Human USP8 Antibody

USP8 (Ubiquitin-Specific-Processing protein 8; also UBPY and ubiquitin carboxyterminal hydrolase 8) is a 125-130 kDa member of the peptidase C19 family of proteins. It is a widely expressed deubiquitinating enzyme that regulates the internalization and trafficking of transmembrane growth factor receptors. Ubiquitinated TKRs are typically targeted for internalization and degradation, and USP8 appears to block this activity. Conversely, USP8 has been shown to have opposite effects on GPCR activity. Here, it accelerates ubiquitinated chemokine receptor (CXCR4) internalization and subsequent inactivation, notably through a deubiquitination-independent mechanism. Human USP8 is 1118 amino acids (aa) in length. It contains one MIT domain that mediates endosomal trafficking (aa 33-116), a rhodanese domain that binds RNF proteins (aa 184-305), an SH3 domain binding sequence (aa 405-413), and a C-terminal catalytic domain that hydrolyses ubiquitin adducts (aa 776‑1106). USP8 is phosphorylated at Ser702, 705, 784 and 787. There is one oncogenic recombination isoform that fuses the p85 beta-subunit of PI3 kinase to the C‑terminal 363 aa of USP8, beginning with Pro746. Full-length human and mouse USP8 share 82% aa sequence identity.