Rhodamine phalloidin (PHDR1)

Material
Phalloidin's usefulness as a laboratory tool is well established and lies in it's ability to inhibit microfilament de-polymerization. Thus, phalloidin stabilized microfilaments are used as substrates for the identification and characterization of the ever increasing number of microfilament associated proteins. In addition, rhodamine phalloidin can be used for staining the actin cytoskeleton in cells, and also as a fluorescent marker/stabilizer for microfilaments used in motility assays.

The rhodamine phalloidin is provided as a lyophilized powder. When reconstituted with 500 µl methanol, it is at 14 µM (200 x stock).

Purity
In keeping with our policy of providing only the highest quality products, we are now pleased to inform you that Cytoskeleton is offering rhodamine phalloidin at a chromatographic purity of >99%. This is the purest phalloidin commercially available for research use.

Biological Activity
We have determined that the microfilament stabilizing property of our product is equal or superior to any other commercially available phalloidins. Microfilaments in 70 nM phalloidin are stable at room temperature for over one week.

Figure 1. A Swiss 3T3 fibroblast stained with rhodamine phalloidin (PHDR1). The phalloidin binds specifically to F-actin and does therefore stain the actin stress fibers in the cell

Examples of publications where this product was used:
Chandhoke, S. K., Williams, M., Schaefer, E., Zorn, L. and Blystone, S. D. (2004). β3 integrin phosphorylation is essential for Arp3 organization into leukocyte αVβ3-vitronectin adhesion contacts. J. Cell Sci. 117, 1431-1441.

Chen, J., Fabry, B., Schiffrin, E. L. and Wang, N. (2001). Twisting integrin receptors increases endothelin-1 gene expression in endothelial cells. Am J Physiol Cell Physiol 280, C1475-1484.

Ezratty, E. J., Partridge, M. A. and Gundersen, G. G. (2005). Microtubule-induced focal adhesion disassembly is mediated by dynamin and focal adhesion kinase. Nat. Cell Biol. 7, 581-590.

Gomes, E. R., Jani, S. and Gundersen, G. G. (2005). Nuclear movement regulated by Cdc42, MRCK, myosin, and actin flow establishes MTOC polarization in migrating cells. Cell 121, 451-463.

Hsieh-Wilson, L. C., Benfenati, F., Snyder, G. L., Allen, P. B., Nairn, A. C. and Greengard, P. (2003). Phosphorylation of spinophilin modulates its interaction with actin filaments. J. Biol. Chem. 278, 1186-1194.

Qian, Y., Baisden, J. M., Cherezova, L., Summy, J. M., Guappone-Koay, A., Shi, X., Mast, T., Pustula, J., Zot, H. G., Mazloum, N. et al. (2002). PKC phosphorylation increases the ability of AFAP-110 to cross-link actin filaments. Mol. Biol. Cell 13, 2311-2322.