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C8992

Sigma-Aldrich

Monoclonal Ant-phospho-Cofilin (pSer3)

IgG fraction of antiserum, buffered aqueous solution

Sinonimo/i:

Anti-18 kDa phosphoprotein, Anti-CFL1, Anti-Cofilin 1 (non-muscle), Anti-p18

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About This Item

Numero MDL:
Codice UNSPSC:
12352203
NACRES:
NA.41

Origine biologica

rabbit

Livello qualitativo

Coniugato

unconjugated

Forma dell’anticorpo

IgG fraction of antiserum

Tipo di anticorpo

primary antibodies

Clone

polyclonal

Stato

buffered aqueous solution

PM

antigen ~19 kDa

Reattività contro le specie

mouse, human, pig (predicted), rat (predicted)

tecniche

western blot: 1:2,000-1:4,000 using whole extracts of HeLa human epithelioid carcinoma and mouse NIH3T3 cells

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

phosphorylation (pSer3)

Informazioni sul gene

human ... CFL1(1072)
mouse ... Cfl1(12631)
rat ... Cfl1(29271)

Descrizione generale

Cofilin is a small phosphoinositide-sensitive actin-binding protein capable of depolymerizing actin-filaments in vitro. It has gelsolin-like actin filament-severing protein similar to destrin/ADF (Actin Depolymerizing Factor). Cofilin has has a short β-strand at the C terminus. In mammals it has two isoforms: non-muscle (NM-CF, CF-L1) and muscle (M-CF, CF-L2). The protein is ubiquitiously present in tissues of eukaryotes and is especially abundant in neuronal tissues. It can shuttle between the cytoplasm and the nucleus in response to various stresses or signals, and may translocate from the cytoplasm to the plasma membrane in various cells.

Immunogeno

synthetic phosphopeptide corresponding to amino acids 2-9 (pSer3) of human cofilin with a C-terminal added cysteine, conjugated to KLH. This sequence is identical in mouse, rat, and pig.

Applicazioni

Anti-phospho-Cofilin antibody was used:
  • as primary antibody for immunoblottingto to study the role of the Rac1 GTPase.
  • for western blot analysis in a comparative study of signals induced by integrin ligation during cell attachment, mechanical force from intracellular contraction, or cell stretching by external force.
  • as primary antibody for western blotting in a study to detect the level of cofilin.

Azioni biochim/fisiol

Cofilin binds stoichiometrically to monomeric G-actin and actin protomers in filaments in an apparently pH-dependent, Ca2+ independent manner. Cofilin intercalates between longitudinally associated actin monomers within the filament and distorts its helical twist.It cleaves the filaments and accelerates actin subunits dissociation from their ‘pointed′ ends under specific conditions. Cofilin is essential for viability and is important for many cellular processes involving actin remodeling such as motility at the leading edge of cells, polarized cell growth, endocytosis, phagocytosis, cellular activation, cytokinesis, and pathogen intracellular motility. It′s activity is regulated through reversible phosphorylation and dephosphorylation. In phosphorylated form, it behaves inactive and unable to bond with actin. Phosphorylation of cofilin is regulated in vertebrates by at least four protein kinases: LIM Kinase 1, LIM Kinase 2, Testicular Kinase 1, and Testicular Kinase 2. The dephosphorylation of cofilin enables its actin severing and depolymerizing activity and drives directional cell motility, thus providing a simple phosphoregulatory mechanism for actin reorganization.

Stato fisico

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Esclusione di responsabilità

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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N° Catalogo
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Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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Hongxia Zhao et al.
Biophysical journal, 98(10), 2327-2336 (2010-05-21)
Actin-depolymerizing-factor (ADF)/cofilins have emerged as key regulators of cytoskeletal dynamics in cell motility, morphogenesis, endocytosis, and cytokinesis. The activities of ADF/cofilins are regulated by membrane phospholipid PI(4,5)P(2) in vitro and in cells, but the mechanism of the ADF/cofilin-PI(4,5)P(2) interaction has
Timothy Y Huang et al.
Current opinion in cell biology, 18(1), 26-31 (2005-12-13)
Cofilin is a ubiquitous actin-binding factor required for the reorganization of actin filaments in eukaryotes. The dephosphorylation of cofilin enables its actin severing and depolymerizing activity and drives directional cell motility, thus providing a simple phosphoregulatory mechanism for actin reorganization.
K Kuželová et al.
Journal of cellular biochemistry, 111(6), 1413-1425 (2010-09-11)
The fusion protein Bcr-Abl, which is the molecular cause of chronic myelogenous leukemia (CML) interacts in multiple points with signaling pathways regulating the cellular adhesivity and cytoskeleton architecture and dynamics. We explored the effects of imatinib mesylate, an inhibitor of
Christopher A Foote et al.
American journal of physiology. Heart and circulatory physiology, 310(2), H188-H198 (2015-11-15)
Inward remodeling of the resistance vasculature is strongly associated with life-threatening cardiovascular events. Previous studies have demonstrated that both actin polymerization and the activation of transglutaminases mediate early stages of the transition from a structurally normal vessel to an inwardly
S Arber et al.
Nature, 393(6687), 805-809 (1998-07-09)
Cell division, cell motility and the formation and maintenance of specialized structures in differentiated cells depend directly on the regulated dynamics of the actin cytoskeleton. To understand the mechanisms of these basic cellular processes, the signalling pathways that link external

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