ARIH2 Antibody

1. these findings reveal a novel mechanism of ubiquitination-dependent negative regulation of the NLRP3 inflammasome by ARIH2 and highlight ARIH2 as a potential therapeutic target for inflammatory diseases PMID: 29021376
2. We show that ARIH2 E3-ligase regulates PABPN1 protein accumulation and aggregation PMID: 24486325
3. TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin-RING ligase complexes. PMID: 24076655
4. study demonstrated that TRIAD1 is a ubiquitination target for proteasome-dependent degradation by MDM2; results suggest TRIAD1 degradation by MDM2 suppresses TRIAD1-mediated cell growth; data suggested a novel negative regulatory mechanism of TRIAD1 via MDM2 E3 ligase ubiquitination PMID: 22940738
5. TRIAD1 as a novel modulator of the p53-MDM2 axis that induces p53 activation by inhibiting its regulation by MDM2. PMID: 22819825
6. In sharp contrast to SIAH1/SIAH2 and UBCH8, TRIAD1 binding to PML-RARalpha has no effect on its turnover. PMID: 22037423
7. HoxA10 influences protein ubiquitination by activating transcription of ARIH2, the gene encoding Triad1 PMID: 21454682
8. proteasomal degradation of proteins that are ubiquitinated by Triad1 affects the clonogenic growth of primary myeloid progenitor cells PMID: 16118314
9. The fine-tuning of Gfi1 protein levels regulated by Triad1 defines an unexpected role for this protein in hematopoiesis. PMID: 17646546
10. Triad1 has dual ubiquitin ligase activity; both its RING domains are crucial for inhibiting myeloid proliferation. The N-terminal RING finger (RING1) of Triad1 binds UbcH7; the C-terminal RING finger (RING2) binds Ubc13. PMID: 19340006

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HGNC: 690

OMIM: 605615

KEGG: hsa:10425

STRING: 9606.ENSP00000348769

UniGene: Hs.633601