Product Datasheet  
c-Myc (Phospho-T58+S62) Antibody  
Catalog Number: 13342  
Technical:tech@swbio.com  
Information:info@swbio.com  
Description  
  • host_species：  
  • Rabbit
  • Amount：  
  • 100μgμg
  • Swiss-Prot No.：  
  • Swiss-Prot#:P01106
  • Form of Antibody：  
  • 1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide.
  • Storage：  
  • Store at -20˚C
  • Immunogen：  
  • Synthetic phospho-peptide corresponding to residues surrounding Thr58 and Ser62 of human c-Myc.
  • reactivity：  
  • Hu, Rt
  • appl_detail：  
  • WB: 1:1,000

    ICC: 1:50-1:200

  • other_names：  
  • Avian myelocytomatosis viral oncogene homolog antibody
    bHLHe39 antibody
    c Myc antibody
    Class E basic helix-loop-helix protein 39 antibody
    MRTL antibody
    Myc antibody
    Myc protein antibody
    Myc proto oncogene p
  • Purification：  
  • ProA affinity purified
  • Specificity：  
  • Applications：  
  • WB, ICC/IF, IP
  • Background：  
  • c-Myc-, N-Myc- and L-Myc-encoded proteins function in cell proliferation, differentiation and neoplastic disease. Myc proteins are nuclear proteins with relatively short half lives. Amplification of the c-Myc gene has been found in several types of human tumors including lung, breast and colon carcinomas, while the N-Myc gene has been found amplified in neuroblastomas. The L-Myc gene has been reported to be amplified and expressed at high level in human small cell lung carcinomas. The presence of three sequence motifs in the c-Myc COOH terminus, including the leucine zipper, the helix-loop-helix and a basic region provided initial evidence for a sequence-specific binding function. A basic region helix-loop-helix leucine zipper motif (bHLH-Zip) protein, designated Max, specifically associates with c-Myc, N-Myc and L-Myc proteins. The Myc-Max complex binds to DNA in a sequence-specific manner under conditions where neither Max nor Myc exhibit appreciable binding. Max can also form heterodimers with at least two additional bHLH-Zip proteins, Mad and Mxi1, and Mad-Max dimers have been shown to repress transcription through interaction with mSin3.



 
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