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P5282

Sigma-Aldrich

Phalloidin Peptide

≥90% (HPLC), solid, FITC labeled

Synonym(s):

Phalloidin-FITC

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0.1 MG
CHF 359.00

CHF 359.00


Estimated to ship on28 March 2025


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0.1 MG
CHF 359.00

About This Item

Empirical Formula (Hill Notation):
C56H60N10O15S2
Molecular Weight:
1177.26
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.32

CHF 359.00


Estimated to ship on28 March 2025


Request a Bulk Order

Product Name

Phalloidin, Fluorescein Isothiocyanate Labeled, sequence Amanita phalloides(synthetic: peptide sequence)

biological source

sequence from Amanita phalloides (synthetic: peptide sequence)

Quality Level

form

solid

fluorescence

λex 495 nm; λem 520 nm(lit.)

storage temp.

−20°C

General description

Phalloidin is a phallotoxin produced by death cap mushroom Amanita phalloides. It is a cyclic peptide, which interacts with actin and this was first identified in phalloidin-poisoned rats. It is a heptapeptide, cyclic in nature, with a crosslink between tryptophan at position 6 and cysteine at position 3.[1] The side chain of amino acid 7 (γ-δ-dihydroxyleucine) in phalloidin, is accessible to modifications, through which fluorescently labelled phalloidin compounds can be produced.[2]

Application

Phalloidin, Fluorescein Isothiocyanate Labeled has been used:
  • To visualize F-Actin reorganization in primary neonatal cardiomyocytes (PNCMs) and H9C2 cells (rat cardiac myoblasts) following endothelin-1 (ET-1) and angiotensin II (Ang II) treatment.[3]
  • In immunochemistry to label microfilament.[4]
  • In immunofluorescence analysis to stain F-actin.[5]

Biochem/physiol Actions

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.[1] 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.[2]
Toxin that binds polymeric F actin, stabilizing it and interfering with the function of actin-rich structures.

Pictograms

Skull and crossbones

Signal Word

Danger

Hazard Statements

Hazard Classifications

Acute Tox. 2 Dermal - Acute Tox. 2 Inhalation - Acute Tox. 2 Oral

Storage Class Code

6.1A - Combustible acute toxic Cat. 1 and 2 / very toxic hazardous materials

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Non-muscle myosin heavy chain as a possible target for protein encoded by metastasis-related mts-1 gene.
Kriajevska MV
The Journal of Biological Chemistry, 19679-82, 269(31)-269(31) (1994)
The culture of fibroblasts from diaphragm of giant panda.
Han ZM
In Vitro Cellular & Developmental Biology. Animal, 37(10), 644-645 (2001)
Ting Xu et al.
Journal of leukocyte biology, 84(4), 1192-1201 (2008-07-26)
Recruitment of leukocytes onto inflamed tissues is an important physiological event, in which L-selectin plays an essential role in initial leukocyte capture and at the same time, triggers cell signaling. Lck is a member of the Src family of protein
Fluorescent phallotoxin, a tool for the visualization of cellular actin.
Wulf E
Proceedings of the National Academy of Sciences of the USA, 76(9), 4498-4502 (1979)
The H9C2 cell line and primary neonatal cardiomyocyte cells show similar hypertrophic responses in vitro.
Watkins SJ
In Vitro Cellular & Developmental Biology. Animal, 47(2), 125-131 (2011)

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Questions

1–7 of 7 Questions  
  1. Is it possible to use P5282 with cells fixed in paraformaldehyde instead of methanol-free formaldehyde?

    1 answer
    1. Using P5282 with cells fixed in paraformaldehyde instead of methanol-free formaldehyde was attempted, but the results were not satisfactory with regular formaldehyde. A specific protocol for the reconstitution of Phalloidin P5282-.1MG in the case of tissues fixed in paraformaldehyde and included in O.C.T medium is not available. However, it is suggested to find relevant information in the literature, such as in this article, https://www.oncotarget.com/article/25259/ DOI:[10.18632/oncotarget.25259].

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  2. How do I prepare stock solutions of Product P5282, Phalloidin, Fluorescein Isothiocyanate Labeled?

    1 answer
    1. Stock solutions of  phalloidin conjugates have been made in methanol or DMSO at 0.1 to 5 mg/mL. Make final dilutions in aqueous physiological buffers for a staining range from 0.1 μM to 100 μM with corresponding incubation times of 15 minutes to 72 hours.

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  3. How do I store Product P5282, Phalloidin, Fluorescein Isothiocyanate Labeled?

    1 answer
    1. The product should be stored at a powder in the freezer at -20°C.

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  4. What is the Department of Transportation shipping information for this product?

    1 answer
    1. Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product.

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  5. How do I dissolve Product P5282, Phalloidin, Fluorescein Isothiocyanate Labeled?

    1 answer
    1. This product is soluble in methanol, ethanol, butanol and pyridine. It is soluble in cold water at a concentration of 5 mg/mL; it is much more soluble in hot water. See: The chemicals encyclopedia published by the Royal Society of Chemistry, 12th ed., entry# 7336 (1996). Solutions should be prepared fresh, and protected from light whenever possible.

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  6. How do I stain cells with Product P5282, Phalloidin, Fluorescein Isothiocyanate Labeled?

    1 answer
    1. A typical application for staining cells can be found in the product information sheet (under Documents, above).

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  7. What are the excitation and emission wavelengths used for fluorescent detection of Product P5282, Phalloidin, Fluorescein Isothiocyanate Labeled?

    1 answer
    1. Excitation wavelengths of 540-545 nm and emission wavelengths of 570-573 nm can be used. See: Faulstich, H., J. Muscle Res. Cell Motility, 9, 370 (1988), and Waggoner, A. et al., Methods in Cell Biology, 30, 449 (1989).

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