MilliporeSigma™ Ras, Mouse, Alexa Fluor 647, Clone: RAS10,

Description

• Ras proteins are small GTPases controlling cellular pathways that signal for growth, proliferation, and differentiation
• Mammalian genomes harbor three Ras genes (HRAS, NRAS, and KRAS) that encode four GTPases, two of which (K-Ras4A and K-Ras4B) are transcribed from the KRAS gene via two alternative fourth exons
• Ras proteins share nearly identical sequence homology in sequence encoded by exons 1-3 (a.a
• 1-165), while diverge in their C-terminal 24-a.a
• hypervariable region (HVR) encoded by exon 4
• The first 165 amino acids form the catalytic G domain that mediates GDP/GTP binding and association with effectors, exchange factors, and GTPase-activating proteins (GAPs), while the C-terminal HVR is needed for Ras membrane localization, a process necessary for Ras function
• In addition to the removal of initiator methionine (Met1), Ras proteins are posttranslationally modified by farnesylation of Cys186, followed by proteolytical cleavage their C-terminal end three amino acids (a.a
• 187-189) and carboxyl methylation of the newly formed C-terminal prenylcysteine
• H-Ras, N-Ras, and K-Ras4A are further palmitoylated on cysteine residue(s) near the C-terminus (Cys181/Cys184 in H-Ras, Cys181 in N- and K-Ras), while K-Ras4B lacks a palmitoylation site
• Palmitoylation is required for targeting H- and N-Ras to the plasma membrane (PM), while K-Ras4A and K-Ras4B contain a series of lysines that constitute a polybasic region (PBR) capable of interacting with the inner leaflet of the PM through an electrostatic interaction.