Anti-Phospho-Ubiquitin(Ser65)

Phospho-Ubiquitin Ser65 refers to the phosphorylated form of ubiquitin at serine 65, a modification that plays a critical role in regulating the ubiquitin-proteasome system, which is responsible for degrading and recycling damaged or unneeded proteins within the cell. Ubiquitin is a small protein that typically tags other proteins for degradation by attaching to them in a process known as ubiquitination. Phosphorylation of ubiquitin at Ser65 is an important post-translational modification that modulates the function of ubiquitin, influencing its interactions with other proteins and its involvement in various cellular processes. This modification is particularly significant in the regulation of the DNA damage response, protein quality control, and the modulation of cellular stress responses. Research on phospho-Ubiquitin Ser65 focuses on its role in these pathways and its potential implications in diseases like cancer, neurodegeneration, and other disorders associated with protein misfolding and accumulation.