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9392
Phospho-c-Raf (Ser289) Antibody
Primary Antibodies

Phospho-c-Raf (Ser289) Antibody #9392

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# Product Name Application Reactivity
  • WB
H M

Supporting Data

REACTIVITY
SENSITIVITY
MW (kDa) 74
SOURCE Rabbit

Application Key:

  • W-Western
  • IP-Immunoprecipitation
  • IHC-Immunohistochemistry
  • ChIP-Chromatin Immunoprecipitation
  • IF-Immunofluorescence
  • F-Flow Cytometry
  • E-P-ELISA-Peptide

Species Cross-Reactivity Key:

  • H-Human
  • M-Mouse
  • R-Rat
  • Hm-Hamster
  • Mk-Monkey
  • Mi-Mink
  • C-Chicken
  • Dm-D. melanogaster
  • X-Xenopus
  • Z-Zebrafish
  • B-Bovine
  • Dg-Dog
  • Pg-Pig
  • Sc-S. cerevisiae
  • Ce-C. elegans
  • Hr-Horse
  • All-All Species Expected

Storage:

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

Specificity / Sensitivity

Phospho-c-Raf (Ser289) Antibody detects endogenous levels of c-Raf protein only when phosphorylated at Ser289.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser289 of human c-Raf. Antibodies are purified by protein A and peptide affinity chromatography.

Background

A-Raf, B-Raf, and c-Raf (Raf-1) are the main effectors recruited by GTP-bound Ras to activate the MEK-MAP kinase pathway (1). Activation of c-Raf is the best understood and involves phosphorylation at multiple activating sites including Ser338, Tyr341, Thr491, Ser494, Ser497, and Ser499 (2). p21-activated protein kinase (PAK) has been shown to phosphorylate c-Raf at Ser338, and the Src family phosphorylates Tyr341 to induce c-Raf activity (3,4). Ser338 of c-Raf corresponds to similar sites in A-Raf (Ser299) and B-Raf (Ser445), although this site is constitutively phosphorylated in B-Raf (5). Inhibitory 14-3-3 binding sites on c-Raf (Ser259 and Ser621) can be phosphorylated by Akt and AMPK, respectively (6,7). While A-Raf, B-Raf, and c-Raf are similar in sequence and function, differential regulation has been observed (8). Of particular interest, B-Raf contains three consensus Akt phosphorylation sites (Ser364, Ser428, and Thr439) and lacks a site equivalent to Tyr341 of c-Raf (8,9). Research studies have shown that the B-Raf mutation V600E results in elevated kinase activity and is commonly found in malignant melanoma (10). Six residues of c-Raf (Ser29, Ser43, Ser289, Ser296, Ser301, and Ser642) 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 (11).

  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.
  11. Dougherty MK et al. (2005) Mol Cell 17, 215–24

Pathways & Proteins

Explore pathways + proteins related to this product.

For Research Use Only. Not For Use In Diagnostic Procedures.

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