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Latrunculin A

from sea sponge, ≥85% (HPLC), waxy solid

LAT-A, [1R-[1R*, 4Z, 8E, 10Z, 12S*, 15R*, 17R*(R*)]]-4-(17-Hydroxy-5,12-dimethyl-3-oxo-2,16-dioxabicyclo[13.3.1]nonadeca-4,8,10-trien-17-yl)-2-thiazolidinone
Empirical Formula (Hill Notation):
CAS Number:
Molecular Weight:
PubChem Substance ID:

Quality Level

biological source

sea sponge


≥85% (HPLC)


waxy solid

mol wt



DMSO: soluble
ethanol: soluble

storage temp.


SMILES string




InChI key


General description

Latrunculin A, a toxin extracted from the red sea sponge Latrunculia magnifica. It participates in vitro in the morphological alteration of the polymerization of pure actin. It forms a complex by binding with the nucleotide cleft of actin for actin filaments elongation.


Latrunculin A has been used as medium supplementation for A549 cells to determine the internalization mechanism of CAV9 in A549 human lung carcinoma cells.

Biochem/physiol Actions

Latrunculin A inhibits actin polymerization by a different mechanism than cytochalasins. Latrunculin A disrupts microfilament-mediated processes.

Storage Class Code

13 - Non Combustible Solids



Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificate of Analysis

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Certificate of Origin

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More Documents

Quotes and Ordering

Peter J Wen et al.
Nature communications, 7, 12604-12604 (2016-09-01)
Vesicle fusion is executed via formation of an Ω-shaped structure (Ω-profile), followed by closure (kiss-and-run) or merging of the Ω-profile into the plasma membrane (full fusion). Although Ω-profile closure limits release but recycles vesicles economically, Ω-profile merging facilitates release but
Zhanghan Wu et al.
Nature communications, 9(1), 136-136 (2018-01-13)
Immune cells exhibit stimulation-dependent traveling waves in the cortex, much faster than typical cortical actin waves. These waves reflect rhythmic assembly of both actin machinery and peripheral membrane proteins such as F-BAR domain-containing proteins. Combining theory and experiments, we develop
E G Yarmola et al.
The Journal of biological chemistry, 275(36), 28120-28127 (2000-06-22)
Latrunculin A is used extensively as an agent to sequester monomeric actin in living cells. We hypothesize that additional activities of latrunculin A may be important for its biological activity. Our data are consistent with the formation of a 1:1
M Coué et al.
FEBS letters, 213(2), 316-318 (1987-03-23)
Latrunculin A, a toxin purified from the red sea sponge Latrunculia magnifica, was found previously to induce striking reversible changes in the morphology of mammalian cells in culture and to disrupt the organization of their microfilaments. We now provide evidence
Keiichiro Kushiro et al.
Scientific reports, 7(1), 4244-4244 (2017-06-28)
During metastasis, cancer cells are exposed to various three-dimensional microstructures within the body, but the relationship between cancer migration and three-dimensional geometry remain largely unclear. Here, such geometric effects on cancerous cells were investigated by characterizing the motility of various

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