The Ras-Raf-MAP kinase signaling pathway is involved in control of cell proliferation and differentiation. The Raf kinase family includes A-Raf, B-Raf, and C-Raf. Each family member has three highly conserved regions (CR1-3). The N-terminal CR1 contains the Ras-GTP-binding domain. The CR2 contains a negative regulatory serine residue (C-Raf (S259)/B-Raf(S365)) that may bind 14-3-3 proteins. The CR3 is the catalytic domain that contains phosphorylation sites for Raf-regulating enzymes within two segments, the N-region and the activation segment. Activation of C-Raf involves phosphorylation at many sites including Ser-338, Tyr-341, and multiple catalytic domain sites. EGF receptor activation leads to phosphorylation of Ser-471, which is critical for C-Raf kinase activity and is required for interaction with MEK. In B-Raf, the corresponding conserved site is Ser-578, and mutation of this residue to alanine produces an inactivate kinase. Thus, this Raf phosphorylation site may be critical for kinase activity and may be important for MEK binding and activation.
Zhu, J. et al. (2005) Mol. Biol. Cell 16:4733.
Mason, C.S. et al. (1999) EMBOJ 18(8):2137.
*For more information, see UniProt Accession P04049
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
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