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Latrunculina A
La latrunculina A interrumpe la organización de los microfilamentos en las células cultivadas al unirse a la G-actina monomérica enMás información
| Número de catálogo | Cantidad |
|---|---|
| L12370 | 100 μg |
Número de catálogo L12370
Precio (CLP)
698.726
Each
Cantidad:
100 μg
Precio (CLP)
698.726
Each
La latrunculina A interrumpe la organización de los microfilamentos en las células cultivadas al unirse a la G-actina monomérica en un complejo 1:1 en concentraciones submicromolares. Sus efectos fisiológicos incluyen la inhibición de la fertilización, el desarrollo embrionario temprano y la internalización fagocítica de los complejos inmunológicos.
Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.
Especificaciones
Fórmula molecularC22H31NO5S
Cantidad100 μg
Almacenamiento recomendadoAlmacenar en congelador (de -5 °C a -30 °C)
Condiciones de envíoTemperatura ambiente
Localización subcelularActina, citoesqueleto
Forma físicaSólido
Tipo de productoLatrunculina A
Unit SizeEach
Citations & References (336)
Citations & References
Abstract
A kinase-regulated PDZ-domain interaction controls endocytic sorting of the beta2-adrenergic receptor.
Journal:Nature
PubMed ID:10499588
Caveolin-associated filamentous actin (Cav-actin) defines a novel F-actin structure in adipocytes.
Journal:J Biol Chem
PubMed ID:12039946
Dynamic actin remodeling has been implicated in the translocation of the insulin-responsive glucose transporter 4 (GLUT4) to the plasma membrane in adipocytes. Here we show that fully differentiated 3T3L1 adipocytes have unique cortical filamentous actin structure, designated Cav-actin (caveolae-associated F-actin). During 3T3L1 adipocyte differentiation, rhodamine-phalloidin staining demonstrated the formation of
Actin filament cross-linking by MARCKS: characterization of two actin-binding sites within the phosphorylation site domain.
Journal:J Biol Chem
PubMed ID:11294839
We recently identified conformational changes that occur upon phosphorylation of myristoylated alanine-rich protein kinase C substrate (MARCKS) that preclude efficient cross-linking of actin filaments (Bubb, M. R., Lenox, R. H., and Edison, A. S. (1999) J. Biol. Chem. 274, 36472-36478). These results implied that the phosphorylation site domain of MARCKS
Assembly of adherens junctions is required for sphingosine 1-phosphate-induced matriptase accumulation and activation at mammary epithelial cell-cell contacts.
Journal:Am J Physiol Cell Physiol
PubMed ID:15075215
Sphingosine 1-phosphate (S1P), a bioactive phospholipid, simultaneously induces actin cytoskeletal rearrangements and activation of matriptase, a membrane-associated serine protease in human mammary epithelial cells. In this study, we used a monoclonal antibody selective for activated, two-chain matriptase to examine the functional relationship between these two S1P-induced events. Ten minutes after
Differential control of clustering of the sodium channels Na(v)1.2 and Na(v)1.6 at developing CNS nodes of Ranvier.
Journal:Neuron
PubMed ID:11343648
'Na(v)1.6 is the main sodium channel isoform at adult nodes of Ranvier. Here, we show that Na(v)1.2 and its beta2 subunit, but not Na(v)1.6 or beta1, are clustered in developing central nervous system nodes and that clustering of Na(v)1.2 and Na(v)1.6 is differentially controlled. Oligodendrocyte-conditioned medium is sufficient to induce