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L5163

Sigma-Aldrich

Latrunculin A

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

Sinônimo(s):

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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100 μG
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100 μG
R$ 2.973,00

About This Item

Fórmula empírica (Notação de Hill):
C22H31NO5S
Número CAS:
Peso molecular:
421.55
Código UNSPSC:
12352200
ID de substância PubChem:
NACRES:
NA.77

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fonte biológica

sea sponge

Nível de qualidade

Ensaio

≥85% (HPLC)

Formulário

waxy solid

peso molecular

421.6

solubilidade

DMSO: soluble
ethanol: soluble

temperatura de armazenamento

−20°C

cadeia de caracteres SMILES

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

chave InChI

DDVBPZROPPMBLW-IZGXTMSKSA-N

Descrição geral

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.[1] It forms a complex by binding with the nucleotide cleft of actin for actin filaments elongation.[2]

Aplicação

Latrunculin A has been used as medium supplementation for A549 cells to determine the internalization mechanism of CAV9 in A549 human lung carcinoma cells.[3]

Ações bioquímicas/fisiológicas

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

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, type N95 (US)


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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
Maureen Möckel et al.
Journal of virology, 93(16) (2019-05-31)
Dynamin GTPases, best known for their role in membrane fission of endocytic vesicles, provide a target for viruses to be exploited during endocytic uptake. Recently, we found that entry of herpes simplex virus 1 (HSV-1) into skin cells depends on
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
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

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