Protein protein interaction immunofluorescence result.
Representative image of Proximity Ligation Assay of protein-protein interactions between CDC6 and E2F1. HeLa cells were stained with anti-CDC6 rabbit purified polyclonal antibody 1:1200 and anti-E2F1 mouse monoclonal antibody 1:50. Each red dot represents the detection of protein-protein interaction complex. The images were analyzed using an optimized freeware (BlobFinder) download from The Centre for Image Analysis at Uppsala University.
Antibody pair set content: 1. CDC6 rabbit purified polyclonal antibody (20 ug) 2. E2F1 mouse monoclonal antibody (40 ug) *Reagents are sufficient for at least 30-50 assays using recommended protocols.
Store reagents of the antibody pair set at -20°C or lower. Please aliquot to avoid repeated freeze thaw cycle. Reagents should be returned to -20°C storage immediately after use.
Representative image of Proximity Ligation Assay of protein-protein interactions between CDC6 and E2F1. Huh7 cells were stained with anti-CDC6 rabbit purified polyclonal antibody 1:1200 and anti-E2F1 mouse monoclonal antibody 1:50. Each red dot represents the detection of protein-protein interaction complex, and nuclei were counterstained with DAPI (blue).
The protein encoded by this gene is highly similar to Saccharomyces cerevisiae Cdc6, a protein essential for the initiation of DNA replication. This protein functions as a regulator at the early steps of DNA replication. It localizes in cell nucleus during cell cyle G1, but translocates to the cytoplasm at the start of S phase. The subcellular translocation of this protein during cell cyle is regulated through its phosphorylation by Cdks. Transcription of this protein was reported to be regulated in response to mitogenic signals through transcriptional control mechanism involving E2F proteins. [provided by RefSeq
The protein encoded by this gene is a member of the E2F family of transcription factors. The E2F family plays a crucial role in the control of cell cycle and action of tumor suppressor proteins and is also a target of the transforming proteins of small DNA tumor viruses. The E2F proteins contain several evolutionally conserved domains found in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain. This protein and another 2 members, E2F2 and E2F3, have an additional cyclin binding domain. This protein binds preferentially to retinoblastoma protein pRB in a cell-cycle dependent manner. It can mediate both cell proliferation and p53-dependent/independent apoptosis. [provided by RefSeq
OTTHUMP00000030661,retinoblastoma-associated protein 1