Product Details

Uniprot No.

O60885

Target Names

BRD4

Alternative Names

Bromodomain-containing protein 4 (Protein HUNK1), BRD4, HUNK1

Species Reactivity

Human

Immunogen

A synthesized peptide derived from human Brd4

Immunogen Species

Homo sapiens (Human)

Conjugate

Non-conjugated

Clonality

Monoclonal

Isotype

Rabbit IgG

Clone No.

1E5

Purification Method

Affinity-chromatography

Concentration

It differs from different batches. Please contact us to confirm it.

Buffer

Rabbit IgG in 10mM phosphate buffered saline , pH 7.4, 150mM sodium chloride, 0.05% BSA, 0.02% sodium azide and 50% glycerol.

Form

Liquid

Tested Applications

ELISA, WB, IHC

Recommended Dilution

Application	Recommended Dilution
WB	1:500-1:5000
IHC	1:50-1:200

Protocols

ELISA Protocol
Western Blotting(WB) Protocol
Immunohistochemistry (IHC) Protocol

Troubleshooting and FAQs

Antibody FAQs

Storage

Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.

Lead Time

Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

Description

BRD4 serves as a critical epigenetic reader protein that recognizes acetylated lysine residues on histones, functioning as a key transcriptional regulator that recruits the positive transcription elongation factor complex to promote gene expression. This bromodomain-containing protein has emerged as a compelling therapeutic target in oncology research, where its dysregulation drives aberrant transcriptional programs in multiple cancer types, making it essential for studies investigating chromatin biology and tumor progression mechanisms.

This recombinant monoclonal antibody, generated from clone 1E5 in rabbit host, offers the reproducibility advantages inherent to recombinant technology. Because the antibody sequence is defined and produced through controlled expression systems, researchers can expect consistent performance across experiments and between lots, eliminating the variability concerns that can complicate long-term studies or multi-site collaborations.

Validation testing demonstrates reliable detection of human BRD4 across multiple experimental platforms. In western blot applications, the antibody successfully identifies the 153 kDa band corresponding to the full-length protein in HeLa, 293T, HepG2, and A549 cell lysates at dilutions ranging from 1:500 to 1:5000. While BRD4 exists as multiple isoforms with predicted sizes of 153, 81, and 89 kDa, the observed detection of the 153 kDa species confirms recognition of the predominant full-length variant. For immunohistochemistry applications, the antibody has been validated in paraffin-embedded human brain tissue and human breast cancer specimens using citrate buffer antigen retrieval at dilutions of 1:50 to 1:200, providing flexibility for tissue-based expression studies.

Whether investigating BRD4's role in transcriptional regulation, exploring BET inhibitor mechanisms, or characterizing expression patterns in cancer specimens, this antibody supports diverse experimental approaches in epigenetics and oncology research.

Usage

For Research Use Only. Not for use in diagnostic or therapeutic procedures.

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Target Background

Function

Chromatin reader protein that recognizes and binds acetylated histones and plays a key role in transmission of epigenetic memory across cell divisions and transcription regulation. Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure. During interphase, plays a key role in regulating the transcription of signal-inducible genes by associating with the P-TEFb complex and recruiting it to promoters. Also recruits P-TEFb complex to distal enhancers, so called anti-pause enhancers in collaboration with JMJD6. BRD4 and JMJD6 are required to form the transcriptionally active P-TEFb complex by displacing negative regulators such as HEXIM1 and 7SKsnRNA complex from P-TEFb, thereby transforming it into an active form that can then phosphorylate the C-terminal domain (CTD) of RNA polymerase II. Promotes phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II. According to a report, directly acts as an atypical protein kinase and mediates phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II; these data however need additional evidences in vivo. In addition to acetylated histones, also recognizes and binds acetylated RELA, leading to further recruitment of the P-TEFb complex and subsequent activation of NF-kappa-B. Also acts as a regulator of p53/TP53-mediated transcription: following phosphorylation by CK2, recruited to p53/TP53 specific target promoters.; Acts as a chromatin insulator in the DNA damage response pathway. Inhibits DNA damage response signaling by recruiting the condensin-2 complex to acetylated histones, leading to chromatin structure remodeling, insulating the region from DNA damage response by limiting spreading of histone H2AX/H2A.x phosphorylation.

