Phalloidin-PEG4-DBCO
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 mg | 0.5 mg | 1 mg | 5 mg | 10 mg | |
1 mM | 73.177 µL | 365.885 µL | 731.77 µL | 3.659 mL | 7.318 mL |
5 mM | 14.635 µL | 73.177 µL | 146.354 µL | 731.77 µL | 1.464 mL |
10 mM | 7.318 µL | 36.588 µL | 73.177 µL | 365.885 µL | 731.77 µL |
Molarity calculator
Enter any two values (mass, volume, concentration) to calculate the third.
Mass (Calculate) | Molecular weight | Volume (Calculate) | Concentration (Calculate) | Moles | ||||
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Product family
Name | Excitation (nm) | Emission (nm) | Extinction coefficient (cm -1 M -1) | Quantum yield | Correction Factor (260 nm) | Correction Factor (280 nm) |
XFD488 PEG4 DBCO | 499 | 520 | 71000 | 0.921 | 0.30 | 0.11 |
XFD350 PEG4 DBCO | 343 | 441 | 19000 | - | 0.25 | 0.19 |
XFD405 PEG4 DBCO | 401 | 421 | 35,000 | - | 0.23 | 0.70 |
XFD430 PEG4 DBCO | 432 | 540 | 15,000 | - | - | 0.28 |
XFD514 PEG4 DBCO | 518 | 543 | 80000 | - | 0.31 | 0.18 |
XFD546 PEG4 DBCO | 561 | 572 | 112000 | 0.791 | 0.21 | 0.12 |
XFD532 PEG4 DBCO | 534 | 553 | 81000 | 0.611 | 0.24 | 0.09 |
XFD568 PEG4 DBCO | 579 | 603 | 91300 | 0.691 | 0.45 | 0.46 |
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
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
Authors: Holzinger, A., Blaas, K.
Journal: Methods Mol Biol (2016): 243-61
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
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
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
Authors: Lu, Y. F., Liu, J., Wu, K. C., Klaassen, C. D.
Journal: Toxicol Lett (2015): 326-32
CLSM Analysis of the Phalloidin-Stained Muscle System of the Nemertean Proboscis and Rhynchocoel
Authors: Chernyshev, A. V.
Journal: Zoolog Sci (2015): 547-60
Authors: Chernyshev, A. V.
Journal: Zoolog Sci (2015): 547-60
References
View all 151 references: Citation Explorer
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Journal: ACS Applied Materials & Interfaces (2017)
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