Anti-SMURF2 Antibody Picoband® Fluoro647 Conjugated

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.

E3 ubiquitin-protein ligase SMURF2; hSMURF2; HECT-type E3 ubiquitin transferase SMURF2; SMAD ubiquitination regulatory factor 2; SMAD-specific E3 ubiquitin-protein ligase 2; SMURF2

E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then ly 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.

1. Entrez Gene: SMURF2 SMAD specific E3 ubiquitin protein ligase 2. 2. Blank, M., Tang, Y., Yamashita, M., Burkett, S. S., Cheng, S. Y., Zhang, Y. E. A tumor suppressor function of Smurf2 associated with controlling chromatin landscape and genome stability through RNF20. Nature Med. 18: 227-234, 2012. 3. Lin X, Liang M, Feng XH (Nov 2000) . Smurf2 is a ubiquitin E3 ligase mediating proteasome-dependent degradation of Smad2 in transforming growth factor-beta signaling. The Journal of Biological Chemistry 275 (47) : 36818–22.