C8736

Sigma-Aldrich

Anti-Cofilin antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

MDL number:
NACRES:
NA.46

biological source

rabbit

Quality Level

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~19 kDa

species reactivity

canine, rat, human, mouse

application(s)

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

conjugate

unconjugated

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

Gene Information

General description

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.
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.

Specificity

Reacts with muscle and non-muscle cofilin.

Immunogen

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.

Application

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

Biochem/physiol Actions

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.

Physical form

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

Storage and Stability

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.

Disclaimer

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.

storage_class_code

12 - Non Combustible Liquids

WGK Germany

WGK 3

Flash Point F

Not applicable

Flash Point C

Not applicable

Certificado de Análisis

Certificado de origen

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)
Mapping of human non-muscle type cofilin (CFL1) to chromosome 11q13 and muscle-type cofilin (CFL2) to chromosome 14
Gillett GT, et al.
Annals of Human Genetics, 60(3) (1996)

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