BRD1 (556-688) his tag human

NA.32

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. BRD1 is a bromodomain containing protein that has been identified as a susceptibility gene in neurological disorders, such as schizophrenia and bipolar affective disorder. This protein can be used for the study of bromodomain binding assays, screening inhibitors, and selectivity profiling. Recombinant human BRD1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.

0.5 mg/mL in Phosphate buffer saline (pH 7.4) containing 10% glycerol and 1mM DTT.

human

expressed in E. coli

≥95% (SDS-PAGE)

liquid

17.8 kDa (156 aa, 556-688 aa + His Tag)

pkg of 100 μg

0.5 mg/mL

O95696

dry ice

−70℃

human ... BRD1(23774)

GHS07

Warning

H319

P264 - P280 - P305 + P351 + P338 - P337 + P313

Eye Irrit. 2

11 - Combustible Solids

WGK 3