Product Datasheet  
Raf1 Antibody  
Catalog Number: 21566  
Technical:tech@swbio.com  
Information:info@swbio.com  
Description  
  • host_species：  
  • Rabbit
  • Amount：  
  • 100μgμg
  • Swiss-Prot No.：  
  • Swiss-Prot: P11345
    NCBI Protein: NP_036771.1
  • Form of Antibody：  
  • Supplied at 1.0mg/mL in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
  • Storage：  
  • Store at -20°C for long term preservation (recommended). Store at 4°C for short term use.
  • Immunogen：  
  • Peptide sequence around aa. 641-645(T-S-P-R-L ) derived from Rat Raf-1.
  • reactivity：  
  • Hu Ms Rt
  • appl_detail：  
  • Predicted MW: 74kd
    Western blotting: 1:500~1:1000
  • other_names：  
  • c-RAF; RAF proto-oncogene serine/threonine-protein kinase;
  • Purification：  
  • Antibodies were produced by immunizing rabbits with synthetic peptide and KLH conjugates. Antibodies were purified by affinity-chromatography using epitope-specific peptide
  • Specificity：  
  • The antibody detects endogenous level of total Raf-1 protein.
  • Applications：  
  • WB
  • 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). 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

    Avruch, J. et al. (1994) Trends Biochem. Sci. 19, 279-283.
    Chong, H. et al. (2001) EMBO J. 20, 3716-3727.
    King, A.J. et al. (1998) Nature 396, 180-183.
    Fabian, J.R. et al. (1993) Mol. Cell Biol. 13, 7170-7179.



 
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