BD Pharmingen™ Purified Mouse Anti-Human DP-1

DP-1 and DP-2 are transcription factors which form heterodimers with several members of the E2F family. DP-1 binding to E2F is often required for interaction between E2F and the retinoblastoma family of proteins (Rb, p107 and p130), which restrict E2F/DP complexes to the cytoplasm. These E2F inhibitors are phosphorylated by complexes which are formed during the cell cycle, e.g., cyclin-cdk complexes. Phosphorylation of RB or other inhibitors releases the E2F/DP complex to enter the nucleus, thus providing temporally regulated activation of E2F responsive genes. While some E2F proteins can act alone, formation of a DP-1 heterodimer provides enhanced DNA binding and transcriptional activity to E2F. E2F-DNA binding sites have been identified in the promoter regions of genes important for growth regulation, e.g., c-myc, N-myc, cdc2 and cyclin A as well as within genes which are important for DNA synthesis, e.g., DNA polymerase α and thymidine kinase. Activation of specific gene(s) may also be dependent on the formation of distinct DP/E2F complexes. Cotransfection studies demonstrate specific interactions between E2Fs and DP-1 or -2. DP-1 binds to E2F-1 through -4, while DP-2 is specific for E2F-4. DP-1 may also play a role as a proto-oncogene in cooperation with Ras proteins, a mechanism, which is independent of E2F. DP-1 has a molecular weight of 52-55 kDa by SDS-PAGE. The TFD10 antibody recognizes an epitope between amino acids 83-204 of human DP-1. The specificity of the antibody was verified by immunoprecipitation of in vitro translated DP-1 protein and by western blot analysis of cell extracts.