Cell Signaling Technology

Product Pathways - Cytoskeletal Signaling

β-Actin Antibody #4967

Applications Reactivity Sensitivity MW (kDa) Source
W H M R Hm Mk Mi Dm Z B Dg (C) (X) (Pg) (Hr) Endogenous 45 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  R=Rat  Hm=Hamster  Mk=Monkey  C=Chicken  Mi=Mink  Dm=D. melanogaster  X=Xenopus  Z=Zebrafish  B=Bovine  Dg=Dog  Pg=Pig  Hr=Horse
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

β-Actin Antibody detects endogenous levels of β-actin. This antibody may cross-react with the γ-actin (cytoplasmic) isoform. It does not cross-react with α-skeletal, α-cardiac, α-vascular smooth, or γ-enteric smooth muscle isoforms.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to amino-terminal residues of human β-actin. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from HeLa, C2C12, C6, COS, MvLu cells and guinea pig neutrophils (GPN), using β-Actin Antibody.

Background

Actin, a ubiquitous eukaryotic protein, is the major component of the cytoskeleton. At least six isoforms are known in mammals. Nonmuscle β- and γ-actin, also known as cytoplasmic actin, are predominantly expressed in nonmuscle cells, controlling cell structure and motility (1). α-cardiac and α-skeletal actin are expressed in striated cardiac and skeletal muscles, respectively; two smooth muscle actins, α- and γ-actin, are found primarily in vascular smooth muscle and enteric smooth muscle, respectively. These actin isoforms regulate the contractile potential of muscle cells (1). Actin exists mainly as a fibrous polymer, F-actin. In response to cytoskeletal reorganizing signals during processes such as cytokinesis, endocytosis, or stress, cofilin promotes fragmentation and depolymerization of F-actin, resulting in an increase in the monomeric globular form, G-actin (2). The ARP2/3 complex stabilizes F-actin fragments and promotes formation of new actin filaments (2). Research studies have shown that actin is hyperphosphorylated in primary breast tumors (3). Cleavage of actin under apoptotic conditions has been observed in vitro and in cardiac and skeletal muscle, as shown in research studies (4-6). Actin cleavage by caspase-3 may accelerate ubiquitin/proteasome-dependent muscle proteolysis (6).

  1. Herman, I.M. (1993) Curr. Opin. Cell Biol. 5, 48-55.
  2. Condeelis, J. (2001) Trends Cell Biol. 11, 288-293.
  3. Lim, Y.P. et al. (2004) Clin. Cancer Res. 10, 3980-3987.
  4. Kayalar, C. et al. (1996) Proc. Natl. Acad. Sci. USA. 93, 2234-2238.
  5. Communal, C. et al. (2002) Proc. Natl. Acad. Sci. USA. 99, 6252-6256.
  6. Du, J. et al. (2004) J. Clin. Invest. 113, 115-123.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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