7104 mL |
100 mM | 0.0342 mL | 0.171 mL | 0.3421 mL | 0.6842 mL | 0.8552 mL |
* Note: If you are in the process of experiment, it's necessary to make the dilution ratios of the samples. The dilution data above is only for reference. Normally, it's can get a better solubility within lower of Concentrations. |
Calcutta University
University of Minnesota
University of Maryland School of Medicine
University of Illinois at Chicago
The Ohio State University
University of Zurich
Harvard University
Colorado State University
Auburn University
Yale University
Worcester Polytechnic Institute
Washington State University
Stanford University
University of Leipzig
Universidade da Beira Interior
The Institute of Cancer Research
Heidelberg University
University of Amsterdam
University of Auckland
TsingHua University
The University of Michigan
Miami University
DRURY University
Jilin University
Fudan University
Wuhan University
Sun Yat-sen University
Universite de Paris
Deemed University
Auckland University
The University of Tokyo
Korea University
(-)-Blebbistatin is a cell-permeable non-muscle myosin II ATPases inhibitor with an IC50 range of 2 μM [1,2].
Non-muscle myosin II (NM II), an actin-binding protein, plays a central role in regulation of cell migration, adhesion and differentiation [4]. Recent insight into the importance of NM II in these processes has been highlighted by genetic deletion and mutation methods that discovered NM II mutations affect the function of a wide range of proteins and cause monogenic diseases [5.6].
(-)-Blebbistatin is a small molecule inhibitor and preferentially binds to the myosin-ADP-Pi complex to slow down phosphate release [2]. The inhibitor completely eliminate contraction of activity of actin-activated Mg-ATPase and motility of myosins II for several species in vitro (IC50 = 0.5-5.0 μM) [8,9], but it has poor effects on smooth muscle myosin II (IC50 =80 μM) and myosins I,V, and X [3]. Furthermore, blebbistatin can potently inhibit mammalian arterial smooth muscle (IC50=5 μM) [9]. The property that blebbistatin blocks myosin II in an actin-detached state and prevents rigid actomyosin cross-linking is a great advantage in vivo applications [2,11].
In a constant-pressure grant perfusion model system, the CB and TM cells were treated with blebbistatin (10-200 M) and cell morphology was changed, and actin stress fiber content decreased. The blebbistatin effect was completely reversible by washout within 24 hours [10]. Blebbistatin inhibited single cellular contraction without altering the morphologies of intracellular calcium transients (IC50 = 0.43 μM). Exposure to UV light at wavelengths below 488 nm can also cause blebbistatin rapidly suppressed. [8].
References:
[1]. Straight AF, Cheung A, Limouze J, et al. Dissecting temporal and spatial control of cytokinesis with a myosin II Inhibitor. Science, 2003, 299:1743–1747.
[2]. Kovacs M, Toth J, Hetenyi C, Malnasi-Csizmadia A, Sellers JR. Mechanism of blebbistatin inhibition of myosin II. J Biol Chem, 2004, 279:35557–35563.
[3]. Limouze J, Straight AF, Mitchison T, Sellers JR. Specificity of blebbistatin, an inhibitor of myosin II. J Muscle Res Cell Motil, 2004, 25:337–341.
[4]. Miguel Vicente-Manzanares, Xuefei Ma, Robert S. Adelstein,Alan Rick Horwitz. Non-muscle myosin II takes centre stage in cell adhesion and migration.Nat Rev Mol Cell Biol, 2009 Nov, 10(11): 778–790.
[5]. Burt RA, Joseph JE, Milliken S, Collinge JE, Kile BT. Description of a novel mutation leading to MYH9-related disease. Thrombosis Research, 2008, 122(6): 861-863.
[6]. Butcher DT, Alliston T, Weaver VM. A tense situation: forcing tumour progression. Nature Reviews Cancer, 2009 Feb, 9(2):108-122.
[7]. Chen Y, Boukour S, Milloud R, Favier R, Saposnik B, Schlegel N, et al. The abnormal proplatelet formation in MYH9-related macrothrombocytopenia results from an increased actomyosin contractility and is rescued by myosin IIA inhibition. Journal of thrombosis and haemostasis : JTH , 2013, 11:2163-2175.
[8]. Fedorov VV, Lozinsky IT, Sosunov EA, Anyukhovsky EP, Rosen MR, Balke CW, et al. Application of blebbistatin as an excitation-contraction uncoupler for electrophysiologic study of rat and rabbit hearts. Heart rhythm: the official journal of the Heart Rhythm Society, 2007, 4:619-626.
[9]. Zhang X-h, Aydin M, Kuppam D, Melman A, DiSanto ME. In Vitro and In Vivo Relaxation of Corpus Cavernosum Smooth Muscle by the Selective Myosin II Inhibitor, Blebbistatin. The Journal of Sexual Medicine, 2009, 6:2661-2671.
