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conclude that BRD3/4 and the FLT3 (show FLT3 Proteins)-TAK1 (show MAP3K7 Proteins)/NF-kB pathways collectively control a set of targets that are critically important for the survival of human MLL (show MLL Proteins)-AF9 (show MLLT3 Proteins) cells
The bromodomain and extraterminal domain (BET) family consists of BRDT (show BRDT Proteins), BRD2 (show BRD2 Proteins), BRD3, and BRD4 (show BRD4 Proteins), each containing 2 bromodomains located N-terminal to extraterminal domain, which is located near C-terminus. Data suggest that 10 distinct acylations participate in binding of BET family proteins to histone 4 (oligopeptide fragments used here); C-terminal bromodomains do not cooperatively bind multiple acylation sites.
Ewing sarcoma may be susceptible to treatment with epigenetic inhibitors blocking BRD3/4 activity and the associated pathognomonic EWS (show EWSR1 Proteins)-FLT1 (show FLT1 Proteins) transcriptional program.
An isoform of BRD3, BRD3R (BRD3 with Reprogramming activity) is a reprogramming factor.
Here, we identify NCT, a complex comprising the Nrc1 BET-family tandem bromodomain protein (SPAC631.02), casein kinase II (CKII), and several TAFs, as a regulator of condensin function.
BRD2 (show BRD2 Proteins), BRD3, and BRD4 (show BRD4 Proteins) interact with gammaretroviral INs (show INS Proteins) and serve as cofactors for murine leukemia virus integration.
The BRDT (show BRDT Proteins) gene was not expressed in testicular tissue from patients with Sertoli cells only, whereas the other three genes of the BET family retained expression in all the sperm pathologies.
the structural basis for GATA1 (show GATA1 Proteins) and Brd3 interaction was described.
BRD-NUT fusion proteins contribute to carcinogenesis by associating with chromatin and interfering with epithelial differentiation.
Results report that the double bromodomain proteins Brd2 (show BRD2 Proteins) and Brd3 associate preferentially in vivo with hyperacetylated chromatin along the entire lengths of transcribed genes.
Brd3 knockout significantly decreased the recruitment of acetylase CBP (show CREBBP Proteins) to IL6 (show IL6 Proteins) gene promoter, and the acetylation level of histone3 within IL6 (show IL6 Proteins) gene promoter was repressed.
Data show that infection of macrophages with Listeria monocytogenes caused binding of the BET proteins Brd2, Brd3, and, most prominently, Brd4 to the Nos2 promoter.
Brd3 associates with acetylated GATA1 (show GATA1 Proteins) to promote its chromatin occupancy at erythroid target genes
A conserved but uncharacterized gene encoding Brd3, which was down-regulated during endothelial differentiation, was identified.
This gene was identified based on its homology to the gene encoding the RING3 protein, a serine/threonine kinase. The gene localizes to 9q34, a region which contains several major histocompatibility complex (MHC) genes. The function of the encoded protein is not known.
bromodomain containing 3
, bromodomain containing protein 3
, bromodomain-containing protein 3-like
, RING3-like protein
, bromodomain-containing 3
, bromodomain-containing protein 3
, bromodomain-containing FSH-like protein FSRG2