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Mushroom

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A2263 α-Amanitin from Amanita phalloides, ≥90% (HPLC), powder The major toxic constituent of the mushroom, Amanita phalloides, inhibits eukaryotic RNA polymerase II and III, but does not inhibit RNA polymerase I or bacterial RNA polymerase. Inhibits mammalian protein synthesis.
A1304 β-Amanitin from Amanita phalloides ~90% (HPLC) Toxic constituent of the mushroom, Amanita phalloides, inhibits eukaryotic RNA polymerase II and III, but not RNA polymerase I or bacterial RNA polymerase. Inhibits mammalian protein synthesis.
A8100 β-Amanitin–poly-L-lysine bound ≥85% Toxic constituent of the mushroom, Amanita phalloides, inhibits eukaryotic RNA polymerase II and III, but not RNA polymerase I or bacterial RNA polymerase. Inhibits mammalian protein synthesis.
P2141 Phalloidin from Amanita phalloides ≥90% Phalloidin interacts with polymeric actin, and not oligomeric or monomeric forms. This interaction leads to highly stabilized actin filaments, which resist depolymerization and disassembly. In rats, this toxin causes death due to liver hemorrhage and cells show abnormal actin clustering. The affinity of phalloidin to actin is not significantly altered after derivatizing fluorescently labelled phalloidin compounds. These compounds can be used to study actin structure and organization within eukaryotic cells.
Toxin that binds polymeric F actin, stabilizing it and interfering with the function of actin-rich structures.
P8716 Phalloidin, Biotin Labeled ≥90% Shown to bind actin filaments and streptavidin simultaneously, due to the longer space between the two active components.
Toxin that binds polymeric F actin, stabilizing it and interfering with the function of actin-rich structures.
P5282 Phalloidin, Fluorescein Isothiocyanate Labeled Phalloidin from Amanita phalloides Phalloidin interacts with polymeric actin, and not oligomeric or monomeric forms. This interaction leads to highly stabilized actin filaments, which resist depolymerization and disassembly. In rats, this toxin causes death due to liver hemorrhage, and cells show abnormal actin clustering. The affinity of phalloidin to actin is not significantly altered after derivatizing fluorescently labelled phalloidin compounds. These compounds can be used to study actin structure and organization within eukaryotic cells.
Toxin that binds polymeric F actin, stabilizing it and interfering with the function of actin-rich structures.
P0243 Phalloidin, poly-L-Lysine bound ≥90% It is predicted that poly-L-lysine bound phalloidin is approximately 100 fold more potent than the unbound form.
Toxin that binds polymeric F actin, stabilizing it and interfering with the function of actin-rich structures.
P1951 Phalloidin–Tetramethylrhodamine B isothiocyanate Phalloidin from Amanita phalloides Phalloidin interacts with polymeric actin, and not oligomeric or monomeric forms. This interaction leads to highly stabilized actin filaments, which resist depolymerization and disassembly. In rats, this toxin causes death due to liver hemorrhage, and cells show abnormal actin clustering. The affinity of phalloidin to actin is not significantly altered after derivatizing florescent labelled phalloidin compounds. These compounds can be used to study actin structure and organization within eukaryotic cells.
Toxin that binds polymeric F actin, stabilizing it and interfering with the function of actin-rich structures.