Product Name : |
Phalloidin, Sulforhodamine 101 (Texas-Red) conjugate |
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Catalog Number : |
00033 | |||||||
Unit Size : |
300U | |||||||
Availability : |
In Stock |
Pricing Information:
| Unit Price (1-4 Units) | Unit Price (5 units or more) | Inquire: |
| $230 | $207 | quote@biotium.com |
| • | Price is for US enduser only. International price may vary. Please contact your local distributors for your price. | |
- Description
- Related Products
- References
- Phalloidin and phallacidin are collectively called phallotoxins, which are bicyclic peptides isolated from the deadly Amanita phalloides mushroom. Phallotoxins bind specifically to F-actin filaments with high affinity(1). Fluorescently labeled phallotoxins are very useful tool for investigating the distribution of F-actin. Labeled phallotoxins have similar affinity for both large and small filaments, binding in a stoichiometric ratio of about one phalloidin molecule per actin subunit in muscle and nonmuscle cells from various species of plants and animals. Phallotoxins shift the F-actin monomer/polymer equilibrium toward the polymer, lowering the critical concentration for polymerization up to 30-fold(3,4). Phallotoxins also stabilize F-actin filaments, inhibiting depolymerization by cytochalasins, potassium iodide and elevated temperatures. Moreover, phallotoxin-labeled actin filaments remain functional; labeled glycerinated muscle fibers still contract, and labeled actin filaments still move on solid-phase myosin substrates(5,6). Fluorescent phallotoxins can also be used to quantify the amount of F-actin in cells(7,8).
Sulforhodamine 101 (Texas-Red) Phalloidin binds to F-actin with nanomolar affinity. The red fluorescent phalloidin is typically applied to fixed and permeabilized cells but can also be loaded into live cells via cationic liposomes.
- lex\lem(MeOH) = 591/608nm
- Red solid soluble in MeOH
- Store at -20°C and protect from light
Chemical Structure:
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- Reference:
1. Wieland, T. in Phallotoxins, Springer-Verlag, New York (1986); 2. J Muscle Res Cell Motil 9, 370 (1988); 3. Methods Enzymol 85, 514 (1982); 4. Eur J Biochem 165, 125 (1987); 5. Nature 326, 805 (1987); 6. Proc Natl Acad Sci USA 83, 6272 (1986); 7. Blood

