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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 Proteins (3) and many more products for this protein.
Showing 10 out of 28 products:
Human Monoclonal WWP1 Primary Antibody for IF, IHC (p) - ABIN564794
Edwards, Clowes, Tsang, Connell, Sanderson, Luzio, Reid: Endogenous spartin (SPG20) is recruited to endosomes and lipid droplets and interacts with the ubiquitin E3 ligases AIP4 and AIP5. in The Biochemical journal 2009
Show all 6 Pubmed References
Human Monoclonal WWP1 Primary Antibody for ELISA, WB - ABIN524447
Subik, Shu, Wu, Liang, Hicks, Boyce, Schiffhauer, Chen, Chen, Tang, Xing: The ubiquitin E3 ligase WWP1 decreases CXCL12-mediated MDA231 breast cancer cell migration and bone metastasis. in Bone 2012
study describes a physical and functional interaction between Ebola virus VP40 (eVP40) and WWP1, a host E3 ubiquitin ligase (show MUL1 Antibodies) that ubiquitinates VP40 and regulates virus-like particles egress.
Knock-down of WWP1 abrogates DNA damage-induced down-regulation of DeltaNp63alphaand partially rescues cell apoptosis
Describe an autoinhibitory mechanism for WWP1 ubiquitin ligase involving a linker-HECT domain interaction. This intramolecular interaction traps the HECT enzyme in its inactive state and can be relieved by linker phosphorylation.
results demonstrate that WWP1 catalyzes the formation of Ub chains through a sequential addition mechanism, in which Ub monomers are transferred in a successive fashion to the substrate, and that ubiquitination by WWP1 requires the presence of a low-affinity, noncovalent Ub-binding site within the HECT domain.
Study shows that WWP1 was upregulated in prostate cancer (PCa (show FLVCR1 Antibodies)) clinical specimens and contributed to cancer cell invasion, indicating that this target of Mir (show MLXIP Antibodies)-452 functioned as an oncogene (show RAB1A Antibodies).
Overexpression of WWP1 promotes tumorigenesis in patients with hepatocellular carcinoma.
PTPN14 (show PTPN14 Antibodies), a Pez (show PTPN14 Antibodies) mammalian homolog, is degraded by overexpressed Su(dx) or Su(dx) homologue WWP1 in mammalian cells.
miR (show MLXIP Antibodies)-21 overexpression or WWP1 knockdown in endothelial progenitor cells significantly activates the TGFbeta (show TGFB1 Antibodies) signaling pathway and inhibits cell proliferation.
The cancer-driven alteration of WWP1 culminates in excessive TbetaRI (show TGFBR1 Antibodies) degradation and attenuated TGFbeta1 (show TGFB1 Antibodies) 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 Antibodies) and Smurf2 (show SMURF2 Antibodies) genes may be the mechanisms of occurrence, development and metastasis of prostate cancer.
Atypical ubiquitination by E3 ligase WWP1 inhibits the proteasome-mediated degradation of mutant huntingtin (show HTT Antibodies). This suggests that the E3 ligase WWP1 is involved in the pathogenesis of Huntington's disease; therefore, it may be a novel target for therapeutic intervention.
Cardiomyocyte-specific overexpression of Wwp1 contributes to reduction in Connexin 43 (show GJA1 Antibodies) and arrhythmogenesis.
Wwp1 negatively regulates osteoblast functions.
WWP1 functions as an E3 ligase when cells are stimulated with LPS (show TLR4 Antibodies) by binding to TRAF6 (show TRAF6 Antibodies) and promoting K48-linked polyubiquitination. This results in the proteasomal degradation of TRAF6 (show TRAF6 Antibodies)
WWP1 down-regulates AMPKalpha2 under high glucose culture conditions via the ubiquitin-proteasome pathway
Wwp1 promotes ubiquitination and degradation of JunB (show JUNB Antibodies), an AP-1 (show JUN Antibodies) 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