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C8736

Sigma-Aldrich

Anti-Cofilin antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Sinonimo/i:

Anti-CFL, Anti-HEL-S-15, Anti-cofilin

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About This Item

Numero MDL:
Codice UNSPSC:
12352203
NACRES:
NA.46

Origine biologica

rabbit

Coniugato

unconjugated

Forma dell’anticorpo

IgG fraction of antiserum

Tipo di anticorpo

primary antibodies

Clone

polyclonal

Forma fisica

buffered aqueous solution

PM

antigen ~19 kDa

Reattività contro le specie

canine, rat, human, mouse

tecniche

indirect immunofluorescence: 1:1,000 using using mouse NIH/3T3 fibroblasts
microarray: suitable
western blot: 1:10,000 using using whole extracts of human A-431, rat PC-12, mouse NIH/3T3, and dog MDCK kidney cells

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

Categorie correlate

Descrizione generale

Cofilin is a member of the actin depolymerizing factor/cofilin family. Among all members, cofilin-1 is the predominant isoform. It is located on human chromosome 11q13.
Cofilin is a small phosphoinositide-sensitive actin-binding protein capable of depolymerizing actin-filaments in vitro. 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.

Specificità

Reacts with muscle and non-muscle cofilin.

Immunogeno

Synthetic peptide corresponding to human cofilin sequence, with N-terminal cysteine added, conjugated to KLH. The corresponding sequence is identical in pig and rat non-muscle cofilin and differs by three amino acids from that of human and chicken muscle cofilin.

Applicazioni

Anti-Cofilin antibody has been used:
  • for immunostaining of chick neurons. It is used as a primary antibody
  • for western blotting of protein isolated from mouse hippocampi cells, rat brain samples, human acute lymphoblastic T-cell line, human brain samples, head and neck squamous cell carcinoma cell line, HEK293T cells and renal epithelial cell lines
  • for immunofluorescence studies in tissue samples from human brain

Azioni biochim/fisiol

Cofilin binds stoichiometrically to monomeric G-actin and actin protomers. Cofilin intercalates between longitudinally associated actin monomers within the filament. Under specific conditions, It cleaves the filaments and accelerates actin subunits dissociation from their ‘pointed′ ends. It is essential for viability and vital for many cellular processes involving actin remodeling, such as motility at the leading edge of cells, polarized cell growth, endocytosis, phagocytosis, cellular activation, cytokinesis etc. Cofilin activity is regulated through reversible phosphorylation and dephosphorylation. In phosphorylated form, it is inactive and unable to bond with actin. Phosphorylation of cofilin is regulated by at least four protein kinases: LIM Kinase-1, LIM Kinase-2, Testicular Kinase-1, and Testicular Kinase-2. S-nitrosylation of cofilin is involved in vascular endothelial growth factor (VEGF)-stimulated endothelial cytoskeleton remodeling and migration. Over-expression of cofilin suppresses growth and invasion of non-small cell lung cancer. Dysregulation of cofilin is associated with neurodegeneration.

Stato fisico

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

Stoccaggio e stabilità

For continuous use, store at 2-8 °C for up to one month. For prolonged storage, freeze in working aliquots at -20 °C. Repeated freezing and thawing, or storage in frost-free freezers, is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilutions should be discarded if not used within 12 hours.

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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Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


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K Moriyama et al.
The EMBO journal, 18(23), 6752-6761 (1999-12-03)
The biochemical activities of cofilin are controversial. We demonstrated that porcine cofilin severs actin filaments and accelerates monomer release at the pointed ends. At pH 7.1, 0.8 microM cofilin cut filaments (2.2 microM actin) about every 290 subunits and increased
Hong-Hai Zhang et al.
Journal of cellular physiology, 230(2), 406-417 (2014-07-25)
Nitric oxide (NO) derived from endothelial NO synthase (eNOS) mediates vascular endothelial growth factor (VEGF)-stimulated endothelial cytoskeleton remodeling and migration; however, the underlying mechanisms are elusive. Covalent adduction of a NO moiety (NO(•)) to cysteines called S-nitrosylation (SNO) is a
M F Carlier et al.
The Journal of cell biology, 136(6), 1307-1322 (1997-03-24)
Actin-binding proteins of the actin depolymerizing factor (ADF)/cofilin family are thought to control actin-based motile processes. ADF1 from Arabidopsis thaliana appears to be a good model that is functionally similar to other members of the family. The function of ADF
Immune-complex level of cofilin-1 in sera is associated with cancer progression and poor prognosis in pancreatic cancer
Satoh M, et al.
Cancer Science, 108(4), 795-795 (2017)
Jodie P Simard et al.
Journal of cell science, 124(Pt 14), 2367-2374 (2011-06-23)
Hyperthermia adversely affects cell structure and function, but also induces adaptive responses that allow cells to tolerate these stressful conditions. For example, heat-induced expression of the molecular chaperone protein HSP70 can prevent stress-induced cell death by inhibiting signaling pathways that

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