Revision 2

#9967Store at -20C

1 Kit

(7 x 20 microliters)

Cell Signaling Technology

Orders: 877-616-CELL (2355) [email protected]

Support: 877-678-TECH (8324)

Web: [email protected] cellsignal.com

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For Research Use Only. Not for Use in Diagnostic Procedures.
Product Includes Product # Quantity Mol. Wt Isotype/Source
Phospho-Cofilin (Ser3) (77G2) Rabbit mAb 3313 20 µl 19 kDa Rabbit IgG
Cofilin (D3F9) XP® Rabbit mAb 5175 20 µl 19 kDa Rabbit IgG
Phospho-Ezrin (Thr567)/Radixin (Thr564)/Moesin (Thr558) (48G2) Rabbit mAb 3726 20 µl 75 Moesin. 80 Ezrin, Radixin. kDa Rabbit IgG
Ezrin/Radixin/Moesin Antibody 3142 20 µl 75 Moesin. 80 Ezrin and Radixin. kDa Rabbit 
Phospho-VASP (Ser157) Antibody 3111 20 µl 50 kDa Rabbit 
Phospho-VASP (Ser239) Antibody 3114 20 µl 48, 50 kDa Rabbit 
VASP (9A2) Rabbit mAb 3132 20 µl 46, 50 kDa Rabbit 
Anti-rabbit IgG, HRP-linked Antibody 7074 100 µl Goat 

Please visit cellsignal.com for individual component applications, species cross-reactivity, dilutions, protocols, and additional product information.

Description

The Actin Reorganization Antibody Sampler Kit contains reagents to examine proteins that help regulate the dynamic actin cytoskeleton. This kit includes enough primary and secondary antibodies to perform two Western blot experiments with each primary antibody.

Storage

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

Background

Ubiquitous actin protein comprises the major structural component of the eukaryotic cytoskeleton. The formation and continual reorganization of the actin cytoskeleton is a key step in many biological processes, including cell motility, cytokinesis, endocytosis, embryonic development, tissue regeneration and the stress response (1). The small protein cofilin is one of a conserved family of actin-binding proteins that promote actin filament regeneration by severing preexisting filaments (2). Phosphorylation of cofilin at Ser3 by LIMK or TESK inhibits cofilin severing activity (3-5). Ezrin, radixin, and moesin (ERM) proteins function as linker proteins and signal transducers between the plasma membrane and actin cytoskeleton. These proteins are involved in cell adhesion, membrane ruffling, and microvilli formation (6,7). Interactive cytosolic ERM proteins exist as monomers or dimers that form both intra- and intermolecular associations through their amino- and carboxy-terminal domains (8). Phosphorylation at carboxy-terminal threonine residues (Thr567 of ezrin, radixin at Thr564 and Thr558 of moesin) may alter protein conformation and disrupt these protein associations and result in ERM protein activation (9,10). Vasodilator-stimulated phosphoprotein (VASP) is an adaptor protein that links the cytoskeleton with signal transduction pathways to act in fibroblast migration, platelet activation and axon guidance (11,12). Three phosphorylation sites (Ser157, Ser239, and Thr278) have been identified, with phosphorylation of Ser239 by PKG serving as a marker for nitric oxide and cGMP signaling (13). VASP Ser157 can act as a substrate for both PKA and PKC (14,15). Active VASP appears to promote actin polymerization by restricting actin filament capping, with PKA phosphorylation inhibiting this anti-capping activity (16).

  1. Carlier, M.F. et al. (1999) J. Biol. Chem. 274, 33827-33830.
  2. Condeelis, J. (2001) Trends Cell Biol. 11, 288-293.
  3. Arber, S. et al. (1998) Nature 393, 805-809.
  4. Yang, N. et al. (1998) Nature 393, 809-812.
  5. Toshima, J. et al. (2001) J. Biol. Chem. 276, 31449-31458.
  6. Louvet-Vallée, S. (2000) Biol. Cell 92, 305-316.
  7. Ivetic, A. and Ridley, A.J. (2004) Immunology 112, 165-176.
  8. Matsui, T. et al. (1998) J. Cell Biol. 140, 647-657.
  9. Gautreau, A. et al. (2000) J. Cell Biol. 150, 193-203.
  10. Tran Quang, C. et al. (2000) EMBO J. 19, 4565-4576.
  11. Ball, L.J. et al. (2000) EMBO J. 19, 4903-4914.
  12. Machesky, L.M. (2000) Cell 101, 685-688.
  13. Ibarra-Alvarado, C. et al. (2002) Mol. Pharmacol. 61, 312-319.
  14. Smolenski, A. et al. (1998) J. Biol. Chem. 273, 20029-20035.
  15. Chitaley, K. et al. (2004) FEBS Lett. 556, 211-215.
  16. Barzik, M. et al. (2005) J. Biol. Chem. 280, 28653-28662.

Background References

    Trademarks and Patents

    Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
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