Cell Permeable Rho Inhibitor (C3 Trans based)Cell Permeable Rho Inhibitor (C3 Trans based)
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Cell Permeable Rho Inhibitor (C3 Trans based)

Product Uses Include

  • Inhibit Rho activity within 4h (compared to 24h with siRNA)
  • Stop Rho pathway signalling
  • Determine "activator" specificity for Rho pathway
  • Positive control for Rho Inhibition in cell morphology studies
  • Positive control for Rho inhibition in cell extract biochemical studies
  • Inhibit stress fiber formation
  • Inhibit RhoA, RhoB and RhoC in living cells
  • Inhibits Rho in all cell types currently tested

Material
This product consists of highly purified C3 Transferase (Cat. # CT03) covalently linked to a proprietary cell penetrating moiety via a disulfide bond.  The cell penetrating moiety allows rapid and efficient transport through the plasma membrane.  Once in the cytosol, the cell penetrating moiety is released, thereby allowing C3 Transferase to freely diffuse intracellularly and inactive RhoA, RhoB, and RhoC, but not related GTPases such as Cdc42 or Rac1.

The Exoenzyme C3 Transferase from Clostridium botulinum is commonly used to selectively inactivate the GTPases RhoA, RhoB, and RhoC, both in vivo and in vitro.  C3 Transferase inhibits Rho proteins by ADP-ribosylation on asparagine 41 in the effector binding domain of the GTPase.  A major limitation of C3 Transferase for use in in vivo applications is that this protein is only slightly cell permeable.  Consequently, overnight incubations with C3 Transferase at concentrations as high as 100 µg/ml are often necessary to inactivate Rho proteins in cultured cells.  Under these conditions, the long incubation period and large amount of C3 Transferase that are required can be disruptive to basic cellular functions and economically burdensome.  Cytoskeleton, Inc. has overcome these problems by providing a cell permeable form or C3 Transferase that can efficiently inactivate cellular Rho proteins in as little as 2 h. 

CT04 has been used to inactive Rho proteins to an efficiency of 75-95% in fibroblasts, neurons, epithelial, endothelial, and hematopoietic cells as well as other primary and immortalized cell lines.

Cat# Size Price Qty Buy
CT04-A 1 x 20 µg
£172.11
CT04-B 5 x 20 µg
£514.59
CT04-C 20 x 20 µg
£1,362.16

Additional Information

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

M.J. Herr et al., 2014. Tetraspanin CD9 regulates cell contraction and actin arrangement via RhoA in human vascular smooth muscle cells. PLoS ONE. 9:3106999.

Sakai et al., 2013. LPA1-induced cytoskeleton reorganization drives fibrosis through CTGF-dependent fibroblast proliferation. FASEB J. doi: 10.1096/fj.12-219378.

Ginestier et al., 2012. Mevalonate metabolism regulates basal breast cancer stem cells and is a potential therapeutic target. Stem Cells. 30, 1327-1337.

Zhang et al., 2012. Self-Assembling Peptide Nanofiber Scaffold Enhanced with RhoA Inhibitor CT04 Improves Axonal Regrowth in the Transected Spinal Cord. J. Nanomaterials. doi:10.1155/2012/724857.

 Kim et al., 2012. Inhibition of RhoA but not ROCK induces chondrogenesis of chick limb mesenchymal cells. Biochem. Biophys. Res. Comm. 418, 500-505.

 Wan et al., 2012. Regulation of myosin activation during cell–cell contact formation by Par3-Lgl antagonism: entosis without matrix detachment. Mol. Biol. Cell. 23, 2076-2091.

 Balzer et al., 2012. Physical confinement alters tumor cell adhesion and migration phenotypes. FASEB J. doi: 10.1096/fj.12-211441.

Kakudo et al., 2011. The effect of C3 transferase on human adipose-derived stem cells. Hum. Cell. 24, 4165-169.

 Fan et al., 2011. Macrophage Migration Inhibitory Factor and CD74 Regulate Macrophage Chemotactic Responses via MAPK and Rho GTPase. J. Immunol. 186 4915-4924. 

Kim et al., 2009. Statins decrease dendritic arborization in rat sympathetic neurons by blocking RhoA activation. J. Neurochem. 108, 1057-1071.

Martinelli et al., 2009. ICAM-1–mediated endothelial nitric oxide synthase activation via calcium and AMP-activated protein kinase is required for transendothelial lymphocyte migration. Mol. Biol. Cell. 20, 995–1005.

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