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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 WWP1 Antibodies (28) and many more products for this protein.
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Overexpression of WWP1 promotes tumorigenesis in patients with hepatocellular carcinoma.
PTPN14, a Pez mammalian homolog, is degraded by overexpressed Su(dx) or Su(dx) homologue WWP1 in mammalian cells.
miR (show MLXIP Proteins)-21 overexpression or WWP1 knockdown in endothelial progenitor cells significantly activates the TGFbeta (show TGFB1 Proteins) signaling pathway and inhibits cell proliferation.
The cancer-driven alteration of WWP1 culminates in excessive TbetaRI (show TGFBR1 Proteins) degradation and attenuated TGFbeta1 (show TGFB1 Proteins) cytostatic signaling, a consequence that could conceivably confer tumorigenic properties to WWP1.
Results suggest that elevated transcription and expression levels of ubiquitin ligase E3s WWP1, Smurf1 (show SMURF1 Proteins) and Smurf2 (show SMURF2 Proteins) genes may be the mechanisms of occurrence, development and metastasis of prostate cancer.
Most notably, WWP1 downregulation both inactivated PTEN-Akt (show AKT1 Proteins) signaling pathway in MKN-45 and AGS (show JAG1 Proteins) cells. our findings suggest that WWP1 acts as an oncogenic factor and should be considered as a novel interfering molecular target for gastric carcinoma
Data show that WWP1, which specifically ubiquitinates and degrades DeltaNp73 heterodimerizes with another E3 ligase, WWP2 (show WWP2 Proteins).
Knocking down WWP1 promoted cleaved caspase3 protein and p53 (show TP53 Proteins) expression in hepatocellular carcinoma cells, and caspase3 inhibition could prevent cell apoptosis induced by the knockdown of WWP1.
results reveal that WWP1 might play an oncogenic role in oral cancer cells.
LATS1 is critical in mediating WWP1-induced increased cell proliferation in breast cancer cells.
Cardiomyocyte-specific overexpression of Wwp1 contributes to reduction in Connexin 43 (show GJA1 Proteins) and arrhythmogenesis.
Wwp1 negatively regulates osteoblast functions.
WWP1 functions as an E3 ligase when cells are stimulated with LPS (show TLR4 Proteins) by binding to TRAF6 (show TRAF6 Proteins) and promoting K48-linked polyubiquitination. This results in the proteasomal degradation of TRAF6 (show TRAF6 Proteins)
WWP1 down-regulates AMPKalpha2 under high glucose culture conditions via the ubiquitin-proteasome pathway
Wwp1 promotes ubiquitination and degradation of JunB (show JUNB Proteins), an AP-1 (show JUN Proteins) transcription factor that positively regulates osteoblast differentiation.
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. Ubiquitinates ERBB4 isoforms JM-A CYT-1 and JM-B CYT-1, KLF2, KLF5 and TP63 and promotes their proteasomal degradation. Ubiquitinates RNF11 without targeting it for degradation. Ubiquitinates and promotes degradation of TGFBR1\; the ubiquitination is enhanced by SMAD7. Ubiquitinates SMAD6 and SMAD7. Ubiquitinates and promotes degradation of SMAD2 in response to TGF-beta signaling, which requires interaction with TGIF.
E3 ubiquitin ligase SMURF1
, E3 ubiquitin-protein ligase SMURF1
, WW domain containing E3 ubiquitin protein ligase 1
, smad ubiquitination regulatory factor 1
, WW domain-containing protein 1
, NEDD4-like E3 ubiquitin-protein ligase WWP1
, Nedd-4-like ubiquitin-protein ligase
, TGIF-interacting ubiquitin ligase 1
, atrophin-1 interacting protein 5
, atrophin-1-interacting protein 5