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AAT Bioquest

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 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

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Product family

NameExcitation (nm)Emission (nm)Extinction coefficient (cm -1 M -1)Quantum yieldCorrection Factor (260 nm)Correction Factor (280 nm)
XFD488 PEG4 DBCO499520710000.9210.300.11
XFD350 PEG4 DBCO34344119000-0.250.19
XFD405 PEG4 DBCO40142135,000-0.230.70
XFD430 PEG4 DBCO43254015,000--0.28
XFD514 PEG4 DBCO51854380000-0.310.18
XFD546 PEG4 DBCO5615721120000.7910.210.12
XFD532 PEG4 DBCO534553810000.6110.240.09
XFD568 PEG4 DBCO579603913000.6910.450.46

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
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
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
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
CLSM Analysis of the Phalloidin-Stained Muscle System of the Nemertean Proboscis and Rhynchocoel
Authors: Chernyshev, A. V.
Journal: Zoolog Sci (2015): 547-60

References

View all 151 references: Citation Explorer
DNA Double-Strand Breaks Induce the Nuclear Actin Filaments Formation in Cumulus-Enclosed Oocytes but Not in Denuded Oocytes
Authors: Sun, Ming-Hong and Yang, Mo and Xie, Feng-Yun and Wang, Wei and Zhang, Lili and Shen, Wei and Yin, Shen and Ma, Jun-Yu
Journal: PloS one (2017): e0170308
Biomaterial Surface Can Modify HUVEC Morphology and Inflammatory Response by Regulating MicroRNA Expression
Authors: Gu, Shuangying and Tian, Baoxiang and Chen, Weicong and Zhou, Yue
Journal: Journal of Biosciences and Medicines (2017): 8
Paxillin facilitates timely neurite initiation on soft-substrate environments by interacting with the endocytic machinery
Authors: Chang, Ting-Ya and Chen, Chen and Lee, Min and Chang, Ya-Chu and Lu, Chi-Huan and Lu, Shao-Tzu and Wang, De-Yao and Wang, Aijun and Guo, Chin-Lin and Cheng, Pei-Lin
Journal: eLife (2017): e31101
Enhanced bovine serum albumin absorption on the N-hydroxysuccinimide activated graphene oxide and its corresponding cell affinity
Authors: Xiong, Kun and Fan, Qingbo and Wu, Tingting and Shi, Haishan and Chen, Lin and Yan, Minhao
Journal: Materials Science and Engineering: C (2017)
Cell-Permeable, MMP-2 Activatable, Nickel Ferrite and His-tagged Fusion Protein Self-Assembled Fluorescent Nanoprobe for Tumor Magnetic Targeting and Imaging
Authors: Sun, Lu and Xie, Shuping and Qi, Jing and Liu, Ergang and Liu, Di and Liu, Quan and Chen, Sunhui and He, Huining and Yang, Victor C
Journal: ACS Applied Materials & Interfaces (2017)
Page updated on October 8, 2024

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Catalog Number5303
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Physical properties

Molecular weight

1366.55

Solvent

DMSO

Storage, safety and handling

H-phraseH303, H313, H333
Hazard symbolXN
Intended useResearch Use Only (RUO)
R-phraseR20, R21, R22

Storage

Freeze (< -15 °C); Minimize light exposure
UNSPSC12352200
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