BRD3(29-145) his tag

expressed in E. coli

≥98% (SDS-PAGE)

liquid

16.2 kDa

pkg of 1 mg
pkg of 100 μg
pkg of 20 μg

2 mg/mL

NM_007371

Q15059

dry ice

−70℃

human ... BRD3(8019)

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. BRD3 binds hyper-acetylated chromatin and plays a role in the regulation of transcription, probably by chromatin remodeling and interaction with transcription factors. It regulates transcription by promoting the binding of the transcription factor GATA1 to its targets and transcription of the CCND1 gene. A chromosomal aberration involving BRD3 was found in a rare, aggressive, and lethal carcinoma arising in midline organs of young people. The recombinant protein includes Bromodomain-containing protein 3 (contains 29-145 aa) with N-terminal His-tag.

rh-BRD3-BD1 is supplied as a solution in PBS Buffer containing 10% glycerol.

13 - Non Combustible Solids

WGK 3