LATRUNCULIN B Chemical Properties

alpha 

D24 +112° (c = 0.48 in chloroform)

storage temp. 

-20°C

solubility 

DMSO: soluble

form 

solid

color 

light yellow

optical activity

+120.123 （CHCl3）

Stability:

Stable for 1 year from date of purchase as supplied. Solutions in DMSO or ethanol may be stored at -20° for up to 3 months.

Safety Information

WGK Germany 

3

MSDS

• Language:English Provider:SigmaAldrich

LATRUNCULIN B Usage And Synthesis

Description

Latrunculin B (76343-94-7) inhibits actin polymerization and disrupts microfilament organization.1 Significantly more potent than cytochalasins in the disruption of microfilament mediated processes2, causes shortening and thickening of stress fibers. Active in cell culture.3,4?Effective doses for latrunculin B vary depending upon cell type but are frequently in the low micromolar range. Note: Latrunculin B is slowly inactivated by fetal bovine serum.

Uses

In elucidation of molecular mechanisms of motile processes.

Uses

Latrunculin B is an actin polymerization inhibitor.

Uses

Latrunculin B from Latruncula magnifica has been used for actin depolymerisation in various experiments. It has also been used as a component in bone marrow-derived dendritic cell (BMDC) complete medium, to study the formation of tubules from phagosomes in dendritic cells.

Definition

ChEBI: A macrolide consisting of a 14-membered bicyclic lactone attached to the rare 2-thiazolidinone moiety. It is obtained from the Red Sea sponge Latrunculia magnifica.

General Description

Latrunculin B is a macrocyclic toxin, which is produced by Latruncula magnifica.

Biochem/physiol Actions

Primary TargetActin polymerization

storage

Store at -20°C

References

1) Coue?et al. (1987),?Inhibition of actin polymerization by latrunculin; FEBS Lett.,?213?316 2) Spector?et al. (1989),?Latrunculins-novel marine macrolides that disrupt microfilament organization and affect cell growth; Cell Motil. Cytoskeleton,?13?127 3) Wakatsuki?et al. (2001),?Effects of cytochalasin D and latrunculin B on mechanical properties of cells; J. Cell. Sci.,?114?1025 4) Cha?et al. (2004),?The lateral mobility of NHE3 on the apical membrane of renal epithelial OK cells is limited by the PDZ domain proteins NHERF1/2 but is dependent on an intact actin cytoskeleton as determined by FRAP; Prog. Clin. Biol. Res.,?230 4 5) Herrera (2021), Cell cultures, transfection and treatments. protocols.io???https://dx.doi.org/10.17504/protocols.io.77ehrje [Focus Citation]

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