KRasHis - G-domain

For general laboratory use.

Envio: shipped on gel packs

Condições de armazenamento: store at -20 °C
avoid freeze/thaw cycles

Validade: 12 months

Peso molecular: 25 kDa

Número de acesso: NM_004985.3

Número de acesso: NM_004985.3

Pureza: > 90 % (SDS-PAGE)

Forma: liquid (Supplied in PBS pH 7.5, 5 mM MgCl2 and 50 % glycerol)

Descrição:
Ras proteins are members of the superfamily of small GTP-binding proteins that function as molecular switches controlling a variety of signalling and transport pathways. KRAS gene performs an essential function in normal tissue signaling, and the mutation of a KRAS gene is an essential step in the development of many cancers. KRAS is usually tethered to cell membranes because of the presence of an isoprenyl group on its C-terminus. Protein preparation is 100 % GDP-loaded, measured by HPLC. Human K-Ras is a truncated protein containing amino acids 1-163. The 6His-tag is located at the N-terminus.

Referências selecionadas:
Zimmermann et al. (2013) Small molecule inhibition of the KRAS-PDE≥ interaction impairs oncogenic KRAS signalling. Nature 497:638. Sasazuki et al. (2005) Transformation by Oncogenic RAS Sensitizes Human Colon Cells to TRAIL-induced Apoptosis by Up-regulating Death Receptor 4 and Death Receptor 5 through a MEK-dependent Pathway. J. Biol. Chem. 280:22856. 931Li et al. (2004) Transformation Potential of Ras Isoforms Correlates with Activation of Phosphatidylinositol 3-Kinase but Not ERK. J. Biol. Chem. 279:37398. Wittinghofer et al. (2000) Ras - a molecular switch involved in tumor formation. Angew. Chem. Int. Ed. 39:4192. Li et al. (1997) Uncoupling of membrane ruffling and pinocytosis during Ras signal transduction. J. Biol. Chem. 272:10337. Pacold et al. (2000) Crystal structure and functional analysis of Ras binding to its effector Phosphoinositide 3-kinase. Cell 103:931.