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인용 및 참조 문헌 (249)
Invitrogen™
Jasplakinolide
Jasplakinolide is a macrocyclic peptide isolated from the marine sponge Jaspis johnstoni and is a potent inducer of actin polymerization자세히 알아보기
| 카탈로그 번호 | 수량 |
|---|---|
| J7473 | 100 μg |
카탈로그 번호 J7473
제품 가격(KRW)
849,000
온라인 행사
Ends: 31-Dec-2025
998,000할인액 149,000 (15%)
Each
수량:
100 μg
제품 가격(KRW)
849,000
온라인 행사
Ends: 31-Dec-2025
998,000할인액 149,000 (15%)
Each
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.
사양
분자식C36H45BrN4O6
수량100 μg
권장 스토리지Store in freezer (-5°C to -30°C)
배송 조건Room Temperature
세포하위구조 국지화Actin, Cytoskeleton
물리적 형태Solid
제품 유형Peptide
Unit SizeEach
인용 및 참조 문헌 (249)
인용 및 참조 문헌
Abstract
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
Specification of actin filament function and molecular composition by tropomyosin isoforms.
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,
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
Actin filament turnover removes bundles from Drosophila bristle cells.
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
Gelsolin mediates collagen phagocytosis through a rac-dependent step.
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