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Key Documents

428021

Sigma-Aldrich

Latrunculin A

from Latrunculia magnifica, ≥95% (HPLC), solid, actin polymerization inhibitor, Calbiochem

Synonym(s):

Latrunculin A, Latrunculia magnifica

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About This Item

Empirical Formula (Hill Notation):
C22H31NO5S
CAS Number:
Molecular Weight:
421.55
UNSPSC Code:
12352200
NACRES:
NA.77

product name

Latrunculin A, Latrunculia magnifica, Latrunculin A, CAS 76343-93-6, is a cell-permeable marine toxin that disrupts microfilament organization in cultured cells by the formation of a 1:1 complex with monomeric G-actin (KD = 200 nM).

Quality Level

Assay

≥95% (HPLC)

form

solid

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze
protect from light

color

white

solubility

DMSO: 25 mg/mL

shipped in

ambient

storage temp.

−20°C

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

InChI key

DDVBPZROPPMBLW-IZGXTMSKSA-N

General description

A cell-permeable marine toxin from the Red Sea sponge Latrunculia magnifica that disrupts microfilament organization in cultured cells by the formation of a 1:1 complex with monomeric G-actin (Kd = 200 nM). Also a potent inhibitor of microfilament-mediated processes in sperm, eggs, and embryos.
A cell-permeable marine toxin that disrupts microfilament organization in cultured cells by the formation of a 1:1 complex with monomeric G-actin (Kd = 200 nM). Also a potent inhibitor of microfilament-mediated processes in sperm, eggs, and embryos. A 1 mM (50 µg/119 µl) solution of Latrunculin A, Latrunculia magnifica Cat. No. 428026 in DMSO is also available.

Biochem/physiol Actions

Cell permeable: yes
Kd = 200 nM in formation of a 1:1 complex with monomeric G-actin
Primary Target
G-actin
Product does not compete with ATP.
Reversible: no

Packaging

Packaged under inert gas

Warning

Toxicity: Harmful (C)

Reconstitution

Following reconstitution aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.

Other Notes

Ayscough, K.R., et al. 1997. J. Cell Biol. 137, 399.
Spector, I., et al. 1989. Cell Motil. Cytoskeleton 13, 127.
Coue, M., et al. 1987. FEBS Lett. 213, 316.
Schatten, G., et al. 1986. Exp. Cell Res. 166, 191.
Spector, I., et al. 1983. Science 219, 493.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Molecular biology of the cell, 32(20), ar5-ar5 (2021-08-05)
Mitochondrial division is an important cellular process in both normal and pathological conditions. The dynamin GTPase Drp1 is a central mitochondrial division protein, driving constriction of the outer mitochondrial membrane (OMM). In mammals, the OMM protein mitochondrial fission factor (Mff)
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PLoS biology, 20(10), e3001807-e3001807 (2022-10-11)
Developing tissues can self-organize into a variety of patterned structures through the stabilization of stochastic fluctuations in their molecular and cellular properties. While molecular factors and cell dynamics contributing to self-organization have been identified in vivo, events channeling self-organized systems
Microtubule retrograde flow retains neuronal polarization in a fluctuating state.
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Kem A Sochacki et al.
Developmental cell, 56(8), 1131-1146 (2021-04-07)
Clathrin-mediated endocytosis is the primary pathway for receptor and cargo internalization in eukaryotic cells. It is characterized by a polyhedral clathrin lattice that coats budding membranes. The mechanism and control of lattice assembly, curvature, and vesicle formation at the plasma
Patrick J Woida et al.
Science signaling, 13(614) (2020-01-16)
Multifunctional autoprocessing repeats-in-toxin (MARTX) toxins are pore-forming bacterial toxins that translocate multiple functionally independent effector domains into a target eukaryotic cell. Vibrio cholerae colonizes intestinal epithelial cells (IECs) and uses a MARTX toxin with three effector domains-an actin cross-linking domain

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