Bromodomain-containing protein 4 (BRD4) belongs to the bromodomain and extra-terminal (BET) family. The protein has two bromodomains (BD1 and BD2) connected by a long interdomain linker.
Immunogen
The epitope recognized by PLA0227 maps to a region between residue 1312 and 1362 of human bromodomain-containing protein 4 using the numbering given in entry NP_490597.1 (GeneID 23476).
Biochem/physiol Actions
Bromodomain-containing protein 4 (BRD4) works as a reader of epigenetic marks and is involved in chromatin remodeling and transcriptional regulation. Therefore, it is a target for oncology, inflammation and cardiovascular disease. This gene is upregulated in hepatocellular carcinoma and is associated with poor prognosis. BRD4 is also associated with melanoma, hepatocellular carcinoma, multiple myeloma, Burkitt′s lymphoma, acute myeloid leukemia and breast cancer. BRD4 connects cell cycle and transcription, works as a scaffold for transcription factors and bookmarks active genes during mitosis. It interacts with acetylated histone-3 and histone-4 tails and helps in maintaining chromatin architecture. Also, it regulates transcription elongation via phosphorylation of RNA polymerase II.
Physical form
Tris-citrate/phosphate buffer, pH 7 to 8 containing 0.09% Sodium Azide
Other Notes
Bromodomain-containing protein 4 (BRD4) contains 2 bromo-domains. Bromo-domains are found in chromatin-associating proteins and can interact specifically with acetylated lysine. BRD4 is described as a chromatin adaptor and has been shown to bind acetylated chromatin. It was originally identified as MCAP (mitotic chromosome associated protein) due to its association with mitotic chromosomes. BRD4 also associates with several transcription complexes such as the Mediator complexes and P-TEFb complexes and is considered to function as a transcriptional co-factor.
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Cell death & disease, 14(11), 760-760 (2023-11-23)
Lipid metabolism is the key to ferroptosis susceptibility. However, little is known about the underlying mechanisms in osteosarcoma cells. Functional restriction of bromodomain-containing protein 4 (BRD4) reduced the susceptibility to erastin-induced ferroptosis of osteosarcoma cells both in vitro and in
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