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. BRM is a member of the SWI/SNF protein family, which forms part of a large ATP-dependent chromatin remodeling complex. This complex is required for transcriptional activation of genes normally repressed by chromatin.
Human proteins, cDNA and human recombinants are used in human reactive ELISA kits and to produce anti-human mono and polyclonal antibodies. Modern humans (Homo sapiens, primarily ssp. Homo sapiens sapiens). Depending on the epitopes used human ELISA kits can be cross reactive to many other species. Mainly analyzed are human serum, plasma, urine, saliva, human cell culture supernatants and biological samples.
50 mM Tris, pH 7.5, containing 500 mM sodium chloride, 5% glycerol, and 5 mM β-mercaptoethanol.
BRM bromodomain (1367-1511 aa) (GST-tagged), Human recombinant
For Research Use Only! Not to be used in humans
Centrifuge the vial prior to opening.
43.7 kDa (1367-1511 aa + NT GST Tag)
Recombinants or rec. proteins
SMARCA2A/B; SWI/SNF ATPase