Latrunculin A - 1mM
Latrunculin A
Cell-permeant marine macrolide for sequestration of monomeric G-actin and inhibition of actin polymerization.
Applications
| Applications | Cell-permeant natural compound for prevention of actin polymerization. Latrunculin A is frequently used in biochemical and cell-based assays to disrupt actin filament formation by sequestering monomeric G-actin. |
| Recommended use | Recommended for experiments requiring inhibition of F-actin assembly, depletion of polymerization-competent G-actin, modulation of actin-dependent cellular processes or mechanistic comparison with actin-stabilizing compounds such as Jasplakinolide. |
| Typical workflows | Used in in vitro actin polymerization assays and cell-based cytoskeleton studies to prevent actin polymerization, disrupt microfilament dynamics and study the functional contribution of actin filaments. |
Description
| Product name | Latrunculin A |
| Source note | Marine sponge-derived macrolide. |
| Product description | Latrunculin A is a bioactive macrolide derived from marine sponges that efficiently sequesters monomeric G-actin and prevents F-actin assembly. It binds actin in a 1:1 molar stoichiometry and is widely used to inhibit actin polymerization in biochemical assays and cell-based cytoskeleton studies. By forming a complex with monomeric actin, Latrunculin A reduces the pool of polymerization-competent G-actin and thereby blocks filament assembly. This makes Latrunculin A a useful pharmacological tool for studying actin-dependent cellular processes, actin filament turnover and the functional consequences of disrupting actin polymerization. |
| Mechanism | Latrunculin A prevents actin polymerization by forming a 1:1 complex with monomeric G-actin. In contrast to filament-stabilizing compounds, it primarily acts by sequestering actin monomers rather than stabilizing assembled F-actin. |
| Functional notes | Latrunculin A is described as a cell-permeant macrolide containing a 2-thiazolidinone ring. It disrupts actin polymerization without directly targeting microtubules and has been reported to inhibit binding of thymosin β to actin. |
| Overview | Cell-permeant actin polymerization inhibitor; sequesters monomeric G-actin; prevents F-actin assembly; suitable for actin cytoskeleton disruption in biochemical and cell-based assays. |
Properties
| Form | Lyophilized, ready-to-use after reconstitution in DMSO. |
| Quantity | 1 mM in 100 µl |
| Stock solution | Add 100 µl DMSO to obtain a 1 mM Latrunculin A stock solution. |
| Formal name | (4R)-[(1R,4Z,8E,10Z,12S,15R,17R)-17-hydroxy-5,12-dimethyl-3-oxo-2,16-dioxabicyclo[13.3.1]nonadeca-4,8,10-trien-17-yl]-2-thiazolidinone. |
| Molecular weight | 421.6 g/mol. |
| Purity | 98% by HPLC. |
| Storage instructions | Store at −20 °C upon arrival. The product will be stable in performance for at least 1 year from the date of purchase. |
| Shipping conditions | At ambient temperature. Upon delivery store at −20 °C. |
| Remarks | For research use only. Not for use in human or veterinary diagnostic or therapeutic applications. |
| CAS no. | |
Compounds and reagents from Hypermol® are prepared for reliable research use, as described in our product documentation.
References
Yarmola EG, Somasundaram T, Boring TA, Spector I, Bubb MR. Actin-latrunculin A structure and function. Differential modulation of actin-binding protein function by latrunculin A. J Biol Chem. 2000 Sep 8;275(36):28120-28127.
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Compounds and reagents from Hypermol® are prepared for reliable research use, as described in our product documentation.
Compounds and reagents from Hypermol® are prepared for reliable research use, as described in our product documentation.
