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.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFIHC
recommended for detection of Thr 358 phosphorylated c-Myc of mouse, rat and human origin by WB, IP, IF and IHC(P):
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to phosphorylated Thr 358 of c-Myc of human origin
Tissue Specificity
epitope corresponding to phosphorylated Thr 358 of c-Myc of human origin
Search the catalog number from any major antibody supplier/brand in the search bar above. The search engine will return OmnimAbs products for these targets.