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- Anti-cofilin: rabbit polyclonal
Anti-cofilin: rabbit polyclonal
Product Uses
This antibody is recommended for detection of cofilin in human, mouse, rat, and Xenopus (Fig. 2). The following protocols have been tested with this antibody:
| Western Blot | Immunocytochemistry | ELISA | Immunoprecipitation | |
| Yes | Yes | Yes | No |
Material
ACFL02 is provided as an affinity purified rabbit polyclonal antibody. Cofilin is an actin binding protein that regulates actin dynamics and reorganization through monomer binding and severing of F-actin (reviewed in Bamburg. 1999. Annu Rev Cell Dev Biol. 14:185-230). The antibody was raised against the N-terminal 13-22 amino acids of human cofilin1. Native cofilin has a predicted molecular weight of 19 kD and migrates on an SDS-PAGE gel at 21 kD (Yonezawa et al., 1987; Cell Structure and Function 12:443-452). Platelet cell extract (1 mg; Cat. # EXT01) is included as a Western blot positive control (see Fig. 1). ACFL02 is supplied as a lyophilized white powder.
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Figure 1. Western blot analysis of anti-cofilin antibody (Cat. # ACFL02). Protein samples were separated by electrophoresis and transferred to PVDF membrane as described in the methods. ACFL02 antibody was diluted to 500 ng/ml (1:500) for Western blot analysis. Cofilin was detected in 20 µg of platelet cell extract (see arrow). Molecular weight markers are from Invitrogen. |
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Figure 2. Western blot of cell extracts probed with anti-cofilin antibody (Cat. # ACFL02). Chemiluminescence detection of cofilin (see arrow) in 50 µg human HeLa cell extract (lane 5). Other lanes shown on the blot are Drosophila S2 (lane 1), Xenopus A6 (lane 2), mouse Swiss 3T3 (lane 3), rat NRK (lane 4), and human platelet (lane 6) cell extracts (50 µg each). Molecular weight markers are from Invitrogen. |
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Figure 3. Immunofluorescence images of mouse Swiss 3T3 cells stained with anti-cofilin antibody (Cat. # ACFL02). Mouse Swiss 3T3 cells were grown to semi-confluency and fixed with 3.7% formaldehyde. Immunofluorescence staining using 500 ng/ml (1:250 dilution) ACFL02 antibody is shown (red). The primary antibody was detected with a 1:500 dilution of goat anti-rabbit rhodamine conjugated antibody (Cat. # RG05). DNA (blue) was stained with 100 nM DAPI in PBS. Photograph was taken with a 20X objective lens. |
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
Borm, B., Requardt, R. P., Herzog, V. and Kirfel, G. (2005). Membrane ruffles in cell migration: indicators of inefficient lamellipodia adhesion and compartments of actin filament reorganization. Exp. Cell Res. 302, 83-95.
Gohla, A., Birkenfeld, J. and Bokoch, G. M. (2005). Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics. Nat. Cell Biol. 7, 21-29.
Gupton, S. L., Anderson, K. L., Kole, T. P., Fischer, R. S., Ponti, A., Hitchcock-DeGregori, S. E., Danuser, G., Fowler, V. M., Wirtz, D., Hanein, D. et al. (2005). Cell migration without a lamellipodium: translation of actin dynamics into cell movement mediated by tropomyosin. J. Cell Biol. 168, 619-631.
Osiak, A. E., Zenner, G. and Linder, S. (2005). Subconfluent endothelial cells form podosomes downstream of cytokine and RhoGTPase signaling. Exp. Cell Res. 307, 342-353.
Pullikuth, A., McKinnon, E., Schaeffer, H. J. and Catling, A. D. (2005). The MEK1 Scaffolding Protein MP1 Regulates Cell Spreading by Integrating PAK1 and Rho Signals. Mol. Cell. Biol. 25, 5119-5133.
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.
Ivanov, A. I., McCall, I. C., Parkos, C. A. and Nusrat, A. (2004). Role for actin filament turnover and a myosin II motor in cytoskeleton-driven disassembly of the epithelial apical junctional complex. Mol. Biol. Cell 15, 2639-2651.
Lee, S. and Helfman, D. M. (2004). Cytoplasmic p21Cip1 is involved in Ras-induced inhibition of the ROCK/LIMK/cofilin pathway. J. Biol. Chem. 279, 1885-1891.
Posern, G., Miralles, F., Guettler, S. and Treisman, R. (2004). Mutant actins that stabilise F-actin use distinct mechanisms to activate the SRF coactivator MAL. EMBO J. 23, 3973-3983.
Ruegg, J., Holsboer, F., Turck, C. and Rein, T. (2004). Cofilin 1 is revealed as an inhibitor of glucocorticoid receptor by analysis of hormone-resistant cells. Mol. Cell. Biol. 24, 9371-9382.
Styers, M. L., Salazar, G., Love, R., Peden, A. A., Kowalczyk, A. P. and Faundez, V. (2004). The endo-lysosomal sorting machinery interacts with the intermediate filament cytoskeleton. Mol. Biol. Cell 15, 5369-5382.
Chua, B. T., Volbracht, C., Tan, K. O., Li, R., Yu, V. C. and Li, P. (2003). Mitochondrial translocation of cofilin is an early step in apoptosis induction. Nat. Cell Biol. 5, 1083-1089.
Hryciw, D. H., Wang, Y., Devuyst, O., Pollock, C. A., Poronnik, P. and Guggino, W. B. (2003). Cofilin interacts with ClC-5 and regulates albumin uptake in proximal tubule cell lines. J. Biol. Chem. 278, 40169-40176.
Keezer, S. M., Ivie, S. E., Krutzsch, H. C., Tandle, A., Libutti, S. K. and Roberts, D. D. (2003). Angiogenesis inhibitors target the endothelial cell cytoskeleton through altered regulation of heat shock protein 27 and cofilin. Cancer Res. 63, 6405-6412.
Seike, M., Kondo, T., Mori, Y., Gemma, A., Kudoh, S., Sakamoto, M., Yamada, T. and Hirohashi, S. (2003). Proteomic analysis of intestinal epithelial cells expressing stabilized ƒÀ-catenin. Cancer Res. 63, 4641-4647.
Worthylake, R. A. and Burridge, K. (2003). RhoA and ROCK promote migration by limiting membrane protrusions. J. Biol. Chem. 278, 13578-13584.
Papakonstanti, E. A. and Stournaras, C. (2002). Association of PI-3 kinase with PAK1 leads to actin phosphorylation and cytoskeletal reorganization. Mol. Biol. Cell 13, 2946-2962.
Pawlak, G. and Helfman, D. M. (2002). Post-transcriptional down-regulation of ROCKI/Rho-kinase through an MEK-dependent pathway leads to cytoskeleton disruption in Ras-transformed fibroblasts. Mol. Biol. Cell 13, 336-347.
Sumi, T., Matsumoto, K., Shibuya, A. and Nakamura, T. (2001). Activation of LIM kinases by myotonic dystrophy kinase-related Cdc42-binding kinase ƒ¿. J. Biol. Chem. 276, 23092-23096.
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