Phalloidin is a colorless peptide substance isolated from a highly toxic mushroom (Amanita phalloides). It belongs to the toxin peptide toxin and is a strong toxin. Its toxicity is so strong that it has made humans scared. However, scientists have in-depth understanding of it in just a few decades, and rational use of its toxicity, so that it can play an important intrinsic value on the scientific research stage.
Phalloidin usually exists together with amanitin in nature, and its toxicity is weaker than amanitin. The lethal dose to mice is 50 micrograms. It is also very toxic to humans and can cause drooling and vomiting. , Blood in the stool, cyanosis, cramps, muscle contractures, and death. It has the opposite effect to cytochalasin B, and only binds to aggregated microfilaments, not to actin monomer molecules. When combined with the polymerized microfilaments, it inhibits the disintegration of the microfilaments, thereby disrupting the dynamic balance of the polymerization and disaggregation of the microfilaments. By having the toxin attached to a fluorescent dye, researchers can study the inner workings of cells and see how cells divide. Through these observations, they can unravel the mystery of how cancer works and tissue growth.
Two chemists, Scott Rocky and Laura Schuresko, of the University of California, Santa Cruz, created a method called solid-phase synthesis Glu7-Phalloidin, which is a similar substance to ghost pen cyclic peptide. Another scientist (Anderson MO) synthesized another similar substance, alanine 7-Phalloidin.
Researchers at American Peptide Company, USA, Baosheng Liu and Jianheng Zhang have successfully synthesized ghost pen cyclic peptides using a combination of solid-phase synthesis and liquid-phase synthesis. The physical and chemical properties of the chemically synthesized ghost pen cyclopeptide are consistent with the natural ghost pen cyclopeptide extracted from poisonous mushrooms.
FITC and Rhodamin and other fluorescent-labeled ghost pen cyclic peptides can specifically bind to F-actin of eukaryotic cells, thereby showing the distribution of microfilament skeleton in cells.
Based on this principle, Abbkine’s R & D personnel have designed a series of ghost pen cyclic peptide products, providing a variety of different fluorescent group labeled ghost pen cyclic peptides, which can meet the different needs of your multi-label experiments. They are easy to use and reasonably priced, please refer to the following table for details:
|product name||Catalogue NO（Link）|
|TraKine™ F-actin Staining Kit (Green Fluorescence)||KTC4008|
|TraKine™ F-actin Staining Kit (Orange Fluorescence)||KTC4009|
The advantages of phalloidin staining over fluorescent antibodies are as follows:
(1) High affinity: Kd = 20 nM;
(2) Strong specificity: it selectively binds to filamentous actin F-actin without binding to monomeric actin G-actin;
(3) Better than antibody staining: Phalloidin has no species restriction, and there is almost no non-specific staining. The contrast between stained and non-stained areas is extremely obvious;
(4) High sensitivity: nanomolar (nM) staining can meet the experimental requirements;
(5) Good compatibility without affecting the activity of actin: the derivative of phalloidin is very small, about 12-15 Å in diameter, and the molecular weight is less than 2000 Da. Many physiological properties of the labeled actin are maintained;
(6) Wide range of application: no species difference; also applicable to tissue samples after formaldehyde fixation and punching treatment.
Effect of used customer feedback, Tumor tissue section stained with AbFluor™ 594-Phalloidin.
As shown, the nucleus stained with DAPI and Hela cells stained with AbFluor™ 555-Phalloidin.
As shown, the nucleus stained with DAPI and Hela cells stained with AbFluor™ 488-Phalloidin.
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