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SDS-Page (Recombinant BRD4 (333-460) protein gel. BRD4 (333-460) protein was run on an SDS-PAGE gel and stained with Coomassie blue.)

BRD4 recombinant protein

Recombinant BRD4 (333-460) protein

Gene Names
BRD4; CAP; MCAP; HUNK1; HUNKI
Purity
The recombinant protein is >87% pure by SDS-PAGE.
Synonyms
BRD4; Recombinant BRD4 (333-460) protein; CAP; MCAP; HUNK1; HUNKI; BRD4 recombinant protein
Ordering
For Research Use Only!
Host
E Coli
Purity/Purification
The recombinant protein is >87% pure by SDS-PAGE.
Form/Format
Recombinant BRD4 (333-460) protein expressed in E Coli and supplied in 25mM HEPES pH7.5, 150mM NaCl and 5% glycerol.
Protein Species
Human
Tag
DYKDDDDK-Tag, His-Tag
Notes
Recombinant BRD4 (333-460) is suitable for use in binding assays, inhibitor screening, and selectivity profiling.
Dry Ice Shipment
Extra charge fee may add to your shipping cost as dry ice is required to ship this product.
Preparation and Storage
Recombinant proteins in solution are temperature sensitive and must be stored at -80 degree C to prevent degradation. Avoid repeated freeze/thaw cycles and keep on ice when not in storage.
Shipping Temp: Dry Ice

SDS-Page

(Recombinant BRD4 (333-460) protein gel. BRD4 (333-460) protein was run on an SDS-PAGE gel and stained with Coomassie blue.)

SDS-Page (Recombinant BRD4 (333-460) protein gel. BRD4 (333-460) protein was run on an SDS-PAGE gel and stained with Coomassie blue.)

Testing Data

(Recombinant BRD4 (333-460) HTRF activity assay 3.3 uM histone peptide H4K5/8/12/16(4Ac) was incubated with BRD4 (333-460) protein in reaction buffer including 50mM HEPES-NaOH pH 7.0, 0.1% BSA for 1 hour at room temperature. Anti-DYKDDDDK antibody was used to detect reaction products)

Testing Data (Recombinant BRD4 (333-460) HTRF activity assay 3.3 uM histone peptide H4K5/8/12/16(4Ac) was incubated with BRD4 (333-460) protein in reaction buffer including 50mM HEPES-NaOH pH 7.0, 0.1% BSA for 1 hour at room temperature. Anti-DYKDDDDK antibody was used to detect reaction products)
Related Product Information for BRD4 recombinant protein
Short Description: The peptide corresponding to amino acids 333-460 that contains the bromodomain sequences of BRD4 (accession number NP_490597.1) was expressed in E Coli and contains an N-terminal His-tag and C-terminal DYKDDDDK tag with an observed molecular weight of 20.9 kDa. Bromodomain-containing protein 4 (BRD4) belongs to the BET subclass of proteins, which are characterized by two N-terminal bromodomains and one ET (Extra Terminal) domain. BRDs associate with chromatin through their bromodomains that recognize acetylated histone lysine residues. Bromodomains function as 'readers' of these epigenetic histone marks and regulate chromatin structure and gene expression by linking associated proteins to the acetylated nucleosomal targets. The ET domain functions as a protein binding motif and exerts atypical serine-kinase activity. The BET family consists of at least four members in mouse and human, BRD2 (also referred to as FSRG1, RING3), BRD3 (FSRG2, ORFX), BRD4 (FSRG4, MCAP/HUNK1), and BRDT (FSRG3, BRD6). BRD proteins are related to the female Sterile Homeotic protein gene in Drosophila, a gene required maternally for proper expression of other homeotic genes, such as Ubx, which is involved in pattern formation. BRD4 has been identified recently as a therapeutic target in many cancers, including acute myeloid leukemia, multiple myeloma, Burkitt's lymphoma, NUT midline carcinoma, colon cancer, and breast cancer. BRD4 regulates the transcription of oncogenes, HIV, and human papilloma virus (HPV). It has been shown to bind and phosphorylate RNA pol II, which implicates its involvement in the regulation of eukaryotic transcription. Recombinant BRD4 (333-460) can be used in binding assays and inhibitor screening.

Background: BRD4 (Bromodomain-containing protein 4) belongs to the BET subclass of proteins, which are characterized by two N-terminal bromodomains and one ET (Extra Terminal) domain. BRDs associate with chromatin through their bromodomains that recognize acetylated histone lysine residues. Bromodomains function as 'readers' of these epigenetic histone marks and regulate chromatin structure and gene expression by linking associated proteins to the acetylated nucleosomal targets. The ET domain functions as a protein binding motif and exerts atypical serine-kinase activity. The BET family consists of at least four members in mouse and human, BRD2 (also referred to as FSRG1, RING3), BRD3 (FSRG2, ORFX), BRD4 (FSRG4, MCAP/HUNK1), and BRDT (FSRG3, BRD6). BRD proteins are related to the female Sterile Homeotic protein gene in Drosophila, a gene required maternally for proper expression of other homeotic genes, such as Ubx, which is involved in pattern formation. BRD4 has been identified recently as a therapeutic target in many cancers, including acute myeloid leukemia, multiple myeloma, Burkitt's lymphoma, NUT midline carcinoma, colon cancer, and breast cancer. BRD4 regulates the transcription of oncogenes, HIV, and human papilloma virus (HPV). It has been shown to bind and phosphorylate RNA pol II, which implicates its involvement in the regulation of eukaryotic transcription.
Product Categories/Family for BRD4 recombinant protein

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
155.8kDa
NCBI Official Full Name
bromodomain-containing protein 4 isoform long
NCBI Official Synonym Full Names
bromodomain containing 4
NCBI Official Symbol
BRD4
NCBI Official Synonym Symbols
CAP; MCAP; HUNK1; HUNKI
NCBI Protein Information
bromodomain-containing protein 4
UniProt Protein Name
Bromodomain-containing protein 4
UniProt Gene Name
BRD4
UniProt Synonym Gene Names
HUNK1
UniProt Entry Name
BRD4_HUMAN

NCBI Description

The protein encoded by this gene is homologous to the murine protein MCAP, which associates with chromosomes during mitosis, and to the human RING3 protein, a serine/threonine kinase. Each of these proteins contains two bromodomains, a conserved sequence motif which may be involved in chromatin targeting. This gene has been implicated as the chromosome 19 target of translocation t(15;19)(q13;p13.1), which defines an upper respiratory tract carcinoma in young people. Two alternatively spliced transcript variants have been described. [provided by RefSeq, Jul 2008]

Research Articles on BRD4

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Product Notes

The BRD4 brd4 (Catalog #AAA388160) is a Recombinant Protein produced from E Coli and is intended for research purposes only. The product is available for immediate purchase. It is sometimes possible for the material contained within the vial of "BRD4, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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