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| | A Raf antibody Chemical Properties |
| | A Raf antibody Usage And Synthesis |
| Source | Rabbit | | Reactivity | Human;Mouse;Rat | | Background | A-Raf, B-Raf, and c-Raf are the main effectors recruited by GTP-bound Ras to activate the MEK-MAP kinase pathway. Activation of c-Raf is the best understood and involves phosphorylation at multiple activating sites, including Ser338, Tyr341, Thr491, Ser494, Ser497, and Ser499. p21-activated kinase has been shown to phosphorylate c-Raf at Ser338, and the Src family phosphorylates Tyr341 to induce c-Raf activity. Ser338 of c-Raf corresponds to similar sites in A-Raf and B-Raf, although this site is constitutively phosphorylated in B-Raf. Inhibitory 14-3-3 binding sites on c-Raf can be phosphorylated by Akt and AMPK, respectively. While A-Raf, B-Raf, and c-Raf are similar in sequence and function, differential regulation has been observed. Of particular interest, B-Raf contains three consensus Akt phosphorylation sites and lacks a site equivalent to Tyr341 of c-Raf. Research studies have shown that the B-Raf mutation V600E results in elevated kinase activity and is commonly found in malignant melanoma. Six residues of c-Raf become hyperphosphorylated in a manner consistent with c-Raf inactivation. The hyperphosphorylation of these six sites is dependent on downstream MEK signaling and renders c-Raf unresponsive to subsequent activation events. | | References | [1] Avruch, J. et al. (1994) Trends Biochem Sci 19, 279-83.
[2] Chong, H. et al. (2001) EMBO J 20, 3716-27.
[3] King, A.J. et al. (1998) Nature 396, 180-3.
[4] Fabian, J.R. et al. (1993) Mol Cell Biol 13, 7170-9.
[5] Mason, C.S. et al. (1999) EMBO J 18, 2137-48.
[6] Zimmermann, S. and Moelling, K. (1999) Science 286, 1741-4.
[7] Sprenkle, A.B. et al. (1997) FEBS Lett 403, 254-8.
[8] Marais, R. et al. (1997) J Biol Chem 272, 4378-83.
[9] Guan, K.L. et al. (2000) J Biol Chem 275, 27354-9.
[10] Davies, H. et al. (2002) Nature 417, 949-54.
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| | A Raf antibody Preparation Products And Raw materials |
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