[10]. Zhang M, Rao PV. Blebbistatin, a novel inhibitor of myosin II ATPase activity, increases aqueous humor outflow facility in perfused enucleated porcine eyes. Investigative ophthalmology & visual science, 2005, 46:4130-4138.
[11]. Lucas-Lopez C, Allingham JS, Lebl T, Lawson CP, Brenk R, Sellers JR, et al. The small molecule tool (S)-(-)-blebbistatin: novel insights of relevance to myosin inhibitor design. Organic & biomolecular chemistry, 2008, 6:2076-2084.
- Tedizolid
Catalog No.:BCC1990
CAS No.:856866-72-3
- AM 114
Catalog No.:BCC3589
CAS No.:856849-35-9
- CBiPES hydrochloride
Catalog No.:BCC7824
CAS No.:856702-40-4
- Choline Fenofibrate
Catalog No.:BCC1478
CAS No.:856676-23-8
- Setiptiline maleate
Catalog No.:BCC1946
CAS No.:85650-57-3
- Asenapine
Catalog No.:BCC2476
CAS No.:85650-56-2
- Mirtazapine
Catalog No.:BCC4923
CAS No.:85650-52-8
- Laurycolactone B
Catalog No.:BCN3110
CAS No.:85643-77-2
- Laurycolactone A
Catalog No.:BCN3109
CAS No.:85643-76-1
- Curculigoside
Catalog No.:BCN4406
CAS No.:85643-19-2
- Boc-Ala-NH2
Catalog No.:BCC3046
CAS No.:85642-13-3
- WP1130
Catalog No.:BCC3686
CAS No.:856243-80-6
- alpha-Conidendrin
Catalog No.:BCN4407
CAS No.:85699-62-3
- (3S,3'R,8R,9R,9As)-8-methoxy-3'-methyl-3-[(2S,4S)-4-methyl-5-oxooxolan-2-yl]spiro[1,2,3,5,6,7,8,9a-octahydropyrrolo[1,2-a]azepine-9,5'-oxolane]-2'-one
Catalog No.:BCC9250
CAS No.:85700-47-6
- Scopine HCl
Catalog No.:BCC4940
CAS No.:85700-55-6
- WP1066
Catalog No.:BCC2194
CAS No.:857064-38-1
- TMC353121
Catalog No.:BCC2004
CAS No.:857066-90-1
- PF 915275
Catalog No.:BCC7631
CAS No.:857290-04-1
- 3-Hydroxysarpagine
Catalog No.:BCN4566
CAS No.:857297-90-6
- Isoflavidinin
Catalog No.:BCN7604
CAS No.:85734-02-7
- Retaspimycin
Catalog No.:BCC1889
CAS No.:857402-23-4
- IPI-504 (Retaspimycin hydrochloride)
Catalog No.:BCC2126
CAS No.:857402-63-2
- K-252c
Catalog No.:BCC3706
CAS No.:85753-43-1
- AT7867
Catalog No.:BCC2536
CAS No.:857531-00-1
Block the function of nonmuscle myosin II by blebbistatin induces zebrafish embryo cardia bifida.[Pubmed:25403653]
In Vitro Cell Dev Biol Anim. 2015 Mar;51(3):211-7.
Nonmuscle myosin II (NM II) is the name given to the multi-subunit protein product of three genes encoding different nonmuscle myosin heavy chains including NM II-A, NM II-B, and NM II-C. Blebbistatin is a small molecule that has been shown to be a relatively specific inhibitor of NM II. Blocking the function of NM II by blebbistatin induces zebrafish embryo cardia bifida at a dose-dependent manner. In situ hybridization analysis with ventricular marker ventricular myosin heavy chain (vmhc) and atrial marker atrial myosin heavy chain (amhc) showed each of the heart contained both distinct atria and ventricle. However, the cardia bifida embryos had highly variable distance between two separate ventricles. We also provided evidence that time window from 12 to 20 h post fertilization (hpf) is necessary and sufficient for cardia bifida formation caused by blebbistatin treatment. Expression of spinster homolog 2 (spns2) was decreased in blebbistatin-treated embryos, suggesting the cardia bifida phenotype caused by NM II inhibition was relevant to precardiac mesoderm migration defects. Through in situ hybridization analysis, we showed that foxa1 was expressed in endoderm of blebbistatin-treated embryos at 24-hpf stage, suggesting the endoderm formation is normal in cardia bifida embryos caused by blebbistatin treatment. In addition, we demonstrated that blebbistatin treatment resulted in morphology alteration of zebrafish cardiomyocytes in vivo and neonatal mouse cardiomyocytes in vitro.
The Selective Myosin II Inhibitor Blebbistatin Reversibly Eliminates Gastrovascular Flow and Stolon Tip Pulsations in the Colonial Hydroid Podocoryna carnea.[Pubmed:26605798]
PLoS One. 2015 Nov 25;10(11):e0143564.
