β-Actin Antibody

4967:

Western Blotting

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.

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

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.

• Bish, R.A. and Myers, M.P. (2007) J Biol Chem 282, 23184-93. Applications: Western Blotting
• Nociari, M. et al. (2007) J Virol 81, 4145-57. Applications: Western Blotting
• Wei, F. et al. (2007) J Biol Chem 282, 21551-60. Applications: Western Blotting
• Guo, A. et al. (2008) Proc Natl Acad Sci U S A 105, 692-7. Applications: Western Blotting
• Widenmaier, S.B. et al. (2009) J Biol Chem 284, 30372-82. Applications: Western Blotting
• Zheng, Y.S. et al. (2011) Oncogene , . Applications: Western Blotting

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