Product Pathways - Cytoskeletal Signaling
β-Actin (13E5) Rabbit mAb (Biotinylated) #5057
|5057S||100 µl (10 western blots)||---||In Stock||---|
|5057||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse, Rat, Monkey, Bovine, Pig||Endogenous||45||Rabbit IgG|
Species cross-reactivity is determined by western blot using the unconjugated antibody.
Applications Key: W=Western Blotting, F=Flow Cytometry
Species predicted to react based on 100% sequence homology: Chicken, Horse.
Specificity / Sensitivity
β-Actin (13E5) Rabbit mAb detects endogenous levels of total β-actin protein. 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
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino-terminus of human β-actin.
Western blot analysis of extracts from various cell lines using β-Actin (13E5) Rabbit mAb (Biotinylated).
This Cell Signaling Technology (CST) antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated antibody (β-Actin (13E5) Rabbit mAb #4970).
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).
- 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.
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For Research Use Only. Not For Use In Diagnostic Procedures.
Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.
This antibody is developed, validated, and produced by CST using in part technology under license (granting certain rights including those under U.S. Patents No. 5,675,063 and 7,429,487) from Epitomics, Inc.