Blebbistatin reversibly disrupted both stolon tip pulsations and gastrovascular flow in the colonial hydroid Podocoryna carnea. Epithelial longitudinal muscles of polyps were unaffected by blebbistatin, as polyps contracted when challenged with a pulse of KCl. Latrunculin B, which sequesters G actin preventing F actin assembly, caused stolons to retract, exposing focal adhesions where the tip epithelial cells adhere to the substratum. These results are consistent with earlier suggestions that non-muscle myosin II provides the motive force for stolon tip pulsations and further suggest that tip oscillations are functionally coupled to hydrorhizal axial muscle contraction.
Protein kinase C activation of a blebbistatin sensitive contractile component in the wall of hypertrophying mouse urinary bladder.[Pubmed:25794194]
Neurourol Urodyn. 2015 Feb;34(2):196-202.
AIM: To examine the role of protein kinase C (PKC) and non-muscle myosin in regulation of wall tension in the hypertrophied urinary bladder. METHODS: A partial urinary outflow obstruction was induced in the mouse. Tissue strips from sham operated controls and obstructed bladders were examined in vitro with quantitative gel electrophoresis, immunohistochemistry, and in vitro force recordings. RESULTS: Outlet obstruction (14-18 days) induced a significant growth of the bladder, 73 +/- 6.13 mg compared to 19 +/- 1 13 mg in sham operated controls. The hypertrophying bladder tissue had increased expression of non-muscle myosin B (SMemb) mainly localized to serosa and suburothelium. Direct activation of PKC with PDBu did not alter force in the control urinary bladder. In contrast, PDBu initiated a prominent and sustained contraction which had an increased sensitivity to the myosin type II inhibitor blebbistatin. CONCLUSIONS: PKC activates a significant contractile response in the wall of the hypertrophying urinary bladder, possibly supported by non-muscle myosin. This contractile component is not contributing to the physiological response to muscarinic stimulation, but might be separately regulated by other, yet unknown, mechanisms.
A highly soluble, non-phototoxic, non-fluorescent blebbistatin derivative.[Pubmed:27241904]
Sci Rep. 2016 May 31;6:26141.
Blebbistatin is a commonly used molecular tool for the specific inhibition of various myosin II isoforms both in vitro and in vivo. Despite its popularity, the use of blebbistatin is hindered by its poor water-solubility (below 10 micromolar in aqueous buffer) and blue-light sensitivity, resulting in the photoconversion of the molecule, causing severe cellular phototoxicity in addition to its cytotoxicity. Furthermore, blebbistatin forms insoluble aggregates in water-based media above 10 micromolar with extremely high fluorescence and also high adherence to different types of surfaces, which biases its experimental usage. Here, we report a highly soluble (440 micromolar in aqueous buffer), non-fluorescent and photostable C15 amino-substituted derivative of blebbistatin, called para-aminoblebbistatin. Importantly, it is neither photo- nor cytotoxic, as demonstrated on HeLa cells and zebrafish embryos. Additionally, para-aminoblebbistatin bears similar myosin II inhibitory properties to blebbistatin or para-nitroblebbistatin (not to be confused with the C7 substituted nitroblebbistatin), tested on rabbit skeletal muscle myosin S1 and on M2 and HeLa cells. Due to its drastically improved solubility and photochemical feature, as well as lack of photo- or cytotoxicity, para-aminoblebbistatin may become a feasible replacement for blebbistatin, especially at applications when high concentrations of the inhibitor or blue light irradiation is required.
Specificity of blebbistatin, an inhibitor of myosin II.[Pubmed:15548862]
J Muscle Res Cell Motil. 2004;25(4-5):337-41.
Blebbistatin is a small molecule inhibitor discovered in a screen for inhibitors of nonmuscle myosin IIA. We have examined the specificity and potency of the drug by assaying its effects on the actin-activated MgATPase assay of diverse members of the myosin superfamily. Blebbistatin potently inhibits several striated muscle myosins as well as vertebrate nonmuscle myosin IIA and IIB with IC50 values ranging from 0.5 to 5 microM. Interestingly, smooth muscle which is highly homologous to vertebrate nonmuscle myosin is only poorly inhibited (IC50=80 microM). The drug potently inhibits Dictyostelium myosin II, but poorly inhibits Acanthamoeba myosin II. Blebbistatin did not inhibit representative myosin superfamily members from classes I, V, and X.
Dissecting temporal and spatial control of cytokinesis with a myosin II Inhibitor.[Pubmed:12637748]
Science. 2003 Mar 14;299(5613):1743-7.
Completion of cell division during cytokinesis requires temporally and spatially regulated communication from the microtubule cytoskeleton to the actin cytoskeleton and the cell membrane. We identified a specific inhibitor of nonmuscle myosin II, blebbistatin, that inhibited contraction of the cleavage furrow without disrupting mitosis or contractile ring assembly. Using blebbistatin and other drugs, we showed that exit from the cytokinetic phase of the cell cycle depends on ubiquitin-mediated proteolysis. Continuous signals from microtubules are required to maintain the position of the cleavage furrow, and these signals control the localization of myosin II independently of other furrow components.