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Merck

C8736

Anti-Cofilin antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Synonyme(s) :

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

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A propos de cet article

UNSPSC Code:
12352203
NACRES:
NA.46
MDL number:
Conjugate:
unconjugated
Clone:
polyclonal
Application:
ARR, IF, WB
Species reactivity:
canine, rat, human, mouse
Citations:
26
Technique(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
Uniprot accession no.:
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biological source

rabbit

conjugate

unconjugated

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

technique(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

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Quality Level

Gene Information

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.
Reacts with muscle and non-muscle cofilin.

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.

General description

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.

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.

Physical form

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

Preparation Note

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.

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Classe de stockage

10 - Combustible liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Consulter la Bibliothèque de documents

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
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
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
Patrick J Hensley et al.
Urologic oncology, 37(9), 572-572 (2019-07-22)
Cisplatin-based neoadjuvant chemotherapy (NAC) for muscle-invasive urothelial carcinoma of the bladder confers only a modest survival advantage. Patients with pathologic progression on NAC have poor outcomes related to a delay in definitive surgical management. To characterize the value of epithelial-mesenchymal

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