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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 Antibodies (66) and and many more products for this protein.
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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 Proteins) signaling pathway during early pregnancy
the findings of this study demonstrate that the downregulation of SnoN (show SKIL Proteins) expression in hRPTECs under high-glucose conditions is mediated by the increased expression of Smurf2 through the TGF-b1/Smad (show SMAD1 Proteins) signaling pathway.
SMURF2 is a critical target of USP15 (show USP15 Proteins) in the TGF-beta (show TGFB1 Proteins) signaling pathway.
Data show that miR15b mediates SMURF2 expression in pancreatic cancer and suggest miR15b as an oncogene (show RAB1A Proteins) 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 Proteins) may regulate Smurf2 stability and control TGF-beta (show TGFB1 Proteins) 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.
Results suggest that elevated transcription and expression levels of ubiquitin ligase E3s WWP1 (show WWP1 Proteins), Smurf1 (show SMURF1 Proteins) and Smurf2 genes may be the mechanisms of occurrence, development and metastasis of prostate cancer.
miR (show MLXIP Proteins)-424 regulates the myofibroblast differentiation during epithelial-to-mesenchymal transition by potentiating the TGF-beta (show TGFB1 Proteins) signaling pathway, likely through Smurf2.
The SMURF2:UBCH5 complex is critical in maintaining KRAS protein stability.
These results suggest a novel regulatory mechanism for YY1 (show YY1 Proteins) function by Smurf2.
Provide evidence of posttranscriptional downregulation of Smurf2 in triple-negative breast cancers, and demonstrate that the loss of RB function is involved in microRNA-mediated interference with Smurf2 translation.
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 Proteins) fused to WW2/WW3 of Smurf2 could interfere with TGF-beta (show TGFB1 Proteins) signaling and reduce ArgI gene expression.
Smurf-mediated endocytosis of Patched1 (show PTCH1 Proteins) is required in sonic hedgehog (show SHH Proteins) signal reception
Data indicate that TNF receptor associated factor 4 (TRAF4 (show TRAF4 Proteins)) recruited the E3-ligase SMURF2, to degrade the IL-25R-inhibitory molecule DAZ associated protein 2 (DAZAP2 (show DAZAP2 Proteins)).
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 Proteins) self-renewal and aging.
Akt (show AKT1 Proteins) regulates osteoblast differentiation by enhancing the protein stability and transcriptional activity of Runx2 (show RUNX2 Proteins) 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 Proteins) for K48-linked ubiquitination and degradation.
Smurf2 mediates ubiquitination and degradation of YY1 (show YY1 Proteins), 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 Proteins), reducing proliferation and production of proinflammatory cytokines.
Data demonstrate that Smurf1 (show SMURF1 Proteins) 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