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Key Documents

L5163

Sigma-Aldrich

Latrunculin A

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

Sinonimo/i:

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

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About This Item

Formula empirica (notazione di Hill):
C22H31NO5S
Numero CAS:
Peso molecolare:
421.55
Codice UNSPSC:
12352200
ID PubChem:
NACRES:
NA.77

Origine biologica

sea sponge

Livello qualitativo

Saggio

≥85% (HPLC)

Forma fisica

waxy solid

PM

421.6

Solubilità

DMSO: soluble
ethanol: soluble

Temperatura di conservazione

−20°C

Stringa SMILE

C[C@H]1CC[C@@H]2C[C@H](C[C@@](O)(O2)[C@@H]3CSC(=O)N3)OC(=O)C=C(C)CC\C=C\C=C1

InChI

1S/C22H31NO5S/c1-15-7-5-3-4-6-8-16(2)11-20(24)27-18-12-17(10-9-15)28-22(26,13-18)19-14-29-21(25)23-19/h3-5,7,11,15,17-19,26H,6,8-10,12-14H2,1-2H3,(H,23,25)/b4-3+,7-5-,16-11-/t15-,17-,18-,19+,22-/m1/s1
DDVBPZROPPMBLW-IZGXTMSKSA-N

Descrizione generale

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.

Applicazioni

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

Azioni biochim/fisiol

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

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)


Certificati d'analisi (COA)

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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
Peter J Wen et al.
Nature communications, 7, 12604-12604 (2016-09-01)
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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
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