β-Actin Antibody #4967
- WB
Supporting Data
| REACTIVITY | H M R Hm Mk Mi Dm Z B |
| SENSITIVITY | Endogenous |
| MW (kDa) | 45 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Hm-Hamster
- Mk-Monkey
- Mi-Mink
- Dm-D. melanogaster
- Z-Zebrafish
- B-Bovine
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Simple Western™ | 1:10 - 1:50 |
Storage
Protocol
Specificity / Sensitivity
β-Actin Antibody detects endogenous levels of β-actin. Due to the high sequence identity between the actin isoforms, β-Actin Antibody may cross-react with other actin isoforms.
Species Reactivity:
Human, Mouse, Rat, Hamster, Monkey, Mink, D. melanogaster, Zebrafish, Bovine
The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.
Species predicted to react based on 100% sequence homology:
Chicken, Xenopus, Dog, Pig, Horse
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.
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 ubiquitously expressed, controlling cell structure and motility (1). While all actin isoforms are highly homologous, cytoplasmic β- and γ-actin protein sequences differ by only four biochemically similar amino acids (2). For this reason, antibodies raised to β-actin may cross-react with γ-actin, and vice versa. 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 (3). The ARP2/3 complex stabilizes F-actin fragments and promotes formation of new actin filaments (3). Research studies have shown that actin is hyperphosphorylated in primary breast tumors (4). Cleavage of actin under apoptotic conditions has been observed in vitro and in cardiac and skeletal muscle, as shown in research studies (5-7). Actin cleavage by caspase-3 may accelerate ubiquitin/proteasome-dependent muscle proteolysis (7).
- Herman, I.M. (1993) Curr. Opin. Cell Biol. 5, 48-55.
- Perrin, B.J. and Ervasti, J.M. (2010) Cytoskeleton (Hoboken) 67, 630-4.
- Condeelis, J. (2001) Trends Cell Biol 11, 288-93.
- Lim, Y.P. et al. (2004) Clin Cancer Res 10, 3980-7.
- Kayalar, C. et al. (1996) Proc Natl Acad Sci U S A 93, 2234-8.
- Communal, C. et al. (2002) Proc Natl Acad Sci U S A 99, 6252-6.
- Du, J. et al. (2004) J Clin Invest 113, 115-23.
Limited Uses
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