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- Cdc42 protein: His tagged: human wild type
Cdc42 protein: His tagged: human wild type
Product Uses Include
- Cdc42 biochemistry
- Cdc42 GTPase assays
- Cdc42 nucleotide exchange assays
- Cdc42 binding studies
The human Cdc42 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 22 kDa, consisting of the 22 kDa Cdc42 protein plus a 6 amino acid histidine tag in the amino-terminus.
For other forms of Cdc42 as well as many other purified small G-proteins, see our main small G-protein product page.
Purity is determined by scanning densitometry of proteins on SDS-PAGE gels. His-Cdc42 samples are >90% pure.
Figure 1: His-Cdc42 protein purity determination. A 10 µg sample of CD01 (His-Cdc42 molecular weight approx. 22 kDa) was separated by electrophoresis in a 12% SDS-PAGE system. The protein was stained with Coomassie Blue.
The biological activity of CD01 is determined by its ability to exchange nucleotide. This is tested by a pulldown assay using GST-tagged PAK-1 PBD beads (Cat. # PAK02) and GTPγS (Cat. # BS01) or GDP loaded His-Cdc42. The PAK (p21 activated kinase) protein is an effector of Cdc42, and will specifically bind to the GTP bound form Cdc42. Using this assay, the amount of biologically active GTP-bound Cdc42 is determined. Stringent quality control ensures that >70% of the Cdc42 protein produced is capable of binding GTP.
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 email@example.com
Nevins, A. K. and Thurmond, D. C. (2005). A direct interaction between Cdc42 and vesicle-associated membrane protein 2 regulates SNARE-dependent insulin exocytosis. J. Biol. Chem. 280, 1944-1952.
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.
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