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Cytochalasin D

Ultra-pure; inhibits actin polymerization; K+ channel blocker
BML-T109-0001 1 mg 116.00 USD
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Replaces Prod. #: ALX-380-031

Cytochalasin D is a cell-permeable fungal toxin which binds to the barbed end of actin filaments inhibiting both the association and dissociation of subunits. It causes the disruption of actin filaments and inhibition of actin polymerization. It is about 10-fold more effective than cytochalasin B and does not inhibit monosaccharide transport across cell membranes. Inactivates low conductance K+ channels. Modulates CD4 cross-linking in T-lymphocytes and increases intracellular Ca2+ levels. Exhibits antitumor activity. Induces apoptosis.

Product Details

Source:Isolated from Zygosporium mansonii
Purity:≥97% (HPLC, single spot by TLC)
Appearance:White to off-white solid
Solubility:Soluble in methylene chloride (10mg/ml) or DMSO (up to 25mg/ml)
Long Term Storage:-20°C
Handling:Protect from light.
Regulatory Status:RUO - Research Use Only
BML-T109 structure
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BML-T109 structure

Product Literature References

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Merotelic kinetochore attachment in oocyte meiosis II causes sister chromatids segregation errors in aged mice: J. Cheng, et al.; Cell Cycle 15, 140 (2017), Abstract; Full Text
The Role of Arp2/3 in Growth Cone Actin Dynamics and Guidance Is Substrate Dependent: J. Miguel-Ruiz, et al.; J. Neurosci. 17, 5895 (2017), Abstract; Full Text
Filopodia-based Wnt transport during vertebrate tissue patterning: E. Stanganello, et al.; Nat. Commun. 6, 5846 (2015), Application(s): Cell Culture, Abstract;
IQGAP1 regulates actin cytoskeleton organization in podocytes through interaction with nephrin: Y. Liu, et al.; Cell. Signal. 27, 867 (2015), Application(s): Cell Culture, Abstract;
Scavenger receptor for lipoteichoic acid is involved in the potent ability of Lactobacillus plantarum strain L-137 to stimulate production of interleukin-12p40: S. Hatano, et al.; Int. Immunopharmacol. 25, 321 (2015), Application(s): Cell Culture, Assay, Abstract;
The DNA fibers of shrimp hemocyte extracellular traps are essential for the clearance of Escherichia coli: T.H. Ng, et al.; Dev. Comp. Immunol. 48, 229 (2015), Abstract;
A novel 2.5D culture platform to investigate the role of stiffness gradients on adhesion-independent cell migration: M.P. Pebworth, et al.; PLoS One 9, e110453 (2014), Abstract; Full Text
Different contributions of clathrin-and caveolae-mediated endocytosis of vascular endothelial cadherin to lipopolysaccharide-induced vascular : Y. Zhang, et al.; PLoS One 9, e106328 (2014), Abstract; Full Text
The role of the gap junction protein connexin43 in B lymphocyte motility and migration: S. Machtaler, et al.; FEBS Lett. 588, 1249 (2014), Abstract;
Histones trigger sterile inflammation by activating the NLRP3 inflammasome: R. Allam, et al.; Eur. J. Immunol. 43, 3336 (2013), Abstract; Full Text
Noncanonical dendritic cell differentiation and survival driven by a bacteremic pathogen: B. Miles, et al.; J. Leukoc. Biol. 2, 281 (2013), Abstract; Full Text
The signalling imprints of nanoparticle uptake by bone marrow derived dendritic cells: L. Karlson Tde, et al.; Methods 60, 275 (2013), Abstract;
Diabetes-induced increased oxidative stress in cardiomyocytes is sustained by a positive feedback loop involving Rho kinase and PKCβ2.: H. Soliman, et al.; Am. J. Physiol. Heart Circ. Physiol. 303, H989 (2012), Abstract; Full Text
Evidence for Gardnerella vaginalis uptake and internalization by squamous vaginal epithelial cells: implications for the pathogenesis of bacterial vaginosis: C.N. Marrs, et al.; Microbes Infect. 14, 500 (2012), Abstract; Full Text
Staurosporine and cytochalasin D induce chondrogenesis by regulation of actin dynamics in different way: M. Kim, et al.; Exp. Mol. Med. 44, 521 (2012), Abstract; Full Text
Transport of influenza virus neuraminidase (NA) to host cell surface is regulated by ARHGAP21 and Cdc42 proteins: S. Wang, et al.; J. Biol. Chem. 287, 9804 (2012), Abstract; Full Text
Thymosin beta4 inhibits TNF-alpha-induced NF-kappaB activation, IL-8 expression, and the sensitizing effects by its partners PINCH-1 and ILK: P. Qiu, et al.; FASEB J. 25, 1815 (2011), Abstract; Full Text
Keratinocyte growth factor enhances barrier function without altering claudin expression in primary alveolar epithelial cells: M.J. LaFemina, et al.; Am. J. Physiol. Lung Cell. Mol. Physiol. 299, L724 (2010), Abstract; Full Text
Hexokinase translocation during neutrophil activation, chemotaxis, and phagocytosis: disruption by cytochalasin D, dexamethasone, and indomethacin: J.B. Huang, et al.; Cell Immunol. 218, 95 (2002), Abstract;
Disruption of actin microfilaments by cytochalasin D leads to activation of p53: S. N. Rubtsova, et al.; FEBS Lett. 430, 353 (1998), Abstract;
Signaling pathways involved in thrombin-induced cell protection: F.M. Donovan & D.D. Cunningham; J. Biol. Chem. 273, 12746 (1998), Abstract;
The role of actin-binding protein 280 in integrin-dependent mechanoprotection: M. Glogauer, et al.; J. Biol. Chem. 273, 1689 (1998), Abstract;
Myosin-actin interaction plays an important role in human immunodeficiency virus type 1 release from host cells: H. Sasaki, et al.; PNAS 92, 2026 (1995), Abstract;
Cytochalasin D modulates CD4 crosslinking sensitive mitogenic signal in T lymphocytes: A. Aszalos, et al.; Cell. Immunol. 157, 81 (1994), Abstract;
Involvement of actin cytoskeleton in modulation of apical K channel activity in rat collecting duc: W.H. Wang, et al.; Am. J. Physiol. 267, F592 (1994), Abstract;
Effects of cytochalasin and phalloidin on actin: J.A. Cooper ; J. Cell. Biol. 105, 1473 (1987), Abstract;
Actin polymerization. The mechanism of action of cytochalasin D: D.W. Goddette & C. Frieden; J. Biol. Chem. 261, 15974 (1986), Abstract;
Action of cytochalasin D on cytoskeletal networks: M. Schliwa; J. Cell. Biol. 92, 79 (1982), Abstract;
Cytochalasins block actin filament elongation by binding to high affinity sites associated with F-actin: M.D. Flangan & S. Li; J. Biol. Chem. 255, 835 (1980), Abstract;
Antitumor activity of cytochalasin D: K. Katagiri & S. Matsuura; J. Antibiot. (Tokyo) 24, 722 (1971), Abstract;

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