Phospho-c-Myc (T58+S62) Recombinant Rabbit monoclonal Antibody IgG
Fig1: Western blot analysis of Phospho-c-Myc(T58+S62) on K562 cells lysates using anti-Phospho-c-Myc(T58+S62) antibody at 1/1,000 dilution.
Host Species; Species ReactivityRabbit; Human, Rat
ImmunogenSynthetic phospho-Peptide corresponding to residues surrounding Thr58 and Ser62 of human c-Myc.
Application SummaryWB, ICC/IF, IP
Purification; FormulationProA affinity purified; 1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide.; Liquid form.
ALTnamesMyc proto-oncogene protein, Class E basic helix-loop-helix protein 39, Proto-oncogene c-Myc, Transcription factor p64
Backgroundc-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.(ET1603-24)