Latrunculin A, Latrunculia magnifica A stabilizer of monomeric G-actin and polymerization inhibitor

Latrunculin A, Latrunculia magnifica (CAS 76343-93-6)

Latrunculin A, Latrunculia magnifica | CAS 76343-93-6 is rated 5.0 out of 5 by 2.
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Synonym: LAT-A
Application: A stabilizer of monomeric G-actin and polymerization inhibitor
CAS Number: 76343-93-6
Purity: ≥96%
Molecular Weight: 421.55
Molecular Formula: C22H31NO5S
* Refer to Certificate of Analysis for lot specific data (including water content).
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Latruculin A is a macrolide toxin isolated from the red sea sponge Latrunculia magnifica. Latruculin A binds and stabilizes globular G-actin in a 1:1 complex, preventing the conversion of globular (monomeric) G-actin into filamentous (polymeric) F-actin, disturbing microfilament organization in the cell. The equlibrilium dissociaion constant for the reaction in cultured cell is 0.1-1 μM. Polymerization of G-actin and microfilament organization is essential for cellular mechanical processes including motility and cytoskeleton scaffolding, and disruption of this by Latruculin A affects normal functioning of the cell. Latrunculin A, Latrunculia magnifica is an inhibitor of Actin.


References

1. Coué, M., et al. 1987. FEBS Lett. 213: 316-318. PMID: 3556584
2. Lyubimova, A., et al. 1999. J. Cell. Biochem. 76: 1-12. PMID: 10580995
3. Yarmola, E.G., et al. 2000. J. Biol. Chem. 275: 28120-28127. PMID: 10859320
4. Hayot, C., et al. 2006. Toxicol. Appl. Pharmacol. 211: 30-40. PMID: 16005926
5. Loubéry, S., et al. 2008. Traffic. 9: 492-509. PMID: 18194411

Physical State :
Solid
Derived From :
Latrunculia magnifica
Solubility :
Soluble in DMSO (25 mg/ml), and ethanol (25 mg/ml).
Storage :
Store at -20° C
Melting Point :
270.68° C (Predicted)
Boiling Point :
624.34° C (Predicted)
Density :
1.16 g/cm3 (Predicted)
Refractive Index :
n20D 1.53 (Predicted)
IC50 :
A549: IC50 = 142.31 nM (human); H522-T1 : IC50 = 142.31 nM; HT-29: IC50 = 142.31 nM (human); U-937: IC50 = 166.03 nM (human); MDA-MB-435: IC50 = 94.88 nM (human)
pK Values :
pKa: 11.76 (Predicted)
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.
WGK Germany :
3
PubChem CID :
445420
Merck Index :
14: 5378
MDL Number :
MFCD00272613
SMILES :
C[C@H]/1CC[C@@H]2C[C@H](C[C@@](O2)([C@@H]3CSC(=O)N3)O)OC(=O)/C=C(\CC/C=C/C=C1)/C

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Certificate of Analysis

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Latrunculin A, Latrunculia magnifica  Product Citations

See how others have used Latrunculin A, Latrunculia magnifica. Click on the entry to view the PubMed entry .

Citations 1 to 10 of 15 total

PMID: # 26033825  Serbo, JV. et al. 2016. Adv Healthc Mater. 5: 146-58.

PMID: # 25749170  Mallol, A. et al. 2015. PLoS ONE. 10: e0120033.

PMID: # 25679223  Ito, T. et al. 2015. PLoS ONE. 10: e0118336.

PMID: # 24673933  Narayanareddy, BR. et al. 2014. Traffic. 15: 762-71.

PMID: # 24807265  Mutlu, N. et al. 2014. G3 (Bethesda). 4: 1247-58.

PMID: # 25068567  Mallol, A. et al. 2014. Cell Reprogram. 16: 392-406.

PMID: # 12873448  Liu, X. et al. 2003. Exp. Eye Res. 77: 181-188.

PMID: # 12118012  García-Ruiz, C. et al. 2002. J. Biol. Chem. 277: 36443-36448.

PMID: # 11994301  Bertoni, A. et al. 2002. J. Biol. Chem. 277: 25715-25721.

PMID: # 12055249  Porter, JC. et al. 2002. J. Immunol. 168: 6330-6335.

Citations 1 to 10 of 15 total

What is the solubility of this product?

Asked by: hawkeye11
Thank you for your question. Latrunculin A, Latrunculia magnifica (CAS 76343-93-6) is soluble in DMSO (25 mg/ml), and ethanol (25 mg/ml).
Answered by: Technical Support
Date published: 2017-08-19
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Rated 5 out of 5 by from The chain reaction We fully bind to the adrenal chemical enzyme and stabilize G-globular actin, catalyze the conversion of G-globular actin into filamentous F-actin, disrupting the cells in the cell tissue, detailing the catalytic chemical chain reaction
Date published: 2017-02-12
Rated 5 out of 5 by from Liu Liu, et. al. (PubMed ID 12873448) found that recovery of human trabecular meshwork (HTM) cells was quickened by treating them with latrunculin A post dexamethasone treatment/removal. -SCBT Publication Review
Date published: 2015-03-20
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