Product Pathways - Cytoskeletal Signaling
β-Actin (8H10D10) Mouse mAb #3700
|W IHC-P IF-IC F||H M R Hm Mk Dg||Endogenous||45||Mouse IgG2b|
Reactivity Key: H=Human M=Mouse R=Rat Hm=Hamster Mk=Monkey Dg=Dog
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
* Product-specific protocol.
Specificity / Sensitivity
β-Actin (8H10D10) Mouse mAb detects endogenous levels of total β-actin protein.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to amino-terminal residues of human β-actin.
Western blot analysis of extracts from various cell types using β-Actin (8H10D10) Mouse mAb.
Immunohistochemical analysis of paraffin-embedded human breast carcinoma using β-Actin (8H10D10) Mouse mAb.
Immunohistochemical analysis of paraffin-embedded human heart using β-Actin (8H10D10) Mouse mAb. Note the lack of staining of cardiac muscle.
Flow cytometric analysis of HeLa cells using β-Actin (8H10D10) Mouse mAb (blue) compared to a nonspecific negative control antibody (red).
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.
- Zheng, Y.S. et al. (2011) Oncogene , . Applications: Western Blotting
- Tarassishin, L. et al. (2011) Glia 59, 1911-22. Applications: Western Blotting
- Tarassishin, L. et al. (2011) J Neuroinflammation 8, 187. Applications: Western Blotting
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For Research Use Only. Not For Use In Diagnostic Procedures.