Rac1 protein: GST tagged: human wild type

Rac1 protein: GST tagged: human wild type
$0.00

Product Uses Include

  • Rac biochemistry
  • Rac1 GTPase assays
  • Rac1 nucleotide exchange assays
  • Rac1 binding studies

Material
The human Rac1 protein has been produced in a bacterial expression system. The protein is supplied as a lyophilized powder. When it is reconstituted in distilled water to 1 mg/ml, the protein is in the following buffer: 2 mM Tris pH 7.6, 0.5 mM MgCl2, 0.5% sucrose, 0.1% dextran. Protein concentration is determined by the Precision Red Advanced Protein Assay Reagent, Cat. # ADV02.

The recombinant protein is 50 kDa, consisting of the 22 kDa Rac1 protein plus a 28 kDa GST tag in the amino-terminus.

For other forms of Rac1 as well as many other purified small G-proteins, see our main small G-protein product page.

Purity
Purity is determined by scanning densitometry of proteins on SDS-PAGE gels. GST-Rac1 samples are >90% pure.

rcg01gel

Figure 1: GST-Rac1 protein purity determination. A 20 µg sample of RCG01 (GST-Rac1 molecular weight approx. 50 kDa) was separated by electrophoresis in a 12% SDS-PAGE system. The protein was stained with Coomassie Blue.

Biological Activity
The biological activity of GST-Rac1 protein was monitored by measuring the ability of the protein to hydrolyze GTP in the presence and absence of a GTPase-activating protein (RhoGAP) using Cat. # BK055. In the absence of RhoGAP (Cat. # GAS01), GST-Rac1 hydrolyzed 40-50% of bound GTP in 5 min at 23ºC, while in the presence of RhoGAP (1:1 RhoGAP : GST-Rac1) 75-80% of bound GTP was hydrolyzed under identical conditions.

For product Datasheets and MSDSs please click on the PDF links below.   For additional information, click on the FAQs tab above or contact our Technical Support department at tservice@cytoskeleton.com

Teckchandani, A. M., Panetti, T. S. and Tsygankov, A. Y. (2005). c-Cbl regulates migration of v-Abl-transformed NIH 3T3 fibroblasts via Rac1. Exp. Cell Res. 307, 247-258.

Grabham, P. W., Reznik, B. and Goldberg, D. J. (2003). Microtubule and Rac 1-dependent F-actin in growth cones. J. Cell Sci. 116, 3739-3748.

Li, X., Bu, X., Lu, B., Avraham, H., Flavell, R. A. and Lim, B. (2002). The hematopoiesis-specific GTP-binding protein RhoH is GTPase deficient and modulates activities of other Rho GTPases by an inhibitory function. Mol. Cell. Biol. 22, 1158-1171.

Lesser, C. F. and Miller, S. I. (2001). Expression of microbial virulence proteins in Saccharomyces cerevisiae models mammalian infection. EMBO J. 20, 1840-1849.

Slater, S. J., Seiz, J. L., Stagliano, B. A. and Stubbs, C. D. (2001). Interaction of protein kinase C isozymes with Rho GTPases. Biochemistry 40, 4437-4445.

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