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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. Zusätzlich bieten wir Ihnen WWP1 Proteine (3) und viele weitere Produktgruppen zu diesem Protein an.
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Human Monoclonal WWP1 Primary Antibody für 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
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Human Monoclonal WWP1 Primary Antibody für 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
Results show that WWP1 is frequently upregulated in gastric cancer (GC) tissues and cells, and that its 3'-UTR (zeige UTS2R Antikörper) is a putative target of miR (zeige MLXIP Antikörper)-584 which suppresses its protein expression by mRNA degradation.
study describes a physical and functional interaction between Ebola virus VP40 (eVP40) and WWP1, a host E3 ubiquitin ligase (zeige MUL1 Antikörper) 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 (zeige FLVCR1 Antikörper)) clinical specimens and contributed to cancer cell invasion, indicating that this target of Mir (zeige MLXIP Antikörper)-452 functioned as an oncogene (zeige RAB1A Antikörper).
Overexpression of WWP1 promotes tumorigenesis in patients with hepatocellular carcinoma.
PTPN14 (zeige PTPN14 Antikörper), a Pez (zeige PTPN14 Antikörper) mammalian homolog, is degraded by overexpressed Su(dx) or Su(dx) homologue WWP1 in mammalian cells.
miR (zeige MLXIP Antikörper)-21 overexpression or WWP1 knockdown in endothelial progenitor cells significantly activates the TGFbeta (zeige TGFB1 Antikörper) signaling pathway and inhibits cell proliferation.
The cancer-driven alteration of WWP1 culminates in excessive TbetaRI (zeige TGFBR1 Antikörper) degradation and attenuated TGFbeta1 (zeige TGFB1 Antikörper) cytostatic signaling, a consequence that could conceivably confer tumorigenic properties to WWP1.
Atypical ubiquitination by E3 ligase WWP1 inhibits the proteasome-mediated degradation of mutant huntingtin (zeige HTT Antikörper). 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 (zeige GJA1 Antikörper) and arrhythmogenesis.
Wwp1 negatively regulates osteoblast functions.
WWP1 functions as an E3 ligase when cells are stimulated with LPS (zeige TLR4 Antikörper) by binding to TRAF6 (zeige TRAF6 Antikörper) and promoting K48-linked polyubiquitination. This results in the proteasomal degradation of TRAF6 (zeige TRAF6 Antikörper)
WWP1 down-regulates AMPKalpha2 under high glucose culture conditions via the ubiquitin-proteasome pathway
Wwp1 promotes ubiquitination and degradation of JunB (zeige JUNB Antikörper), an AP-1 (zeige JUN Antikörper) 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