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Phalloidin-PEG4-DBCO

Chemical structure for Phalloidin-PEG4-DBCO.
Chemical structure for Phalloidin-PEG4-DBCO.
Ordering information
Price ()
Catalog Number5303
Unit Size
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Additional ordering information
Telephone1-408-733-1055
Fax1-408-733-1304
Emailsales@aatbio.com
InternationalSee distributors
ShippingStandard overnight for United States, inquire for international
Physical properties
Molecular weight1366.55
SolventDMSO
Storage, safety and handling
H-phraseH303, H313, H333
Hazard symbolXN
Intended useResearch Use Only (RUO)
R-phraseR20, R21, R22
StorageFreeze (< -15 °C); Minimize light exposure
UNSPSC12352200

OverviewpdfSDSpdfProtocol


Molecular weight
1366.55
Phalloidin, a bicyclic heptapeptide toxin, binds specifically at the interface between F-actin subunits, locking adjacent subunits together. Phalloidin binds to actin filaments much more tightly than to actin monomers, leading to a decrease in the rate constant for the dissociation of actin subunits from filament ends, essentially stabilizing actin filaments through the prevention of filament depolymerization. Moreover, phalloidin is found to inhibit the ATP hydrolysis activity of F-actin. Thus, phalloidin traps actin monomers in a conformation distinct from G-actin and it stabilizes the structure of F-actin by greatly reducing the rate constant for monomer dissociation, an event associated with the trapping of ADP. Phalloidin functions differently at various concentrations in cells. When introduced into the cytoplasm at low concentrations, phalloidin recruits the less polymerized forms of cytoplasmic actin as well as filamin into stable "islands" of aggregated actin polymers, yet it does not interfere with stress fibers, i.e. thick bundles of microfilaments. The property of phalloidin is a useful tool for investigating the distribution of F-actin in cells by labeling phalloidin with fluorescent analogs and using them to stain actin filaments for light microscopy. Fluorescent derivatives of phalloidin have turned out to be enormously useful in localizing actin filaments in living or fixed cells as well as for visualizing individual actin filaments in vitro. Fluorescent phalloidin derivatives have been used as an important tool in the study of actin networks at high resolution. AAT Bioquest offers a variety of fluorescent phalloidin derivatives with different colors for multicolor imaging applications. Phalloidin-PEG4-DBCO can be readily used for conjugations with azido-containing molecules.

Calculators


Common stock solution preparation

Table 1. Volume of DMSO needed to reconstitute specific mass of Phalloidin-PEG4-DBCO to given concentration. Note that volume is only for preparing stock solution. Refer to sample experimental protocol for appropriate experimental/physiological buffers.

0.1 mg0.5 mg1 mg5 mg10 mg
1 mM73.177 µL365.885 µL731.77 µL3.659 mL7.318 mL
5 mM14.635 µL73.177 µL146.354 µL731.77 µL1.464 mL
10 mM7.318 µL36.588 µL73.177 µL365.885 µL731.77 µL

Molarity calculator

Enter any two values (mass, volume, concentration) to calculate the third.

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Citations


View all 9 citations: Citation Explorer
Staining Fission Yeast Filamentous Actin with Fluorescent Phalloidin Conjugates
Authors: Hagan, I. M.
Journal: Cold Spring Harb Protoc (2016): se name="My EndNote Library.enl" path="C:\Use
Actin-Dynamics in Plant Cells: The Function of Actin-Perturbing Substances: Jasplakinolide, Chondramides, Phalloidin, Cytochalasins, and Latrunculins
Authors: Holzinger, A., Blaas, K.
Journal: Methods Mol Biol (2016): 243-61
CLSM Analysis of the Phalloidin-Stained Muscle System of the Nemertean Proboscis and Rhynchocoel
Authors: Chernyshev, A. V.
Journal: Zoolog Sci (2015): 547-60
Protection against phalloidin-induced liver injury by oleanolic acid involves Nrf2 activation and suppression of Oatp1b2
Authors: Lu, Y. F., Liu, J., Wu, K. C., Klaassen, C. D.
Journal: Toxicol Lett (2015): 326-32
Impact of C24:0 on actin-microtubule interaction in human neuronal SK-N-BE cells: evaluation by FRET confocal spectral imaging microscopy after dual staining with rhodamine-phalloidin and tubulin tracker green
Authors: Zarrouk, A., Nury, T., Dauphin, A., Frere, P., Riedinger, J. M., Bachelet, C. M., Frouin, F., Moreau, T., Hammami, M., Kahn, E., Lizard, G.
Journal: Funct Neurol (2015): 33-46
Amatoxins (alpha- and beta-Amanitin) and phallotoxin (Phalloidin) analyses in urines using high-resolution accurate mass LC-MS technology
Authors: Gicquel, T., Lepage, S., Fradin, M., Tribut, O., Duretz, B., Morel, I.
Journal: J Anal Toxicol (2014): 335-40
Permeation of fluorophore-conjugated phalloidin into live hair cells of the inner ear is modulated by P2Y receptors
Authors: Thiede, B. R., Corwin, J. T.
Journal: J Assoc Res Otolaryngol (2014): 13-30
Single-molecule super-resolution imaging by tryptophan-quenching-induced photoswitching of phalloidin-fluorophore conjugates
Authors: Nanguneri, S., Flottmann, B., Herrmannsdorfer, F., Thomas, K., Heilemann, M.
Journal: Microsc Res Tech (2014): 510-6
Ultrastructural localization of F-actin using phalloidin and quantum dots in HL-60 promyelocytic leukemia cell line after cell death induction by arsenic trioxide
Authors: Izdebska, M., Gagat, M., Grzanka, D., Grzanka, A.
Journal: Acta Histochem (2013): 487-95

References


View all 151 references: Citation Explorer
Enhanced bovine serum albumin absorption on the N-hydroxysuccinimide activated graphene oxide and its corresponding cell affinity
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Journal: Materials Science and Engineering: C (2017)
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Journal: ACS Applied Materials & Interfaces (2017)
The correlation between osteopontin adsorption and cell adhesion to mixed self-assembled monolayers of varying charges and wettability
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Journal: Biomaterials Science (2017)
Study on the Regulation of Focal Adesions and Cortical Actin by Matrix Nanotopography in 3D Environment
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Journal: RSC Advances (2017): 46472--46479
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Paxillin facilitates timely neurite initiation on soft-substrate environments by interacting with the endocytic machinery
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Biomaterial Surface Can Modify HUVEC Morphology and Inflammatory Response by Regulating MicroRNA Expression
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DNA Double-Strand Breaks Induce the Nuclear Actin Filaments Formation in Cumulus-Enclosed Oocytes but Not in Denuded Oocytes
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