Cytoskeleton provides a rabbit polyclonal actin antibody which recognizes the C-terminal portion of mammalian actins. As such it detects methanol fixed (denatured conformation) and paraformaldehyde fixed (native conformation) actin in filament (F-actin) or subunit (G-actin) form. See below for more information about this antibody.
In addition, Cytoskeleton has developed a unique line of fluorescent phalloidins with improved brightness and stability compared to other conjugates such as Alexa fluor and Cy dyes, for more information see the Acti-stain information page.
For product Datasheets and MSDSs please click on the PDF links below. For additional information, click on the FAQs tab above or contact our Technical Support department at tservice@cytoskeleton.com.
Cytoskeleton's antibodies products have been cited hundreds of times over the past 18 years. A select few are described here, for more citations on individual products please use the "Citations" tab on each individual product page.
Actin Polyclonal Antibody (Cat. # AAN01)
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Klees, R. F., Salasznyk, R. M., Kingsley, K., Williams, W. A., Boskey, A. and Plopper, G. E. (2005). Laminin-5 induces osteogenic gene expression in human mesenchymal stem cells through an ERK-dependent pathway. Mol. Biol. Cell 16, 881-890.
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Meeks, M. K., Ripley, M. L., Jin, Z. and Rembold, C. M. (2005). Heat shock protein 20-mediated force suppression in forskolin-relaxed swine carotid artery. Am. J. Physiol. 288, C633-639.
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Turvey, M. R., Fogarty, K. E. and Thorn, P. (2005). Inositol (1,4,5)-trisphosphate receptor links to filamentous actin are important for generating local Ca2+ signals in pancreatic acinar cells. J. Cell Sci. 118, 971-980.
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Bharadwaj, S., Hitchcock-DeGregori, S., Thorburn, A. and Prasad, G. L. (2004). N terminus is essential for tropomyosin functions: N-terminal modification disrupts stress fiber organization and abolishes anti-oncogenic effects of tropomyosin-1. J. Biol. Chem. 279, 14039-14048.
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Chen, G., Raman, P., Bhonagiri, P., Strawbridge, A. B., Pattar, G. R. and Elmendorf, J. S. (2004). Protective effect of phosphatidylinositol 4,5-bisphosphate against cortical filamentous actin loss and insulin resistance induced by sustained exposure of 3T3-L1 adipocytes to insulin. J. Biol. Chem. 279, 39705-39709.
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Kojima, K., Musch, M. W., Ropeleski, M. J., Boone, D. L., Ma, A. and Chang, E. B. (2004). Escherichia coli LPS induces heat shock protein 25 in intestinal epithelial cells through MAP kinase activation. Am. J. Physiol. 286, G645-652.
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Strachan, L. R. and Condic, M. L. (2004). Cranial neural crest recycle surface integrins in a substratum-dependent manner to promote rapid motility. J. Cell Biol. 167, 545-554.
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Lyerla, T. A., Rusiniak, M. E., Borchers, M., Jahreis, G., Tan, J., Ohtake, P., Novak, E. K. and Swank, R. T. (2003). Aberrant lung structure, composition, and function in a murine model of Hermansky-Pudlak syndrome. Am. J. Physiol. 285, L643-653.
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Mercer, K. B., Flaherty, D. B., Miller, R. K., Qadota, H., Tinley, T. L., Moerman, D. G. and Benian, G. M. (2003). Caenorhabditis elegans UNC-98, a C2H2 Zn finger protein, is a novel partner of UNC-97/PINCH in muscle adhesion complexes. Mol. Biol. Cell 14, 2492-2507.
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Ono, K., Parast, M., Alberico, C., Benian, G. M. and Ono, S. (2003). Specific requirement for two ADF/cofilin isoforms in distinct actin-dependent processes in Caenorhabditis elegans. J. Cell Sci. 116, 2073-2085.
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Question 1: What is the best way to stain F-actin in cell and tissues?
Answer 1: Cytoskeleton offers our Acti-stain line of fluorescently-labeled phalloidins that specifically stain F-actin in fixed cell and tissue samples. The Acti-stain fluorescent phalloidin probes are very bright and stable and provide a very easy and economical way to label F-actin. Phalloidin is labeled with different green and red fluorophores (Cat. # PHDG1, PHDR1, PHDH1 and PHDN1).
Question 2: What dilution do you recommend for the polyclonal anti-actin antibody?
Answer 2: The dilution of antibody depends on the cell/tissue type and experimental format being used. For western blotting, we have tested and recommend using the antibody at a concentration of 500 ng/ml (1:1000 dilution). At this dilution, we detected actin in cell extracts of Xenopus A6 cells, mouse Swiss 3T3 cells, rat NRK cells, human HeLa cells and platelet cells. For immunofluorescence, we used the anti-actin antibody to detect actin in mouse Swiss 3T3 cells. The antibody was used at a concentration of 2 μg/ml (1:500 dilution) followed by incubation with a 1:500 dilution of anti-rabbit rhodamine-conjugated secondary antibody. This information is found usually in the figure legends or within the “Product Uses” section of our antibody datasheets.
For more information, click on the Document tab above to see the datasheet.