Gene References into Functions

Genetic and pharmacological inhibition of BRD4 suppressed IL-1beta-induced expression and translocation of HMGB1. Chromatin immunoprecipitation (ChIP) showed the enrichment of BRD4 around the HMGB1 upstream non-promoter region, which diminished with JQ1 treatment. PMID: 28844955
miR204 directly binds to UCA1 and the 3'untranslated region of BRD4. Furthermore, UCA1 competed with BRD4 for miR204 binding. miR204 knockdown enhanced BRD4 expression, which can be partially restored by short hairpinUCA1. PMID: 30015945
High BRD4 expression is associated with preeclampsia. PMID: 29748248
BRD4 silencing was negatively correlated palomid 529-induced apoptosis in the primary human renal cell carcinoma cells and tumor growth in SCID mice. PMID: 30308518
miR-608 inhibits hepatocellular carcinoma cell proliferation possibly via targeting BET family protein BRD4. PMID: 29777702
MS645 blocks BRD4 binding to transcription enhancer/mediator proteins MED1 and YY1 with potency superior to monovalent BET inhibitors, resulting in down-regulation of proinflammatory cytokines and genes for cell-cycle control and DNA damage repair that are largely unaffected by monovalent BrD inhibition. PMID: 30012592
Study shows that BRD4 is significantly highly expressed in gastric cancer patients and cell lines and positively regulates the expression of c-MYC through transcription regulation and epigenetic levels. Functionally, these result demonstrate that the knockdown of BRD4 represses the proliferation and induces the apoptosis of gastric cancer cells through repression of c-MYC. PMID: 28681984
BRD4 hyperphosphorylation is associated with cellular transformation in NUT midline carcinoma PMID: 28630312
Results suggest structure-based drug design of bromodomain-containing protein 4 (Brd4) inhibitors. PMID: 27494802
Cells harboring the fusion gene are selectively sensitive to small-molecule inhibition of protein targets induced by, or bound to, PAX3-FOXO1-occupied super enhancers. Furthermore, PAX3-FOXO1 recruits and requires the BET bromodomain protein BRD4 to function at super enhancers, resulting in a complete dependence on BRD4 and a significant susceptibility to BRD inhibition PMID: 28446439
Our data suggested that downregulation of BRD4 in gallbladder cancer (GBC) cells induced apoptosis by PI3K/AKT pathway. Inhibition of BRD4 expression may be a novel therapeutic strategy for patients with GBC. PMID: 28766687
these results highlighted the significant genetic contribution of the ARID1B variant, rs73013281, to susceptibility for HCC, especially in interaction with physical activity. PMID: 28415703
In pluripotent cells, Brd2-Brd4 occupy Nodal gene regulatory elements (NREs), but only Brd4 is required for pluripotency gene expression. Brd4 downregulation facilitates pluripotent exit and drives enhanced Brd2 NRE occupancy, thereby unveiling a specific function for Brd2 in differentiative Nodal-Smad2 signalling PMID: 28588073
Findings reveal that PCa-associated ERG can interact and co-occupy with BRD4 in the genome, and suggest this druggable interaction is critical for ERG-mediated cell invasion and PCa progression. PMID: 27223260
Data suggest that pharmacological inhibition of BET proteins could be a potential treatment for renal fibrosis. PMID: 27732564
Our data strongly support the use of CCR2 and CD180 mRNAs as whole blood pharmacodynamic (PD)biomarkers for BRD4 inhibitors, especially in situations where paired tumor biopsies are unavailable. In addition, they can be used as tumor-based PD biomarkers for hematologic tumors. PMID: 28073847
Study identified Brd4 as a novel proline hydroxylation substrate with nearly 60% stoichiometry under normoxia states and its hydroxylation level is enzymatically regulated. PMID: 27764789
Further analysis indicated that JQ1 inhibited the recruitment of BDR4 to the promoter complex of the Myc and Ccnd1 genes in rat thyroid follicular PCCL3 cells, resulting in decreased MYC expression at the mRNA and protein levels to inhibit tumor cell proliferation PMID: 27440272
The Brd4 acetyllysine-binding protein of RelA is involved in activation of polyomavirus JC. PMID: 27007123
BRD4 phosphorylation regulates HPV E2-mediated viral transcription and cellular MMP-9 expression PMID: 27477287
conclude that BRD3/4 and the FLT3-TAK1/NF-kB pathways collectively control a set of targets that are critically important for the survival of human MLL-AF9 cells PMID: 29240787
Diverse gastric cancer cell lines of Asian and Brazilian origins differ in BRD4 and c-MYC expression levels and sensitivity to BET inhibitors. PMID: 27259267
Together, dual inhibition of BRD4 and PI3K by SF2523 suppresses human prostate cancer cell growth in vitro and in vivo. PMID: 29133261
peroxisome proliferator activated receptor alpha peroxisome proliferator-activated receptor alpha PPAR-alpha nuclear receptor subfamily 1 group C member 1 peroxisome proliferative activated receptor alpha peroxisome proliferator-activated nuclear receptor alpha variant 3 PMID: 28012209
