Anti-SMURF2

0.5mg/ml if reconstituted with 0.2ml sterile DI water. E3 ubiquitin-protein ligase SMURF2 is an enzyme that in humans is encoded by the SMURF2 gene. The SMURF2 gene is mapped to chromosome 17q22-q23 based on sequence similarity between the SMURF2 sequence and a genomic contig. SMURF2 is a HECT domain E3 ubiquitin ligase involved in degradation of SMADs, TGF-beta receptor (TGFBR), and other substrates. It also functions in regulation of neuronal and planar cell polarity, induction of senescence, and tumor suppression 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. Interacts with SMAD1 and SMAD7 in order to trigger their ubiquitination and proteasome-dependent degradation. In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with SCYE1. Forms a stable complex with the TGF-beta receptor-mediated phosphorylated SMAD2 and SMAD3. In this way, SMAD2 may recruit substrates, such as SNON, for ubiquitin-mediated degradation. Enhances the inhibitory activity of SMAD7 and reduces the transcriptional activity of SMAD2. Coexpression of SMURF2 with SMAD1 results in considerable decrease in steady-state level of SMAD1 protein and a smaller decrease of SMAD2 level. [The UniProt Consortium]