|Reactivity||Human, Mouse, Rat|
|Calculated MW||79542 Da|
|Positive Control||Western blot: 3T3 cell lysate|
|Application & Usage||Western blot: 1:200|
|Other Names||Bromodomain containing 3, isoform CRA_b, ORFX; RING3L; Bromodomain containing protein 3; RING3-like protein|
|Formulation||100 µg (0.5 mg/ml) of antibody in PBS, 0.01 % BSA, 0.01 % thimerosal, and 50 % glycerol, pH 7.2|
|Handling||The antibody solution should be gently mixed before use.|
|Reconstitution & Storage||-20 °C|
|Precautions||BRD3 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Binds hyperacetylated chromatin and plays a role in the regulation of transcription, probably by chromatin remodeling and interaction with transcription factors. Regulates transcription by promoting the binding of the transcription factor GATA1 to its targets (By similarity). Regulates transcription of the CCND1 gene.|
|Cellular Location||Nucleus. Note=Detected on chromatin.|
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Provided below are standard protocols that you may find useful for product applications.
The acetylation of histone lysine residues plays a crucial role in the epigenetic regulation of gene transcription. A bromodomain is a protein domain that recognizes acetylated lysine residues such as those on the N-terminal tails of histones. This recognition is often a prerequisite for protein-histone association and chromatin remodeling. These domains function in the linking of protein complexes to acetylated nucleosomes, thereby controlling chromatin structure and gene expression. Thus, bromodomains serve as “readers” of histone acetylation marks regulating the transcription of target promoters. The BET family of proteins, defined by tandem Bromodomains and an Extra Terminal domain, include BRD2, BRD3, BRD4, and BRDT. The BET proteins play a key role in many cellular processes, including inflammatory gene expression, mitosis, and viral/host interactions. The isolated individual or tandem bromodomains of BRD3 have been shown to bind acetylated histone tails, serving to couple histone acetylation marks to the transcriptional regulation of target promoters. Small molecule inhibitors of these interactions hold promise as useful therapeutics for human disease.
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