Brd4 is involved in different steps of the papillomavirus life cycle. (Review) PMID: 27965149
BRD4 and MYC are essential for the expression of a subgroup of genes induced by class-I HDAC inhibitors. PMID: 28369619
Data show that BRD4 controls RUNX2 by binding to the enhancers (ENHs) and each RUNX2 ENH is potentially controlled by a distinct set of TFs and c-JUN as the principal pivot of this regulatory platform. PMID: 28981843
any of the molecules or processes in the network could be targeted to curb the oncogenic effects of c-Myc, just as BRD4 can be targeted. And since the targeting of metabolic enzymes has proved effective in mouse tumor models, it might be possible to develop new therapies based on the fact that c-Myc has a role in controlling cellular metabolism PMID: 28100396
Brd4 inhibition attenuates unilateral ureteral obstruction-induced fibrosis by blocking TGF-beta-mediated Nox4 expression. PMID: 28063381
The response of the kinome to targeted BETi treatment in a panel of BRD4-dependent ovarian carcinoma (OC) cell lines. PMID: 27452461
A miR-9 mimic represses stimulus-dependent targeting of BRD4. PMID: 27425608
BRD4 and CDK9 have independent, coordinated roles in promoting the myofibroblast transition PMID: 28182006
Long-term treatment with bromodomain-containing protein 4 (BRD4) inhibitors caused telomere shortening in both mouse and human cells, suggesting BRD4 plays a role in telomere maintenance in vivo. PMID: 28854735
The short isoform of BRD4 cooperates with SWI/SNF nucleosome remodelers to repress HIV transcription during latency, a phenotype reversed by BET inhibitor treatment. PMID: 28844864
results indicated that in MPNST samples BRD4 mRNA levels were not upregulated and that MPNST cell lines were relatively insensitive to the bromodomain inhibitor JQ1. PMID: 28813519
High BRD4 expression is associated with stomach neoplasms. PMID: 28481868
These findings reveal a novel mechanism by which the HBV genome hijacks the host P-TEFb-containing complexes to promote its own transcription; both the super elongation complex and BRD4 can bind to the HBV genome. PMID: 28694331
Chemical degrader of BET bromodomain proteins, dBET6, led to the unexpected identification of BRD4 as master regulator of global transcription elongation in acute T-cell leukemia. BRD4 loss does not directly affect CDK9 localization. PMID: 28673542
BRD4 binds and stays associated with chromatin during mitosis, bookmarking early G1 genes and reactivating transcription after mitotic silencing. BRD4 acts as a passive scaffold via its recruitment of vital transcription factors and as an active kinase that phosphorylates RNA polymerase II. A model in which BRD4 actively coordinates chromatin structure and transcription is described. Review. PMID: 27450555
we have discovered that BRD4-bound super-enhancers provide a powerful tool for enriching and prioritizing PC and BC genetic risk loci PMID: 28359301
BRD4 represses autophagy and lysosome gene expression. This repression is alleviated during nutrient deprivation through AMPK-SIRT1 signaling, allowing autophagy activation. BRD4 inhibition enhances autophagic flux and lysosomal function and promotes the degradation of protein aggregates. Sakamaki et PMID: 28525743
The studies show that BRD4 inhibition may have therapeutic implications for the treatment of mitochondrial diseases. PMID: 27666594
A BRD4 missense mutation was the likely disease-causing mutation in this family with autosomal dominant syndromic congenital cataracts associated with neuro-skeletal anomalies. PMID: 28076398
these studies highlight the importance of Brd4 in Helicobacter pylori-induced inflammatory gene expression and suggest that Brd4 could be a potential therapeutic target for the treatment of Helicobacter pylori-triggered inflammatory diseases and cancer PMID: 27084101
BRD4 positively regulates EZH2 transcription through upregulation of C-MYC, and is a novel promising target for pharmacologic treatment in transcriptional program intervention against this intractable disease. PMID: 26939702
We postulate that BRD4-NUT (B4N) complexes override the preexisting histone code with new posttranslational modifications patterns that reflect aberrant transcription and that epigenetically modulate the nucleosome environment toward the NUT-midline carcinoma (NMC) state. PMID: 27698495
The authors show that, upon infection of primary human keratinocytes with human papillomavirus 18 quasivirus, Brd4 activates viral transcription and replication. PMID: 27879331
research reveals that BRD4 probably play a critical role in Renal Cell Carcinoma progression, and is a new promising target for pharmacological treatment directed against this intractable disease. PMID: 28391274
These data provide a detailed mechanism for how activated NF-kappaB and BRD4 control epithelial-mesenchymal transition initiation and transcriptional elongation in model airway epithelial cells in vitro and in a murine pulmonary fibrosis model in vivo. PMID: 27793799
BRD4 localization to lineage-specific enhancers is associated with a distinct transcription factor repertoire. PMID: 27651452

