手机验证
研卉生物
30-100 assays
30-100 assays (Cat. # BK003)
Product Uses Include
Introduction
The Actin Polymerization Biochem Kit™ is based on the enhanced fluorescence of pyrene conjugated actin that occurs during polymerization. The enhanced fluorescence that occurs when pyrene G-actin (monomer) forms pyrene F-actin can be measured in a fluorimeter to follow polymerization over time. Also, by using preformed pyrene F-actin, it is possible to follow depolymerization. Both cell/tissue extracts and purified proteins can be added to the reaction mixture to identify their effect on actin polymerization. The components of the kit can also be used separately for other actin based assays such as a spin-down assays to detect F-actin binding proteins (see also BK001) or size exclusion chromatography to identify G-actin binding proteins. See the About Actin page for more information on assays testing actin binding proteins.
While this kit comes with pyrene labeled skeletal muscle actin, it can also be used to study polymerization of other types of actin such as non-muscle actin (Cat. # APHL99) or cardiac actin (Cat. # AD99). Polymerization assays with these actins can be performed using a 10:1 ratio between the actin you want to study and the included pyrene actin
Kit contents
The kit contains enough materials for 30-100 assays depending on assay volume. The following reagents are included:
Equipment needed
Example results
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).
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Butler et al., 2012. Inhibitory effects of pectenotoxins from marine algae on the polymerization of various actin isoforms. Toxicol. In Vitro. v 26, pp 493-499.
Jiwani et al., 2012. Chlamydia trachomatis Tarp cooperates with the Arp2/3 complex to increase the rate of actin polymerization. Biochem. Biophys. Res. Commun. v 420, pp 816-821.
Fan et al., 2012. A role for γS-crystallin in the organization of actin and fiber cell maturation in the mouse lens. FEBS. J. v 279, pp 2892-2904.
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Takamiya et al., 2005. Overexpression of mutated Cu,Zn-SOD in neuroblastoma cells results in cytoskeletal change. Am. J. Physiol. v 288, pp C253-C259.
Kumar et al., 2004. Functional dissection and molecular characterization of calcium-sensitive actin-capping and actin-depolymerizing sites in villin. J. Biol. Chem. v 279, pp 45036-45046.
Fontao et al., 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. v 114, pp 2065-2076.
Zhai et al., 2001. Tyrosine phosphorylation of villin regulates the organization of the actin cytoskeleton. J. Biol. Chem . v 276, pp 36163-36167.
Blader et al., 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. v 10, pp 581-596.
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