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DR1 encodes a TBP- (TATA box-binding protein) associated phosphoprotein that represses both basal and activated levels of transcription. Additionally we are shipping DR1 Antibodies (61) and many more products for this protein.
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Mot1, Ino80 chromatin remodeling complex (Ino80C (show INO80C Proteins)), and NC2 (show GTF2H5 Proteins) co-localize on chromatin and coordinately suppress pervasive transcription in murine embryonic stem cells.
results suggest that DR1 are expressed in the osteosarcoma cells and inhibit the proliferation of osteosarcoma cells by the down-regulation of the ERK1/2 and PI3K (show PIK3CA Proteins)-Akt (show AKT1 Proteins) pathways.
Knockdown of DR1 resulted in reductions of viral RNA and protein production, demonstrating that DR1 acts as a positive host factor in influenza A virus replication.
The physiological functions of human Dr1 include regulation of polymerase III transcription.
NC2 (show GTF2H5 Proteins) controls TBP (show TBP Proteins) binding and maintenance on DNA that is largely independent of a canonical TATA sequence
the initiator core promoter element antagonizes repression of TATA-directed transcription by negative cofactor NC2 (show GTF2H5 Proteins)
Data show that NC2beta is specifically involved in neuroblastoma (show ARHGEF16 Proteins) pathogenesis and may be considered a new neuroblastoma (show ARHGEF16 Proteins) biomarker.
ATAC Is a GCN5/PCAF-containing acetylase complex with a novel NC2-like histone fold module that interacts with the TATA-binding protein
heterodimerization with NC2alpha masks the nuclear localization signal in NC2beta, which prevents nuclear export of the NC2 (show GTF2H5 Proteins) complex
This gene encodes a TBP- (TATA box-binding protein) associated phosphoprotein that represses both basal and activated levels of transcription. The encoded protein is phosphorylated in vivo and this phosphorylation affects its interaction with TBP. This protein contains a histone fold motif at the amino terminus, a TBP-binding domain, and a glutamine- and alanine-rich region. The binding of DR1 repressor complexes to TBP-promoter complexes may establish a mechanism in which an altered DNA conformation, together with the formation of higher order complexes, inhibits the assembly of the preinitiation complex and controls the rate of RNA polymerase II transcription.
, TATA-BINDING PROTEIN-ASSOCIATED PHOSPHOPROTEIN
, TATA-binding protein-associated phosphoprotein
, protein Dr1
, negative cofactor 2-beta