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Ubiquitin antibodies

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Ubiquitin, a small protein found in nearly all eukaryotic cells, plays a fundamental role in regulating various cellular processes. Its primary function is to mark proteins for degradation through the ubiquitin-proteasome system, a highly controlled and selective process known as ubiquitination. When a protein is destined for degradation or clearance, multiple ubiquitin molecules are covalently attached to specific lysine residues on the target protein, forming a polyubiquitin chain. This ubiquitin chain acts as a signal, directing the tagged protein to the proteasome, a large multi-subunit protein complex responsible for protein degradation. Once delivered to the proteasome, the ubiquitinated protein is unfolded and processed, and its constituent amino acids are recycled for the synthesis of new proteins. Apart from its role in protein degradation, ubiquitin also participates in various non-proteolytic functions, such as DNA repair, endocytosis, and signal transduction, where monoubiquitination or other ubiquitin modifications can serve as regulatory signals. The precise and intricate control of ubiquitin-mediated processes ensures proper cellular homeostasis, protein turnover, and the maintenance of critical cellular functions.