Purified anti-Rad23B

Yeast Rad23, originally identified as a DNA repair protein, has been proposed to participate in other cellular functions, i.e., the proteasome-degradation pathway, the process of spindle pole body duplication, and as a component of the anaphase checkpoint. Two human homologs of yeast Rad23 (Rad23A and Rad23B) exhibit high sequence homology with yeast Rad23 and also have been shown to be involved in DNA repair and proteasome-dependent degradation.Rad23B is involved in global genome nucleotide excision repair (GG-NER) by acting as a component of the XPC complex. The XPC complex recognizes a wide spectrum of damaged DNA, characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles, and single-stranded overhangs.The Rad23 family provides an essential connection between the 26S proteasome and ubiquitinated proteins. It can bind simultaneously to the 26S proteasome and to polyubiquitinated substrates to deliver ubiquitinated proteins to the proteasome. It may play a role in endoplasmatic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and by delivering deglycosylated proteins to the proteasome. The interactions of Rad23B, Atx3, and valosin-containing protein (VCP) are dynamic and modulated by proteotoxic stresses. Recent studies also show that Rad23B is a candidate cancer biomarker identified in a genome-wide loss-of-function screen, which influences sensitivity to HDAC inhibitors.