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 제품안내  면역학   Cell Structure  Actin Assay

Actin polymerization Assay Kit

Actin binding protein은 세포의 형태와 운동성, 근육수축, intracellular trafficking, cell pathogenesis, signal transduction등의 연구에 관여됩니다. Actin polymerization kit은 actin의 polymerization kinetics를 연구하기위한 modified actin과 시약을 제공합니다.

제품 문의하기

  • Actin polymerization kinetics를 연구하기 위한 modified actin과 시약을 제공합니다.
  • Polymerization중에 발생하는 pyrene conjugated actin의 형광증가 정도를 측정해줍니다.
  • non-muscle actin이나 cardiac actin등의 다른 타입의 polymerization 연구에도 사용될수 있습니다.
Kit의 구성
  • 5 x 1 mg Pyrene labeled actin (Cat. # AP05).
  • General Actin Buffer (Cat. # BSA01).
  • Actin Polymerization Buffer (Cat. # BSA02).
  • ATP 100mM (Cat. # BSA04).
  • Tris-HCl pH 7.5, 100 mM
  • Manual with detailed protocols and extensive troubleshooting guide.
  • To show quantitative / qualitative effects on actin polymerization by the addition of a tissue extract, an actin binding protein or compound.
  • To show quantitative / qualitative effects on actin polymerization by addition of an F-actin nucleating protein, compound or extract.
  • To show quantitative / qualitative effects on steady-state F-actin levels by addition of an F-actin severing protein, compound or tissue extract.
  • To show quantitative / qualitative effects on actin depolymerization by addition of an actin binding protein, compound or tissue extract.
The Actin Polymerization Biochem Kit™ was used to study the effects of Arp2/3 (Cat. # RP01) and the VCA domain of WASP (Cat. # VCG03) on actin polymerization rates. The Arp2/3 complex is an actin filament nucleator but has low nucleating/polymerizing activity on its own. The VCA domain of WASP is an activator of the Arp2/3 complex. Hence, when the Arp2/3 complex is mixed with the WASP VCA domain, these two exert a potent actin polymerizing activity (Fig. 1).
Figure 1. Actin polymerization stimulated by Arp2/3 complex and the VCA domain of WASP. Actin polymerization was measured using kit BK003. The addition of Arp2/3 complex or the VCA domain alone to actin has minimal effects on actin polymerization, while the combination of Arp2/3 and the VCA domain strongly stimulates the rate of actin polymerization.
  • 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.
  • 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.
  • 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.
  • 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.
  • 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.
주문정보(Ordering Information)
BK003Actin polymerization Biochem Kit30-100 assays