GF®594 Phalloidin标记鬼笔环肽
货号:JXF40171-300T
规格:300T
价格:1200元
NTRODUCTION
Phalloidin is a bicyclic peptide that belongs to a family of toxins isolated from the deadly Amanita
phalloides mushroom. Fluorescent phalloid ins bind F-actin with nanomolar affinity and are water soluble,
thus providing convenient probes for labeling, identifying, and quantifying F-actin in cryopreserved tissue sections,
cell cultures, or cell-free experiments. halloid in contains an unusual thioether bridge between cysteine and
tryptophan residues that forms an inner ring structure. At elevated pH, this thioether is cleaved and the toxin loses
its affinity for actin. Fluorescently labeled phalloid ins stain F-actin at nanomolarconcentrations. Labeled phalloidins
have similar affinity for both large and small filaments, binding in a stoichiometric ratio of about one phalloid in
molecule per actin subunit in muscle and non-muscle cells from various species of plants and animals.
Different from antibodies, the binding affinity of phalloid in does not change significantly with actin among different
species.Non-specific staining is negligible, and the contrast between stained and unstained areas is extremely large.
Phalloid in shifts the monomer/polymer equilibrium toward the polymer, lowering the critical concentration for
polymerization up to 30-fold. Phallotoxins also stabilize F-actin, inhibiting depolymerization by cytochalasin, potassium iodide and elevated temperatures. Because the phalloidin conjugates are small, with an approximate diameter of 12-15Å
and molecular weight of <2000 Daltons, a variety of actin-binding proteins including myosin, tropomyosin and troponin
can still bind to actin after treatment with phalloidin. Even more significantly, phalloid in-labeled actin filaments remain
functional; labeled glycerinated muscle fibers still contract, and labeled actin filaments still move on solid-phase myosin
substrates. Fluorescent phalloid in can also be used to quantify the amount of F-actin in cells.
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