PathScan® Total β-Actin Sandwich ELISA Antibody Pair #7881
Important Ordering Details
Custom Ordering Details: Product is assembled to order. Please allow up to three business days for your order to be processed.Supporting Data
| REACTIVITY | H M R Hm Mk |
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Hm-Hamster
- Mk-Monkey
Product Information
Storage
Protocol
Product Description
*Antibodies in the kit are custom formulations specific to the kit.
Specificity / Sensitivity
For Antibody Pair specificity and sensitivity, please refer to the corresponding PathScan® Sandwich ELISA Kit. Note: This antibody pair detects proteins from the indicated species, as determined through in-house testing, but may also detect homologous proteins from other species.
Species Reactivity:
Human, Mouse, Rat, Hamster, Monkey
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.
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