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Actin & Actin Binding Proteins

Actin & Actin Binding Proteins

Cytoskeleton's actin 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 protein (>99% pure): rabbit skeletal muscle (Cat. # AKL99)

Windhorst S, Kalinina T, Schmid K, Blechner C, Kriebitzsch N, Hinsch R, Chang L, Herich L, Schumacher U, Mayr GW. (2010). Functional role of inositol-1,4,5-trisphosphate-3-kinase-A for motility of malignant transformed cells. Int J Cancer.

Arora, P. D., Glogauer, M., Kapus, A., Kwiatkowski, D. J. and McCulloch, C. A. (2004). Gelsolin mediates collagen phagocytosis through a rac-dependent step. Mol. Biol. Cell 15, 588-599.

Ishikawa, T., Cheng, N., Liu, X., Korn, E. D. and Steven, A. C. (2004). Subdomain organization of the Acanthamoeba myosin IC tail from cryo-electron microscopy. Proc. Natl. Acad. Sci. U. S. A. 101, 12189-12194.

Balcer, H. I., Goodman, A. L., Rodal, A. A., Smith, E., Kugler, J., Heuser, J. E. and Goode, B. L. (2003). Coordinated regulation of actin filament turnover by a high-molecular-weight Srv2/CAP complex, cofilin, profilin, and Aip1. Curr. Biol. 13, 2159-2169.

Loomis, P. A., Zheng, L., Sekerkova, G., Changyaleket, B., Mugnaini, E. and Bartles, J. R. (2003). Espin cross-links cause the elongation of microvillus-type parallel actin bundles in vivo. J. Cell Biol. 163, 1045-1055.

Upadhyaya, A., Chabot, J. R., Andreeva, A., Samadani, A. and van Oudenaarden, A. (2003). Probing polymerization forces by using actin-propelled lipid vesicles. Proc. Natl. Acad. Sci. U. S. A. 100, 4521-4526.

Humphries, C. L., Balcer, H. I., D'Agostino, J. L., Winsor, B., Drubin, D. G., Barnes, G., Andrews, B. J. and Goode, B. L. (2002). Direct regulation of Arp2/3 complex activity and function by the actin binding protein coronin. J. Cell Biol. 159, 993-1004.

Sagot, I., Rodal, A. A., Moseley, J., Goode, B. L. and Pellman, D. (2002). An actin nucleation mechanism mediated by Bni1 and profilin. Nat. Cell Biol. 4, 626-631.

Engqvist-Goldstein, A. E., Warren, R. A., Kessels, M. M., Keen, J. H., Heuser, J. and Drubin, D. G. (2001). The actin-binding protein Hip1R associates with clathrin during early stages of endocytosis and promotes clathrin assembly in vitro. J. Cell Biol. 154, 1209-1223.

McGhie, E. J., Hayward, R. D. and Koronakis, V. (2001). Cooperation between actin-binding proteins of invasive Salmonella: SipA potentiates SipC nucleation and bundling of actin. EMBO J. 20, 2131-2139.

Actin Polymerization Biochem Kit (fluorescence format): rabbit skeletal muscle actin (Cat. # BK003)

Takamiya, R., Takahashi, M., Park, Y. S., Tawara, Y., Fujiwara, N., Miyamoto, Y., Gu, J., Suzuki, K. and Taniguchi, N. (2005). Overexpression of mutated Cu,Zn-SOD in neuroblastoma cells results in cytoskeletal change. Am. J. Physiol. 288, C253-259.

Kumar, N., Tomar, A., Parrill, A. L. and Khurana, S. (2004). Functional dissection and molecular characterization of calcium-sensitive actin-capping and actin-depolymerizing sites in villin. J. Biol. Chem. 279, 45036-45046.

Fontao, L., Geerts, D., Kuikman, I., Koster, J., Kramer, D. and Sonnenberg, A. (2001). The interaction of plectin with actin: evidence for cross-linking of actin filaments by dimerization of the actin-binding domain of plectin. J. Cell Sci. 114, 2065-2076.

Zhai, L., Zhao, P., Panebra, A., Guerrerio, A. L. and Khurana, S. (2001). Tyrosine phosphorylation of villin regulates the organization of the actin cytoskeleton. J. Biol. Chem. 276, 36163-36167.

Blader, I. J., Cope, M. J., Jackson, T. R., Profit, A. A., Greenwood, A. F., Drubin, D. G., Prestwich, G. D. and Theibert, A. B. (1999). GCS1, an Arf guanosine triphosphatase-activating protein in Saccharomyces cerevisiae, is required for normal actin cytoskeletal organization in vivo and stimulates actin polymerization in vitro. Mol. Biol. Cell 10, 581-596.

Cofilin 1 protein: human recombinant (Cat. # CF01)

van der Gucht, J., Paluch, E., Plastino, J. and Sykes, C. (2005). Stress release drives symmetry breaking for actin-based movement. Proc. Natl. Acad. Sci. U. S. A. 102, 7847-7852.

Vignjevic, D., Yarar, D., Welch, M. D., Peloquin, J., Svitkina, T. and Borisy, G. G. (2003). Formation of filopodia-like bundles in vitro from a dendritic network. J. Cell Biol. 160, 951-962.

Yokoo, T., Toyoshima, H., Miura, M., Wang, Y., Iida, K. T., Suzuki, H., Sone, H., Shimano, H., Gotoda, T., Nishimori, S. et al. (2003). p57Kip2 regulates actin dynamics by binding and translocating LIM-kinase 1 to the nucleus. J. Biol. Chem. 278, 52919-52923.

Idrissi, F. Z., Wolf, B. L. and Geli, M. I. (2002). Cofilin, but not profilin, is required for myosin-I-induced actin polymerization and the endocytic uptake in yeast. Mol. Biol. Cell 13, 4074-4087.

Question 1: What format is best when designing an assay that measures actin polymerization modulated by an actin binding protein (ABP)?

Answer 1: The best way to measure the effects of an ABP on actin polymerization is to use Cytoskeleton’s actin polymerization biochem kit (Cat. # BK003). The kit uses pyrene-labeled actin to visualize actin polymerization (and depolymerization, if desired). This kit can be adapted to multiple actin sources (muscle, non-muscle, cardiac) and is ideal for discovering and/or characterizing ABPs in the form of compounds, purified proteins or tissue extracts. Changes in one or more of the three stages of polymerization (nucleation, growth or steady state) can be evaluated with this kit. The kit comes with all of the necessary reagents and buffers to perform actin polymerization assays. Click on the Citations tab for references of where these kits were used in research projects.

Question 2: Do you have an actin monomer binding assay?

Answer 2: To examine compounds, proteins or tissue extracts that bind to actin monomers, 96-well plates with streptavidin-coated wells can be complexed with biotinylated actin (Cat. # AB07) to create an actin monomer capture protein. Then the compound, protein or extract can be incubated with the capture proteins and binding can be visualized by an HRP detection system using an antibody (or a tag can be conjugated to the test protein) against the compound or protein of interest. Keep in mind that buffer composition is also important as it will need to be low salt (approx 50 mM) and contain CaCl2 (or other divalent cation) and ATP to maintain actin monomer stability. For an example of a compatible buffer, see our recipe for general actin buffer (Cat. # BSA01-001). Alternatively, the protein of interest could be tagged with GST (avoid reducing agents) and conjugated to the plate and then incubated with biotinylated actin and visualized with HRP-conjugated streptavidin.

For more information, click on Documents and see the datasheet, or for Technical Support, e-mail tservice@cytoskeleton.com.

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