Anti-SMURF2 Antibody

SMURF2 (SMAD ubiquitin regulatory factor 2) is a negative regulator of TGF-beta signaling (1) . SMURF1 and SMURF2 are members of HECT domain E3 ubiquitin ligase which are involved in the enzymatic reactions of the Ub conjugating pathway (1,2) . SMURF2 is widely expressed and was initially identified as an inhibitor of TGF-beta/BMP signaling by targeting R-Smads and TGF type I receptor for ubiquitination and degradation (3) . Studies have shown that SMURF2 functions as a tumor suppressor by maintaining genomic stability through targeting RNF20 (3) . SMURF2 associates constitutively with SMAD7 (4) .

SMURF2 antibody was raised against a 17 amino acid peptide near the amino terminus of human SMURF2. The immunogen is located within amino acids 140 - 190 of SMURF2.

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.