USP28 Recombinant Rabbit mAb (S-5357)

USP28 (Ubiquitin Specific Peptidase 28) is a deubiquitinating enzyme belonging to the USP family that plays a critical role in maintaining genomic stability and regulating cellular stress responses by specifically removing ubiquitin chains from key substrate proteins to prevent their proteasomal degradation. It is best characterized for its essential function in the DNA damage response, where it stabilizes checkpoint mediators such as 53BP1, RNF168, and Claspin to facilitate efficient DNA repair and cell cycle arrest, while also modulating the stability of transcription factors like c-MYC and ΔNp63 to influence cell proliferation and differentiation. Given its involvement in these vital pathways, USP28 is frequently overexpressed in various malignancies, including colorectal, breast, and lung cancers, where it promotes tumorigenesis and therapy resistance, making it an emerging therapeutic target for cancer treatment strategies aimed at restoring proper protein homeostasis and sensitizing tumor cells to DNA-damaging agents.