The human retinoblastoma gene product appears to play an important role in the negative egulation of cell proliferation. Functional inactivation of Rb can be mediated either through mutation or as a consequence of interaction with DNA tumor virus-encoded proteins. Of all the Rb associations described to date, the identification of a complex between Rb and the transcription factor E2F most directly implicates Rb in regulation of cell proliferation. E2F was originally identified through its role in transcriptional activation of the adenovirus E2 promoter. Sequences homologous to the E2F binding site have been found upstream of a number of genes that encode proteins with putative functions in the G1 and S phases of the cell cycle. E2F-1 forms heterodimers with a second protein, designated DP-1, forming an ''active E2F transcriptional regulatory complex. Additional members of the E2F family include E2F-2, E2F-3, E2F-4, E2F-5 and DP-2.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB: 1:500~1:1000 IHC: 1:50~1:200 IF: 1:50~1:200
Application Notes:
TFDP1 (V393) polyclonal antibody detects endogenous levels of TFDP1 protein.
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