Product Pathways - Cytoskeletal Signaling
Pan-Actin Antibody #4968
| Applications | Reactivity | MW (kDa) | Source |
|---|---|---|---|
| W IHC-P | H M R Mk (Dr) (X) (Z) | 45 | Rabbit |
Applications Key:
W=Western Blotting
IHC-P=Immunohistochemistry (Paraffin)
Reactivity Key:
H=Human
M=Mouse
R=Rat
Mk=Monkey
Dr=Drosophila
X=Xenopus
Z=Zebra Fish
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.
Specificity / Sensitivity
Pan-Actin Antibody detects endogenous levels of total actin (all isoforms). The antibody also detects the 30 kDa actin fragment cleaved at glutamate 107.
Source / Purification
Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide (KLH-coupled) corresponding to residues surrounding Asp244 of human beta-actin. Antibodies are purified by protein A and peptide affinity chromatography.
Western Blotting
Western blot analysis of extracts from HeLa, L929, C6 and COS cells, using Pan-Actin Antibody.
IHC-P (paraffin)
Immunohistochemical analysis of paraffin-embedded human colon (smooth muscle), using Pan-Actin Antibody.
IHC-P (paraffin)
Immunohistochemical analysis of paraffin-embedded human heart, using Pan-Actin Antibody.
Background
Actin, a ubiquitous protein in eukaryotes, is the major component of the cytoskeleton. At least six isoforms are known in mammals. Nonmuscle beta- and gamma-actin, also known as cytoplasmic actin, are predominantly expressed in nonmuscle cells, controling cell structure and motility (1). alpha-cardiac and alpha-skeletal actin are expressed in striated cardiac and skeletal muscles, respectively; two smooth muscle actins, alpha- and gamma-actin, are found primarily in vascular smooth muscle and enteric smooth muscle, respectively. These actin isoforms regulate contractile potentials for 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/proteosome 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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