RhoA protein: His tagged: human wild type

RhoA protein: His tagged: human wild type
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Product Uses Include

  • RhoA biochemistry
  • RhoA GTPase assays
  • RhoA nucleotide exchange assays
  • RhoA binding studies

Material
The human RhoA 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 approximately 27 kDa, consisting of the RhoA protein plus a histidine tag in the amino-terminus.

For other forms of RhoA 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. His-RhoA samples are >85% pure.

rh01_image-for-web_2
Figure 1: His-RhoA protein purity determination. A 10 µg sample of RH01 (His-RhoA molecular weight approx. 27 kDa) was separated by electrophoresis in a 12% SDS-PAGE system. The protein was stained with Coomassie Blue.

Biological Activity
The biological activity of His-RhoA is determined from its ability to catalyze the exchange of GDP for GTP. The human Dbs (DH/PH) protein (Cat. # GE01) is an exchange factor for RhoA and Cdc42, and is used with the RhoGEF exchange assay Biochem Kit™ (Cat. # BK100) to monitor the exchange ability of His-RhoA. Stringent quality control ensures that the exchange rate (Vmax) of RhoA is enhanced eight fold in the presence of an equimolar amount of hDbs.

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

Lee, J. H., Katakai, T., Hara, T., Gonda, H., Sugai, M. and Shimizu, A. (2004). Roles of p-ERM and Rho-ROCK signaling in lymphocyte polarity and uropod formation. J. Cell Biol. 167, 327-337.

Kulkarni, S., Goll, D. E. and Fox, J. E. (2002). Calpain cleaves RhoA generating a dominant-negative form that inhibits integrin-induced actin filament assembly and cell spreading. J. Biol. Chem. 277, 24435-24441.

Coming soon!   If you have any questions concerning this product, please contact our Technical Service department at tservice@cytoskeleton.com