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Anti-pan actin: rabbit polyclonal

Anti-pan actin: rabbit polyclonal

*Amount

1x100 ug (Cat. # AAN01-A) +$199.00
3x100 ug (Cat. # AAN01-B) +$515.00

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Product Uses
This antibody is recommended for detection of actin in human, mouse, rat, xenopus, and bovine extracts (Fig. 1 and 2). The following protocols have been tested with this antibody:

	Western Blot	Immunocytochemistry	ELISA	Immunoprecipitation
	Yes	Yes	Yes	No

Material
Rabbit polyclonal antibody against actin protein. Actin is the major protein of the microfilament cytoskeletal system and is a key protein in various cell motility processes. The immunogen used for antibody production was a peptide consisting of the 11 C-terminal amino acids of actin. Human platelet extract (Cat. # EXT01) is included as a positive control for Western blot analysis. A characteristic actin band at 43 kDa is identified on Western blots (see Fig. 1). Antiactin antibody is supplied as a lyophilized white powder.

Example Results

Figure 1. Western blot analysis of anti-actin antibody. Protein samples were separated by electrophoresis and transferred to PVDF membrane as described in the methods. Anti-actin antibody was diluted to 500 ng/ml (1:1000) for Western blot analysis. Actin was detected in 10 μg of platelet extract (43 kDa). Molecular weight markers are from Invitrogen.

Figure 2. Western blot of purified actin and cell extracts probed with anti-actin antibody. Chemiluminescence detection of skeletal muscle actin (100 ng, lane 1), and in cell extracts of Xenopus A6 cells (lane 2), mouse Swiss 3T3 cells (50 μg, lane 3), rat NRK cells (50 μg, lane 4), human HeLa cells (50 μg, lane 5), and platelet cells (50 μg, lane 6). The actin band is indicated at 43 kDa (see arrow). The blot was probed with a 500 ng/ml (1:1000) dilution of antiactin antibody.

Figure 3. Immunofluorescence images of mouse Swiss 3T3 cells stained with anti-actin antibody. Swiss 3T3 cells were grown to 50% confluency and fixed with methanol. Immunofluorescence staining using 2 μg/ml (1:500 dilution) of anti-actin antibody is shown (red). The primary antibody was detected with a 1:500 dilution of goat anti-rabbit rhodamine conjugated antibody. DNA (blue) was stained with 100 nM DAPI in PBS. Photograph was taken with a 100X objective lens.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

Anti-pan actin: rabbit polyclonal

Anti-pan actin: rabbit polyclonal

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