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

ORFX, RING3L, Bromodomain containing protein 3, RING3-like protein

     
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Product info
Primary Accession Q15059
Concentration 0.5
Calculated MW 48.1 kDa (439 aa, 1-416 aa + His Tag), confirmed by MALDI-TOF.
Additional Info
Gene ID 8019
Gene Symbol BRD3
Other Names ORFX, RING3L, Bromodomain containing protein 3, RING3-like protein
Gene Source Human
Source E. coli
Assay&Purity SDS-PAGE; ≥85%
Assay2&Purity2 N/A;
Recombinant Yes
Sequence MGSSHHHHHH SSGLVPRGSH MGSMSTATTV APAGIPATPG PVNPPPPEVS NPSKPGRKTN QLQYMQNVVV KTLWKHQFAW PFYQPVDAIK LNLPDYHKII KNPMDMGTIK KRLENNYYWS ASECMQDFNT MFTNCYIYNK PTDDIVLMAQ ALEKIFLQKV AQMPQEEVEL LPPAPKGKGR KPAAGAQSAG TQQVAAVSSV SPATPFQSVP PTVSQTPVIA ATPVPTITAN VTSVPVPPAA APPPPATPIV PVVPPTPPVV KKKGVKRKAD TTTPTTSAIT ASRSESPPPL SDPKQAKVVA RRESGGRPIK PPKKDLEDGE VPQHAGKKGK LSEHLRYCDS ILREMLSKKH AAYAWPFYKP VDAEALELHD YHDIIKHPMD LSTVKRKMDG REYPDAQGFA ADVRLMFSNC YKYNPPDHEV VAMARKLQDV FEMRFAKMP
Target/Specificity BRD3
Format Liquid
Storage -80°C; 0.5 mg/ml in Phosphate buffer saline (pH 7.4) containing 10% glycerol.
Citations (0)

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Background

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.

References

Nomura N.,et al.DNA Res. 1:223-229(1994).
Ishii H.,et al.DNA Cell Biol. 24:432-437(2005).
Humphray S.J.,et al.Nature 429:369-374(2004).
Mural R.J.,et al.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
Thorpe K.L.,et al.Gene 200:177-183(1997).

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$ 295.00
Cat# PBV11029r
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