|Other Names||E3 ubiquitin-protein ligase SMURF2, hSMURF2, 632-, SMAD ubiquitination regulatory factor 2, SMAD-specific E3 ubiquitin-protein ligase 2, SMURF2|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP2105a was selected from the N-term region of human SMURF2 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|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.|
|Cellular Location||Nucleus. Cytoplasm. Cell membrane. Membrane raft. Note=Cytoplasmic in the presence of SMAD7. Colocalizes with CAV1, SMAD7 and TGF-beta receptor in membrane rafts|
|Tissue Location||Widely expressed.|
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Provided below are standard protocols that you may find useful for product applications.
SMURF2, a 748-amino acid ubiquitin E3 ligase that is 83% identical to SMURF1, codes for a C2-WW-HECT domain ubiquitin ligase that associates constitutively with SMAD7. Binding to SMAD7 induces export of SMURF2 and recruitment to the activated transforming growth factor-beta receptor (TGFBR), where it causes receptor and SMAD7 degradation. A strong interaction of second and third SMURF2 WW domains has been identified with SMAD1, SMAD2, and SMAD3, but not SMAD4. Western blot analysis showed that SMURF2 selectively downregulates the transcription of SMAD2 and SMAD1, but not SMAD3. The nuclear SMURF2/phosphorylated SMAD2 interaction is requires TGFB1.
Zhang, Y., et al., Proc. Natl. Acad. Sci. U.S.A. 98(3):974-979 (2001).Kavsak, P., et al., Mol. Cell 6(6):1365-1375 (2000).Lin, X., et al., J. Biol. Chem. 275(47):36818-36822 (2000).
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