L5163
Latrunculin A
From sea sponge, ≥85% (HPLC), Inhibitor of actin assembly and polymerization, waxy solid
동의어(들):
LAT-A, [1R-[1R*, 4Z, 8E, 10Z, 12S*, 15R*, 17R*(R*)]]-4-(17-Hydroxy-5,12-dimethyl-3-oxo-2,16-dioxabicyclo[13.3.1]nonadeca-4,8,10-trien-17-yl)-2-thiazolidinone
조직 및 계약 가격을 보려면 로그인를 클릭합니다.
크기 선택
보기 변경
제품정보 (DICE 배송 시 비용 별도)
실험식(Hill 표기법):
C22H31NO5S
CAS 번호:
Molecular Weight:
421.55
UNSPSC Code:
12352200
PubChem Substance ID:
NACRES:
NA.77
제품 이름
Latrunculin A, from sea sponge, ≥85% (HPLC), waxy solid
biological source
sea sponge
Quality Level
assay
≥85% (HPLC)
form
waxy solid
mol wt
421.6
solubility
DMSO: soluble, ethanol: soluble
storage temp.
−20°C
SMILES string
C[C@H]1CC[C@@H]2C[C@H](C[C@@](O)(O2)[C@@H]3CSC(=O)N3)OC(=O)C=C(C)CC\C=C\C=C1
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
Latrunculin A, a toxin extracted from the red sea sponge Latrunculia magnifica. It participates in vitro in the morphological alteration of the polymerization of pure actin. It forms a complex by binding with the nucleotide cleft of actin for actin filaments elongation.
Application
Latrunculin A has been used as medium supplementation for A549 cells to determine the internalization mechanism of CAV9 in A549 human lung carcinoma cells.
Biochem/physiol Actions
Latrunculin A inhibits actin polymerization by a different mechanism than cytochalasins. Latrunculin A disrupts microfilament-mediated processes.
저장 등급
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
M Coué et al.
FEBS letters, 213(2), 316-318 (1987-03-23)
Latrunculin A, a toxin purified from the red sea sponge Latrunculia magnifica, was found previously to induce striking reversible changes in the morphology of mammalian cells in culture and to disrupt the organization of their microfilaments. We now provide evidence
Maureen Möckel et al.
Journal of virology, 93(16) (2019-05-31)
Dynamin GTPases, best known for their role in membrane fission of endocytic vesicles, provide a target for viruses to be exploited during endocytic uptake. Recently, we found that entry of herpes simplex virus 1 (HSV-1) into skin cells depends on
Keiichiro Kushiro et al.
Scientific reports, 7(1), 4244-4244 (2017-06-28)
During metastasis, cancer cells are exposed to various three-dimensional microstructures within the body, but the relationship between cancer migration and three-dimensional geometry remain largely unclear. Here, such geometric effects on cancerous cells were investigated by characterizing the motility of various