Latrunculin A
Latrunculin A
Citations & References (336)
Invitrogen™

Latrunculin A

Latrunculin A disrupts microfilament organization in cultured cells by binding to monomeric G-actin in a 1:1 complex at submicromolar concentrations.Read more
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Catalog NumberQuantity
L12370100 μg
Catalog number L12370
Price (INR)
38,900.00
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59,838.00
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Quantity:
100 μg
Price (INR)
38,900.00
線上優惠
Ends: 31-Dec-2025
59,838.00
Save 20,938.00 (35%)
Each
Add to cart
Latrunculin A disrupts microfilament organization in cultured cells by binding to monomeric G-actin in a 1:1 complex at submicromolar concentrations. Its physiological effects include inhibition of fertilization, early embryological development and phagocytic internalization of immune complexes.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Molecular FormulaC22H31NO5S
Quantity100 μg
Recommended StorageStore in freezer (-5°C to -30°C)
Shipping ConditionRoom Temperature
Sub Cellular LocalizationActin, Cytoskeleton
Physical FormSolid
Product TypeInhibitor
Unit SizeEach

Citations & References (336)

Citations & References
Abstract
A kinase-regulated PDZ-domain interaction controls endocytic sorting of the beta2-adrenergic receptor.
Authors:Cao TT,Deacon HW,Reczek D,Bretscher A,von Zastrow M
Journal:Nature
PubMed ID:10499588
Caveolin-associated filamentous actin (Cav-actin) defines a novel F-actin structure in adipocytes.
Authors:Kanzaki M, Pessin JE
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 ... More
Actin filament cross-linking by MARCKS: characterization of two actin-binding sites within the phosphorylation site domain.
Authors:Yarmola EG, Edison AS, Lenox RH, Bubb MR
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 ... More
Assembly of adherens junctions is required for sphingosine 1-phosphate-induced matriptase accumulation and activation at mammary epithelial cell-cell contacts.
Authors:Hung RJ, Hsu IaW, Dreiling JL, Lee MJ, Williams CA, Oberst MD, Dickson RB, Lin CY
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 ... More
Differential control of clustering of the sodium channels Na(v)1.2 and Na(v)1.6 at developing CNS nodes of Ranvier.
Authors:Kaplan MR, Cho MH, Ullian EM, Isom LL, Levinson SR, Barres BA
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 ... More
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