β-Actin Blocking Peptide #1025

This peptide is used to specifically block β-Actin (13E5) Rabbit mAb #4970 by dot blot.

The quality of the peptide was evaluated by reversed-phase HPLC and by mass spectrometry. The peptide blocks beta-Actin (13E5) Rabbit mAb #4970 by dot blot.

Use as a blocking reagent to evaluate the specificity of antibody reactivity in dot blot protocols.

Storage:

Supplied in 20 mM potassium phosphate (pH 7.0), 50 mM NaCl, 0.1 mM EDTA, 1 mg/ml BSA and 5% glycerol. 1% DMSO. Store at –20°C.

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.

• Data sheet (79KB)
• MSDS PDF