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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. Additionally we are shipping SMURF2 Kits (3) and SMURF2 Proteins (3) and many more products for this protein.
Showing 10 out of 72 products:
Human Polyclonal SMURF2 Primary Antibody for IF, IHC (p) - ABIN388831
Tajima, Goto, Yoshida, Shinomiya, Sekimoto, Yoneda, Miyazono, Imamura: Chromosomal region maintenance 1 (CRM1)-dependent nuclear export of Smad ubiquitin regulatory factor 1 (Smurf1) is essential for negative regulation of transforming growth factor-beta signaling by Smad7. in The Journal of biological chemistry 2003
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Human Polyclonal SMURF2 Primary Antibody for IHC (p), WB - ABIN388830
Zhang, Chang, Gehling, Hemmati-Brivanlou, Derynck: Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase. in Proceedings of the National Academy of Sciences of the United States of America 2001
Show all 5 references for 388830
Human Polyclonal SMURF2 Primary Antibody for EIA, IHC (p) - ABIN357472
Suzuki, Murakami, Fukuchi, Shimanuki, Shikauchi, Imamura, Miyazono: Smurf1 regulates the inhibitory activity of Smad7 by targeting Smad7 to the plasma membrane. in The Journal of biological chemistry 2002
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Human Polyclonal SMURF2 Primary Antibody for EIA, IHC (p) - ABIN357471
Lin, Liang, Feng: Smurf2 is a ubiquitin E3 ligase mediating proteasome-dependent degradation of Smad2 in transforming growth factor-beta signaling. in The Journal of biological chemistry 2001
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results provide the evidence that Smurf2 may play specific roles in glandular secretion, trophoblastic cell invasion, and placentation through mediating the expression of the related proteins of TGF-beta (show TGFB1 Antibodies) signaling pathway during early pregnancy
found that phospho-AIMP2 (show AIMP2 Antibodies) dissociated from the multi-tRNA synthetase complex and translocated to the nucleus, where it bound to Smurf2
Ectopic expression of human Smurf2 driven by the Col2a1 (show COL2A1 Antibodies) promoter accelerated disc degeneration in Col2a1 (show COL2A1 Antibodies)-Smurf2 transgenic mice, and that higher levels of connective tissue growth factor (show CTGF Antibodies) protein and mRNA were present in Col2a1 (show COL2A1 Antibodies)-Smurf2 transgenic discs, indicate that Smurf2 accelerates disc degeneration via upregulation of connective tissue growth factor (show CTGF Antibodies).
data suggest for the first time that the choice of binding partners for SMURF2 can sustain or repress TGFbeta (show TGFB1 Antibodies) signaling, and RNF11 (show RNF11 Antibodies) may promote TGFbeta (show TGFB1 Antibodies)-induced cell migration.
Neddylation of Smurf1 (show SMURF1 Antibodies) activates its ubiquitin ligase activity and Smurf2 exerts Nedd8 (show NEDD8 Antibodies) ligase activity. This study provided new clues of Smurf2 activation regulation.
The Smurf2 acts in a sumoylation-regulated manner to suppress TGFbeta (show TGFB1 Antibodies)-induced Epithelial-mesenchymal transition.
the findings of this study demonstrate that the downregulation of SnoN (show SKIL Antibodies) expression in hRPTECs under high-glucose conditions is mediated by the increased expression of Smurf2 through the TGF-b1/Smad (show SMAD1 Antibodies) signaling pathway.
SMURF2 is a critical target of USP15 (show USP15 Antibodies) in the TGF-beta (show TGFB1 Antibodies) signaling pathway.
Data show that miR15b mediates SMURF2 expression in pancreatic cancer and suggest miR15b as an oncogene (show RAB1A Antibodies) by promoting epithelial-mesenchymal transition and SMURF2 as a tumor suppressor gene which expression is inhibited by miR15b in pancreatic cancer.
Methylation by PRMT1 (show PRMT1 Antibodies) may regulate Smurf2 stability and control TGF-beta (show TGFB1 Antibodies) signaling.
Studies on Smurf2 and Nedd4 show that the C2 domain has the potential to regulate E3 activity by maintaining the HECT domain in a low-activity state where its ability for transthiolation and noncovalent Ubiquitin binding are impaired.
Young Smurf2-deficient mice develop milder osteoarthritis in knee articular cartilage compared to WT mice after surgical destabilization of the medial meniscus.
TAT (show TAT Antibodies) fused to WW2/WW3 of Smurf2 could interfere with TGF-beta (show TGFB1 Antibodies) signaling and reduce ArgI gene expression.
Smurf-mediated endocytosis of Patched1 (show PTCH1 Antibodies) is required in sonic hedgehog (show SHH Antibodies) signal reception
Data indicate that TNF receptor associated factor 4 (TRAF4 (show TRAF4 Antibodies)) recruited the E3-ligase SMURF2, to degrade the IL-25R-inhibitory molecule DAZ associated protein 2 (DAZAP2 (show DAZAP2 Antibodies)).
Expression of Smurf2 was increased with age and in response to regenerative stress during serial transplantation, our findings suggest that Smurf2 plays an important role in regulating HSC (show FUT1 Antibodies) self-renewal and aging.
Akt (show AKT1 Antibodies) regulates osteoblast differentiation by enhancing the protein stability and transcriptional activity of Runx2 (show RUNX2 Antibodies) through regulation of degradation of Smurf2.
that Smurf2 is an important nonredundant negative regulator of virus-triggered type I IFN signaling by targeting VISA (show MAVS Antibodies) for K48-linked ubiquitination and degradation.
Smurf2 mediates ubiquitination and degradation of YY1 (show YY1 Antibodies), a key germinal centre transcription factor.
Smurf2 deficiency increased the susceptibility of mice to spontaneous tumorigenesis, most notably B-cell lymphoma
T cell-specific DeltaE2Smurf2 degrades wild-type Smurf2 and controls intestinal tumor growth in mice by up-regulating TGF-beta receptor type II (show TGFBR2 Antibodies), reducing proliferation and production of proinflammatory cytokines.
Data demonstrate that Smurf1 (show SMURF1 Antibodies) and Smurf2 have overlapping and distinct functionalities during early frog embryogenesis; collectively, they regulate ectodermal and mesodermal induction and patterning to ensure normal development of Xenopus embryos.
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 (By similarity).
SMAD specific E3 ubiquitin protein ligase 2
, E3 ubiquitin-protein ligase SMURF2-like
, e3 ubiquitin-protein ligase SMURF2-like
, E3 ubiquitin ligase SMURF2
, E3 ubiquitin-protein ligase SMURF2
, SMAD ubiquitination regulatory factor 2
, SMAD-specific E3 ubiquitin-protein ligase 2
, E3 ubiquitin ligase Smurf2