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RNF7 gene variant is associated with the risk of developing liver fibrosis and cirrhosis in an Eastern European population.
MAF1 (show MAF1 Proteins), RNF7 and SETD3 (show SETD3 Proteins) are identified as PCNA (show PCNA Proteins)-associated proteins in human cells and given this interaction with PCNA (show PCNA Proteins), Maf1 (show MAF1 Proteins), RNF7, and SetD3 (show SETD3 Proteins) are potentially involved in DNA replication, DNA repair, or associated processes.
These findings indicate that Rbx1 and Rbx2 can both activate Cul5 (show CUL5 Proteins)-Vif (show BTG1 Proteins) E3 ligase in vitro, but they may undergo a more delicate selection mechanism in vivo.
SAG (show DMBT1 Proteins) plays an important role in regulating ionizing radiation-induced apoptosis
The findings showed that SAG (show DMBT1 Proteins) E3 ubiquitin ligase (show MUL1 Proteins) plays an essential role in cancer cell proliferation and tumor growth
SAG (show DMBT1 Proteins) possesses a potent peroxidase property to decompose hydrogen peroxide in the presence of dithiothreitol
sensitive to apoptosis gene protein inhibits peroxynitrite-induced DNA damage.
results indicate that protein kinase (show CDK7 Proteins) CKII (show CSNK2A1 Proteins) may control IkappaBalpha (show NFKBIA Proteins) and p27Kip1 (show CDKN1B Proteins) degradation and thereby G1/S phase transition through the phosphorylation of threonine 10 within CKBBP1 protein
These studies suggested that CK2 (show CSNK2A1 Proteins) might regulate SAG (show DMBT1 Proteins)-SCF (show KITLG Proteins) E3 ligase activity through modulating SAG's stability, rather than its enzymatic activity directly.
Endogenous levels of pro-caspase 3 (show CASP3 Proteins) were decreased by overexpression of SAG (show DMBT1 Proteins) protein.
SAG is a novel molecular target that regulates T-cell responses and that inhibiting neddylation with the clinically available small-molecule MLN4924 may represent a novel strategy to mitigate T-cell-mediated immunopathologies, such as graft-versus-host disease.
Attenuation of SAG expression, exacerbates 4-hydroxy-2-nonenal-induced apoptosis and hypertrophy via a disruption of the cellular redox balance.
Inactivation of Sag/Rbx2/Roc2 e3 ubiquitin ligase triggers senescence and inhibits kras-induced immortalization.
as a novel substrate of SAG-betaTrCP (show BTRC Proteins) E3 ligase. By degrading Erbin (show ERBB2IP Proteins) and Nrf2 (show NFE2L2 Proteins), Sag activates the Ras-Raf (show RAF1 Proteins) pathway and causes ROS (show ROS1 Proteins) accumulation to trigger autophagy and senescence
Sag is a Kras-cooperating oncogene (show RAB1A Proteins) that promotes lung tumorigenesis
identifies NF1 as a physiological substrate of SAG-CUL1-FBXW7 E3 ligase and establishes a ubiquitin-dependent regulatory mechanism for the NF1-RAS pathway during embryogenesis
Thus, we concluded that SAG is a cellular protective molecule, which appears to function as an antioxidant, suppressing MPP(+)-induced neurotoxicity.
SAG accelerates ultraviolet B-induced skin hyperplasia, but not carcinogenesis.
The protein encoded by this gene is a highly conserved ring finger protein. It is an essential subunit of SKP1-cullin/CDC53-F box protein ubiquitin ligases, which are a part of the protein degradation machinery important for cell cycle progression and signal transduction. This protein interacts with, and is a substrate of, casein kinase II (CSNK2A1/CKII). The phosphorylation of this protein by CSNK2A1 has been shown to promote the degradation of IkappaBalpha (CHUK/IKK-alpha/IKBKA) and p27Kip1(CDKN1B). Alternatively spliced transcript variants encoding distinct isoforms have been reported.
CKII beta-binding protein 1
, RING-box protein 2
, regulator of cullins 2
, sensitive to apoptosis gene protein
, sensitive to apoptosis, zinc RING finger protein SAG, regulator of cullins 2
, zinc RING finger protein SAG