EID1 polyclonal antibody

E1A-like inhibitor of differentiation-1 (EID-1), an acetyltransferase enzyme, binds both the retinoblastoma protein (Rb), a regulator of cell cycle and tissue specific transcription, and the adenovirus E1A-associated cellular p300 transcriptional co-activator protein. EID-1 inhibits cellular differentiation by blocking the histone acetyltransferase activity of p300. EID-1 also acetylates both histones and non-histone proteins such as NCOA3 co-activator. By acetylating histones, EID-1 gives a specific tag for transcriptional activation. In addition to binding Rb and p300, EID-1 also binds to phosphorylated CREB protein, mediating cAMP gene regulation. EID-1 augments the activity of phosphorylated CREB and activates transcription of cAMP responsive genes as a co-activator.

EP300-interacting inhibitor of differentiation 1; 21 kDa pRb-associated protein; CREBBP/EP300 inhibitory protein 1; E1A-like inhibitor of differentiation 1; EID-1

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE)

Western blot (WB) analysis of EID1 polyclonal antibody at 1:500 dilution Lane1:PC3 whole cell lysate (40ug) Lane2:HCC827 whole cell lysate (40ug) Lane3:HCT116 whole cell lysate (40ug) Lane4:SK-OVCAR3 whole cell lysate (40ug)