Jasplakinolide

Jasplakinolide is a macrocyclic peptide isolated from the marine sponge Jaspis johnstoni and is a potent inducer of actin polymerizationRead more

Catalog Number	Quantity
J7473	100 μg

Catalog number J7473

Price (JPY)

134,100

Quantity:

100 μg

Jasplakinolide is a macrocyclic peptide isolated from the marine sponge Jaspis johnstoni and is a potent inducer of actin polymerization in vitro by stimulating actin filament nucleation. Jasplakinolide competes with phalloidin for actin binding (Kd = 15 nM).

For Research Use Only. Not for use in diagnostic procedures.

Specifications

Molecular FormulaC36H45BrN4O6

Quantity100 μg

Recommended StorageStore in freezer (-5°C to -30°C)

Shipping ConditionRoom Temperature

Sub Cellular LocalizationActin, Cytoskeleton

Physical FormSolid

Product TypePeptide

Unit SizeEach

Citations & References (249)

Citations & References

Abstract

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

Specification of actin filament function and molecular composition by tropomyosin isoforms.

Authors:Bryce NS, Schevzov G, Ferguson V, Percival JM, Lin JJ, Matsumura F, Bamburg JR, Jeffrey PL, Hardeman EC, Gunning P, Weinberger RP

Journal:Mol Biol Cell

PubMed ID:12631719

The specific functions of greater than 40 vertebrate nonmuscle tropomyosins (Tms) are poorly understood. In this article we have tested the ability of two Tm isoforms, TmBr3 and the human homologue of Tm5 (hTM5(NM1)), to regulate actin filament function. We found that these Tms can differentially alter actin filament organization, ... 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

Actin filament turnover removes bundles from Drosophila bristle cells.

Authors:Guild GM, Connelly PS, Vranich KA, Shaw MK, Tilney LG

Journal:J Cell Sci

PubMed ID:11861770

Drosophila bristle cells form enormous extensions that are supported by equally impressive scaffolds of modular, polarized and crosslinked actin filament bundles. As the cell matures and support is taken over by the secreted cuticle, the actin scaffold is completely removed. This removal begins during cell elongation and proceeds via an ... More

Gelsolin mediates collagen phagocytosis through a rac-dependent step.

Authors:Arora PD, Glogauer M, Kapus A, Kwiatkowski DJ, McCulloch CA

Journal:Mol Biol Cell

PubMed ID:14617805

The role of gelsolin, a calcium-dependent actin-severing protein, in mediating collagen phagocytosis, is not defined. We examined alpha 2 beta 1 integrin-mediated phagocytosis in fibroblasts from wild-type (WT) and gelsolin knockout (Gsn(-)) mice. After initial contact with collagen beads, collagen binding and internalization were 60% lower in Gsn(-) than WT ... More

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