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Functions as a bridging factor between STAT6 and the basal transcription factor. Additionally we are shipping SND1 Antibodies (66) and SND1 Kits (7) and many more products for this protein.
Showing 5 out of 6 products:
The data suggested that JNK (show MAPK8 Proteins)-enhanced Tudor-SN phosphorylation promotes the interaction between Tudor-SN and G3BP (show G3BP1 Proteins) and facilitates the efficient recruitment of Tudor-SN into stress granules under conditions of sodium arsenite-induced oxidative stress.
SND1 physically associated with and recruited the histone acetylase GCN5 (show KAT2A Proteins) to the promoter regions of Smad2 (show SMAD2 Proteins)/3/4, and consequently enhanced the gene transcriptional activation of Smad2 (show SMAD2 Proteins)/3/4, which are essential downstream regulators in the TGFbeta1 (show TGFB1 Proteins) pathway.
Our work establishes an oncogenic role for SND1 in promoting tumor-initiating cell formation in hepatocellular carcinoma
Findings indicate the potential values of microRNA miR (show MLXIP Proteins)-320a, staphylococcal nuclease domain-containing 1 (SND1) and beta-catenin (show CTNNB1 Proteins) as prognostic biomarkers and therapeutic candidates for malignant gliomas.
These results highlight SND1 as a potential regulator of cellular cholesterol distribution and homeostasis in hepatoma cells, and support the rationale for the therapeutic use of molecules that influence cholesterol management when SND1 is overexpressed.
This study unravels a novel mechanism of SND1 function and identifies MGLL (show MGLL Proteins) as a unique tumor suppressor for HCC (show FAM126A Proteins). MGLL (show MGLL Proteins) might function as a homeostatic regulator of Akt (show AKT1 Proteins) restraining its activation.
SND1 is a determinant downstream effector of TNFalpha (show TNF Proteins) that contributes to support glycerophospholipid homeostasis in human hepatocellular carcinoma during inflammation.
it could be concluded that miR (show MLXIP Proteins)-361-5p functions as a tumor-suppressive miRNA through directly binding to SND1
we identified a new SND1-BRAF fusion that appeared to be present in a subpopulation of tumor cells.
Study is the first to show a novel regulatory role of SND1, a direct target of miR (show MLXIP Proteins)-184, in glioma progression, suggesting that the miR (show MLXIP Proteins)-184/SND1 axis may be a useful diagnostic and therapeutic tool for malignant glioma.
Tudor-SN is a potential substrate of G1/S phase Cyclin (show PCNA Proteins)-Dependent Kinases, and promotes cell cycle progression by facilitating E2F-1 (show E2F1 Proteins)-mediated gene transcription.
MTDH (show MTDH Proteins) supports the survival of mammary epithelial cells under oncogenic/stress conditions by interacting with and stabilizing SND1.
Tudor-SN and PPARgamma (show PPARG Proteins) are both regulated by C/EBPbeta (show CEBPB Proteins) during adipogenesis and significantly influence the regulation of PPARgamma (show PPARG Proteins) target genes.
p100 (show PATL2 Proteins) regulates the binding activity of RelB (show RELB Proteins)/p50 (show LSP1 Proteins) dimers via at least two distinct mechanisms depending on the signaling pathway involved.
Two alternative transcripts of p100 are expressed during embryogenesis and regulated by Nodal signaling.
Functions as a bridging factor between STAT6 and the basal transcription factor. Plays a role in PIM1 regulation of MYB activity. Plays a role in cell viability. Functions as a transcriptional coactivator for STAT5. Plays a role in cell viability (By similarity).
EBNA-2 co-activator (100kD)
, 100 kDa coactivator
, EBNA2 coactivator p100
, SND1-BRAF fusion
, p100 EBNA2 co-activator
, p100 co-activator
, staphylococcal nuclease domain containing 1
, staphylococcal nuclease domain-containing protein 1
, tudor domain-containing protein 11
, p105 coactivator
, staphylococcal nuclease and tudor domain containing 1
, 4SNc-Tudor domain protein