C-Raf (N-terminal region) (clone M208), anti-human, mouse, rat

Background:
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.

Immunogen: Clone (M208) was generated from a sequence corresponding to amino acids in the N-terminal region of human C-Raf. This C-Raf sequence has high homology to rat and mouse C-Raf.

Specificity: This antibody detects a 74 kDa* protein corresponding to the molecular mass of C-Raf on SDS-PAGE immunoblots of human A431 and Jurkat cells.

Buffer/Storage:
Mouse monoclonal, protein G purified antibody is supplied in 100µl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at -20°C. Stable for 1 year.