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BRD3 bromodomain (1-416 aa) (His-Tag), human recombinant

A protein involved in chromatin targeting
Catalog #: 7407
$295.00

Product Details

Cat # +Size 7407-100
Size 100 μg
Alternate Name ORFX, RING3L, Bromodomain containing protein 3, RING3-like protein
Gene Symbol BRD3
Gene ID 8019
Accession # Q15059
Source E. coli
Appearance Liquid
Physical Form Description 0.5 mg/ml in Phosphate buffer saline (pH 7.4) containing 10% glycerol.
Molecular Weight 48.1 kDa (439 aa, 1-416 aa + His Tag), confirmed by MALDI-TOF.
Purity by SDS-PAGE ≥85%
Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MGSMSTATTV APAGIPATPG PVNPPPPEVS NPSKPGRKTN QLQYMQNVVV KTLWKHQFAW PFYQPVDAIK LNLPDYHKII KNPMDMGTIK KRLENNYYWS ASECMQDFNT MFTNCYIYNK PTDDIVLMAQ ALEKIFLQKV AQMPQEEVEL LPPAPKGKGR KPAAGAQSAG TQQVAAVSSV SPATPFQSVP PTVSQTPVIA ATPVPTITAN VT
Handling Centrifuge the vial prior to opening.
Storage Conditions -80°C
Shipping Conditions Dry Ice
USAGE For Research Use Only! Not to be used in humans

Details

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. Recombinant human BRD3 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.


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