General Actin BufferGeneral Actin Buffer
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General Actin Buffer

Product Uses Include

•  Resuspension of actin protein
•  Dilution and storage of G-actin protein

Material
This buffer contains 5 mM Tris-HCl pH 8.0 and 0.2 mM CaCl2. Used as a general G-actin (monomer) buffer with the addition of 0.2 mM ATP (see Cat. # BSA04) and 0.5 mM DTT (A-buffer). The buffer can be changed to a general F-actin (filament supporting) buffer by the addition of 1/10th volume of actin polymerization buffer (see Cat. # BSA02).

Cat# Size Price Qty Buy
BSA01-001 1 x 10 ml
£53.04
BSA01-010 1 x 100 ml
£116.22

Additional Information

Property Value or Rating
Manufacturer Cytoskeleton, Inc
Storage 4°C
References

Xiao et al., 2013. c-Yes regulates cell adhesion at the apical ectoplasmic specialization-blood-testis barrier axis via its effects on protein recruitment and distribution. Am. J. Physiol. Endocrinol. Metab. 304, E145-E159. 

Butler et al., 2012. Inhibitory effects of pectenotoxins from marine algae on the polymerization of various actin isoforms. Toxicol. In Vitro. 26, 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. 420, 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. 279, 2892-2904.

Tsai et al., 2011. 7-Chloro-6-piperidin-1-yl-quinoline-5,8-dione (PT-262), a novel ROCK inhibitor blocks cytoskeleton function and cell migration. Biochem. Pharmacol. 81, 856-865.

Trigili et al., 2011. Mechanism of Action of the Cytotoxic Macrolides Amphidinolide X and J. ChemBioChem.12, 1027-1030.

Takamiya et al., 2005. Overexpression of mutated Cu,Zn-SOD in neuroblastoma cells results in cytoskeletal change. Am. J. Physiol. 288, 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. 279, 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. 114, 2065-2076.

Zhai et al., 2001. Tyrosine phosphorylation of villin regulates the organization of the actin cytoskeleton. J. Biol. Chem . 276, 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. 10, 581-596.

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