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Key Documents

C8992

Sigma-Aldrich

Monoclonal Ant-phospho-Cofilin (pSer3) antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Synonyme(s) :

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

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

IgG fraction of antiserum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~19 kDa

Espèces réactives

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

Technique(s)

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

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

phosphorylation (pSer3)

Informations sur le gène

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

Description générale

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.

Immunogène

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.

Application

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.

Actions biochimiques/physiologiques

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.

Forme physique

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

Clause de non-responsabilité

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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Produit(s) apparenté(s)

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

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


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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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