Rabbit Polyclonal USP28(Phospho-Ser67) Antibody

The USP28 (Phospho-Ser67) antibody is designed to detect ubiquitin-specific protease 28 (USP28) when phosphorylated at serine 67. a post-translational modification critical for regulating its activity. USP28. a member of the ubiquitin-specific protease family, functions as a deubiquitinase that stabilizes target proteins by removing ubiquitin chains, thereby counteracting proteasomal degradation. It plays roles in DNA damage response, cell cycle control, and apoptosis, often interacting with key regulators like c-Myc and p53. Phosphorylation at Ser67. mediated by kinases such as casein kinase 1 (CK1) or CK2. modulates USP28’s substrate binding, enzymatic activity, or protein-protein interactions, influencing its ability to stabilize oncoproteins or tumor suppressors. This site-specific phosphorylation may also affect USP28’s subcellular localization or stability under stress conditions. The USP28 (Phospho-Ser67) antibody is widely used in research to study USP28’s regulatory mechanisms in cancer biology, particularly in contexts where USP28 is overexpressed, such as in certain carcinomas. It enables detection of endogenous phosphorylated USP28 via techniques like Western blotting, immunoprecipitation, or immunofluorescence, aiding investigations into how post-translational modifications fine-tune USP28’s roles in tumor progression or therapeutic resistance. Validated specificity for the phospho-epitope ensures reliable analysis of USP28 activation states in cellular signaling pathways.