Anti-Human WWP1 Antibody Pair

Product Description: NEDD4-like E3 ubiquitin-protein ligase WWP1 (WWP1) is a member of the HECT (Homologous to the E6-AP Carboxyl Terminus) family of E3 ubiquitin ligases, characterized by an N-terminal C2 domain, four WW domains, and a C-terminal HECT domain. This protein plays a crucial role in regulating various cellular processes, including protein degradation, signal transduction, and cellular proliferation through ubiquitination of target proteins. Dysregulation of WWP1 has been implicated in several diseases, particularly cancers such as breast, prostate, and colorectal cancer, where it can function as an oncogene by promoting tumor growth and survival. Additionally, mutations in WWP1 are associated with Cowden syndrome and Cowden-like syndrome, which increase the risk of developing multiple tumors due to impaired PTEN tumor suppressor activity. Protein Function: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Ubiquitinates ERBB4 isoforms JM-A CYT-1 and JM-B CYT-1, KLF2, KLF5 and TP63 and promotes their proteasomal degradation. Ubiquitinates RNF11 without targeting it for degradation. Ubiquitinates and promotes degradation of TGFBR1, the ubiquitination is enhanced by SMAD7. Ubiquitinates SMAD6 and SMAD7. Ubiquitinates and promotes degradation of SMAD2 in response to TGF-beta signaling, which requires interaction with TGIF. Activates the Hippo signaling pathway in response to cell contact inhibition and recruitment to the Crumbs complex at the cell membrane (PubMed:34404733). Monoubiquitinates AMOTL2 which facilitates its interaction with and activation of LATS2 (PubMed:34404733). LATS2 then phosphorylates YAP1, excluding it from the nucleus and therefore ultimately represses YAP1-driven transcription of target genes (PubMed:34404733) [The Uniprot Consortium]