Cell Signaling Technology

Product Pathways - Cytoskeletal Signaling

Phospho-Cofilin (Ser3) Antibody #3311

Applications Reactivity MW (kDa) Source
W H M R Mk Hm B (Pg) 19 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey  Pg=Pig  Hm=Hamster  B=Bovine
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

Phospho-Cofilin (Ser3) Antibody detects endogenous levels of cofilin only when phosphorylated at serine 3. The antibody may cross-react with phosphorylated cofilin 2, the muscle isoform.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic phospho-peptide (KLH-coupled) corresponding to residues surrounding Ser3 of human cofilin. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from HeLa cells, untreated or H2O2-treated, using Phospho-Cofilin (Ser3) Antibody (A and B) or Cofilin Antibody #3312 (C and D). Membranes (B and D) were treated with alkaline phosphatase (CIP) to demonstrate the phospho-specificity the antibody.

Western Blotting

Western Blotting

Western blot analysis of extracts from asynchronous or mitotic C6, CHO and COS cells, using Phospho-Cofilin (Ser3) Antibody (upper) or Cofilin Antibody #3312 (lower).

Background

Cofilin and ADF (actin-depolymerization factor) are members of a family of essential conserved small actin-binding proteins that play pivotal roles in cytokinesis, endocytosis, embryonic development, stress response and tissue regeneration (1). In response to stimuli, cofilin promotes the regeneration of actin filaments by severing preexisting filaments (2). The severing activity of cofilin is inhibited by LIMK or TESK phosphorylation at Ser3 of cofilin (3-5). Phosphorylation at Ser3 also regulates cofilin translocation from the nucleus to the cytoplasm (6).

  1. Carlier, M. et al. (1999) J. Biol. Chem. 274, 33827-33830.
  2. Condeelis, J. (2001) Trends Cell Biol. 11, 288-293.
  3. Arber, S. et al. (1998) Nature 393, 805-809.
  4. Yang, N. et al. (1998) Nature 393, 809-812.
  5. Toshima, J. et al. (2001) J. Biol. Chem. 276, 31449-31458.
  6. Nebl, G. et al. (1996) J. Biol. Chem. 271, 26276-26280.

Application References

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