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The protein encoded by TRIM8 is a member of the tripartite motif (TRIM) family. De plus, nous expédions TRIM8 Anticorps (51) et beaucoup plus de produits pour cette protéine.
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TRIM8 activates STAT3 by suppressing the expression of PIAS3, an inhibitor of STAT3, most likely through E3-mediated ubiquitination and proteasomal degradation.
we provided evidence that TRIM8 and its regulators miR-17-5p and miR-106b-5 participate to a feedback loop controlling cell proliferation through the reciprocal modulation of p53, miR-34a and N-MYC.
A pathogenic effect of a heterozygous truncating mutation in the tripartite motif containing 8 (TRIM8) gene on the postnatal development of the human brain.
Our study provides evidences that TRIM8 may participate in the carcinogenesis and progression of glioma and that the transcriptional repression of TRIM8 might have potential value for predicting poor prognosis in glioma patients.
These findings provide the first mechanistic link between TRIM8 and the drug resistance of clear cell Renal Cell Carcinoma
Nucleo-cytoplasmic trafficking of TRIM8, a novel oncogene, is involved in positive regulation of TNF induced NF-kappaB pathway.
TRIM8 is a p53 direct target gene that induces p53 stabilization and promotes the degradation of MDM2 protein.
Tripartite motif 8 (TRIM8) modulates TNFalpha- and IL-1beta-triggered NF-kappaB activation by targeting TAK1 for K63-linked polyubiquitination.
TRIM8 modulates translocation of phosphorylated STAT3 into the nucleus through interaction with Hsp90beta and consequently regulates transcription of Nanog in embryonic stem cells.
These findings indicate that TRIM8 enhances the STAT3-dependent signal pathway by inhibiting the function of PIAS3.
interacts with SOCS-1
Gerp transcribes interferon-gamma in epithelial and lymphoid cells and is expressed almost ubiquitously in tissues.
Among genes correlated to nodal metastatic progression, we verified in vitro that NM23-H3 reduced cell motility and TRIM8 were a growth suppressor.
these studies reveal an additional regulatory function of TRIM8 in innate immune responses: TRIM8 catalyzes polyubiquitination of TRIF, resulting in disruption of TRIF-TBK1 interaction
TRIM8 plays a deleterious role in pressure overload-induced cardiac hypertrophy by accelerating the activation of TAK1-dependent signaling pathways.
potent regulator that exacerbates steatohepatitis and metabolic disorders dependent on its binding and ubiquitinating capacity on transforming growth factor-beta-activated kinase 1
TRIM8 has pro-inflammatory effect on Pseudomonas aeruginosa -induced keratitis
The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein localizes to nuclear bodies. Its structure is similar to some tumor suppressor proteins and its gene maps to a locus thought to contain tumor suppressor genes.
glioblastoma expressed ring finger protein
, glioblastoma-expressed RING finger protein
, probable E3 ubiquitin-protein ligase TRIM8
, ring finger protein 27
, tripartite motif protein TRIM8
, tripartite motif-containing 8
, tripartite motif-containing protein 8
, tripartite motif protein 8