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The Guanine nucleotide Exchange Factor domain (GEF domain, also known as the DH/PH tandem domain) of the human RhoGEF Dbs (hDbs) has been produced in a bacterial expression system with a 6xHis tag at its amino terminus. Dbs is an efficient GEF for the RhoA and Cdc42 GTPases and it shows weak GEF activity towards Rac1.
The molecular weight of this His-hDbs DH/PH protein is approximately 40 kDa. The protein is supplied as a lyophilized powder. When reconstituted to 2 mg/ml, the protein is in the following buffer: 20 mM Tris pH 7.5, 0.5 mM MgCl2, 0.5% sucrose and 0.1% dextran. Protein concentration is determined by the Precision Red Advanced Protein Assay Reagent (Cat. # ADV02).
Purity is determined by scanning densitometry of proteins run on SDS-PAGE gels. Samples are >80% pure.
Figure 1: His-hDbs DH/PH protein purity determination. A 10 µg sample of GE01 was separated by electrophoresis in a 12% SDS-PAGE system. The protein was stained with Coomassie Blue.
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|Kanie, Tomoharu et al.||The CEP19-RABL2 GTPase Complex Binds IFT-B to Initiate Intraflagellar Transport at the Ciliary Base||Developmental Cell||2017||ISSN 1878-1551|
|Reichman, Melvin et al.||A high-throughput assay for rho guanine nucleotide exchange factors based on the transcreener GDP assay||Journal of Biomolecular Screening||2015||ISSN 1552-454X|
|Jeon, Hyeona et al.||Phospholipase D2 induces stress fiber formation through mediating nucleotide exchange for RhoA||Cellular Signalling||2011||ISSN 0898--6568|
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