Product Pathways - Cytoskeletal Signaling
β-Actin Blocking Peptide #1025
Description
This peptide is used to specifically block β-Actin (13E5) Rabbit mAb #4970 by immunohistochemistry.
Quality Control
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 immunohistochemistry.
IHC-P (paraffin)
Immunohistochemical analysis of paraffin-embedded human lung carcinoma, using β-Actin (13E5) Rabbit mAb #4970 in the presence of control peptide (left) or β-Actin Blocking Peptide (right).
Applications
Use as a blocking reagent to evaluate the specificity of antibody reactivity in immunohistochemistry protocols.
Directions for Use
For immunohistochemistry, add twice the volume of peptide as volume of antibody used in 100 µl total volume. Incubate for a minimum of 30 minutes prior to adding the entire volume to the slide. Recommended antibody dilutions can be found on the product data sheet.
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). It has been reported 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 (4-6). Actin cleavage by caspase-3 may accelerate ubiquitin/proteasome-dependent muscle proteolysis (6).
- Herman, I.M. (1993) Curr. Opin. Cell Biol. 5, 48-55.
- Condeelis, J. (2001) Trends Cell Biol. 11, 288-293.
- Lim, Y.P. et al. (2004) Clin. Cancer Res. 10, 3980-3987.
- Kayalar, C. et al. (1996) Proc. Natl. Acad. Sci. USA. 93, 2234-2238.
- Communal, C. et al. (2002) Proc. Natl. Acad. Sci. USA. 99, 6252-6256.
- Du, J. et al. (2004) J. Clin. Invest. 113, 115-123.
Application References
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Companion Products
This product is intended for research purposes only. The product is not intended to be used for therapeutic or diagnostic purposes in humans or animals.
