RBPSUH Antibody detects endogenous level of total RBPSUH protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Glu111 of human RBPSUH protein. Antibodies are purified by protein A and peptide affinity chromatography.
Background
RBPSUH (Recombining binding protein suppressor of hairless) is the DNA-binding component of the transcription complex regulated by Notch signaling. In the absence of Notch activation, RBPSUH suppresses target gene expression through interactions with a co-repressor complex containing histone deacetylase. Upon activation, the Notch intracellular domain (NICD) enters the nucleus and binds to RBPSUH to displace the co-repressor complex and replace with a transcription activation complex including Maml, histone acetylase p300, leading to the transcription of Notch target genes (1-3). In addition, RBPSUH is also the DNA-binding partner for Epstein-Barr virus (EBV) nuclear antigen 2 (EBNA2), a protein critical for latent viral transcription and immortalization of EBV-infected B cells (4,5).