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Cdc42 ΔC G12VGST

Cell Division Cycle Protein 42, G12V mutant, C-terminal deletion of 13 residues

human, recombinant, E. coli

Cat. No. Amount Price (EUR) Buy / Note
PR-300 50 μg 212,18 Add to Basket/Quote Add to Notepad

For in vitro use only!

Shipping: shipped on dry ice

Storage Conditions: store at -80 °C
avoid freeze/thaw cycles

Shelf Life: 12 months

Molecular Weight: 19.8 kDa (178 amino acids)

Accession number: AF498962

Accession number: AF498962

Purity: > 90 % (SDS-PAGE)

Form: liquid (Supplied in 50 mM Tris-HCl pH 7.5, 100 mM NaCl, 5 mM MgCl2 and 5 mM beta-mercaptoethanol)

Rho family GTPases Rac1 and Cdc42 (cell division cycle 42) belong to the Ras superfamily of small GTP-binding proteins. The human homolog of yeast Cdc42 is essential for cell polarity and regulates cytoskeletal rearrangements in responses to growth factor stimulation. The C-terminal deletion of 13 amino acids of Cdc42 ΔC includes the polybasic domain consisting of six contiguous basic amino acids. The polybasic domain of Cdc42 is required for homodimer formation. The Gly12 to Val mutation of Cdc42 ΔC leads to a constitutive active protein. The GST-Tag facilitates the protein`s application in typical GST pull-down assays.

Selected References:
Wedlich-Soldner et al. (2003) Spontaneous cell polarization through Actomyosin-based delivery of the Cdc42 GTPase. Science 299:1231.
Zhang et al. (2001) Oligomerization of Rac1 GTPase mediated by carboxy-terminal polybasic domain. J. Biol. Chem. 276:8958.
Zhang et al. (1999) A built-in arginine finger triggers the selfstimulatory GTPase-activating activity of Rho family GTPases. J. Biol. Chem. 274:2609.
Zhang et al. (1998) Negative regulation of Rho family GTPases Cdc42 and Rac2 by homodimer formation. J. Biol. Chem. 273:25728.
Chamberlain et al. (2004) The p85alpha Subunit of Phosphatidylinositol 3’-Kinase Binds to and Stimulates the GTPase Activity of Rab Proteins. J. Biol. Chem. 279 (47):48607.
Rudolph et al. (1999) Nucleotide binding to the G12V-mutant of Cdc42 investigated by X-ray diffraction and fluorescence spectroscopy: two different nucleotide states in one crystal. Protein Sci. 8:778.