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    肌動(dòng)蛋白破壞用于研究體外(例如，遷移、胞吞作用)和體內(nèi)(例如，腫瘤細(xì)胞侵襲)的細(xì)胞功能。Latrunculin A是一種具有生物活性的2-噻唑烷酮大環(huán)內(nèi)酯，來(lái)源于海綿，可隔離G-肌動(dòng)蛋白并阻止F-肌動(dòng)蛋白裝配。它以1:1的化學(xué)計(jì)量結(jié)合單體肌動(dòng)蛋白，可用于在體外(Kd = 0.2微米)和細(xì)胞內(nèi)(0.5微米，30分鐘)阻斷肌動(dòng)蛋白聚合。[1]、[2]、[3] Latrunculin A (1-10微米)在十分鐘內(nèi)引起腫瘤細(xì)胞細(xì)胞骨架的解聚。[4]用latrunculin A (10微米)過(guò)夜處理細(xì)胞強(qiáng)烈抑制肌動(dòng)蛋白合成。[5]延長(zhǎng)的細(xì)胞處理阻斷了地塞米松誘導(dǎo)的肌動(dòng)蛋白細(xì)胞骨架的變化，而對(duì)細(xì)胞活力沒(méi)有影響。[6]

產(chǎn)品性質(zhì)：

Cas No.：76343-93-6

別名：紅海海綿素A,LAT-A

化學(xué)名： (R)-4-((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)thiazolidin-2-one

Canonical SMILES O[C@@](C1)([C@H]2NC(SC2)=O)O[C@H](CC[C@@H](/C=C\C=C\CC/C(C)=C\3)C)C[C@H]1OC3=O

分子式：C22H31NO5S

分子量：421.6

溶解度：25mg/mL in ethanol, or in DMSO

儲(chǔ)存條件：Store at -20°C

注意事項(xiàng)：

為了您的安全和健康，請(qǐng)穿實(shí)驗(yàn)服并戴一次性手套操作。

References

[1]. Coué, M., Brenner, S.L., Spector, I., et al. Inhibition of actin polymerization by latrunculin A. FEBS Letters 213(2), 316-318 (1987).

[2]. Yarmola, E.G., Somasundaram, T., Boring, T.A., et al. Actin-latrunculin A structure and function. The Journal of Biological Chemisty 275(36), 28120-28127 (2000).

[3]. Loubéry, S., Wilhelm, C., Hurbain, I., et al. Different microtubule motors move early and late endocytic compartments. Traffic 9, 492-509 (2008).

[4]. Hayot, C., Debeir, O., Van Ham, P., et al. Characterization of the activities of actin-affecting drugs on tumor cell migration. Toxicology and Applied Pharmacology 211, 30-40 (2006).

[5]. Lyubimova, A., Bershadsky, A.D., and Ben-Ze'ev, A. Autoregulation of actin synthesis requires the 3'-UTR of actin mRNA and protects cells from actin overproduction. Journal of Cellular Biochemistry 76, 1-12 (1999).

[6]. Liu, X., Wu, Z., Sheibani, N., et al. Low dose latrunculin-A inhibits dexamethasone-induced changes in the actin cytoskeleton and alters extracellular matrix protein expression in cultured human trabecular meshwork cells. Experimental Eye Research 77, 181-188 (2003).