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Involvement in disease

A chromosomal aberration involving BRD4 is found in a rare, aggressive, and lethal carcinoma arising in midline organs of young people. Translocation t(15;19)(q14;p13) with NUT which produces a BRD4-NUT fusion protein.

Subcellular Location

Nucleus. Chromosome.; [Isoform B]: Chromosome.

Tissue Specificity

Ubiquitously expressed.

Database Links

HGNC: 13575

OMIM: 608749

KEGG: hsa:23476

STRING: 9606.ENSP00000263377

UniGene: Hs.187763

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Code	CSB-RA152430A0HU
Size	US$210
	Order now
Image	Western Blot Positive WB detected in: Hela whole cell lysate, 293T whole cell lysate, HepG2 whole cell lysate, A549 whole cell lysate All lanes: BRD4 antibody at 1:1500 Secondary Goat polyclonal to rabbit IgG at 1/50000 dilution Predicted band size: 153, 81, 89 kDa Observed band size: 153 kDa IHC image of CSB-RA152430A0HU diluted at 1:100 and staining in paraffin-embedded human brain tissue performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4℃ overnight. The primary is detected by a Goat anti-rabbit IgG polymer labeled by HRP and visualized using 0.05% DAB. IHC image of CSB-RA152430A0HU diluted at 1:100 and staining in paraffin-embedded human breast cancer performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4℃ overnight. The primary is detected by a Goat anti-rabbit IgG polymer labeled by HRP and visualized using 0.05% DAB.
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BRD4 Recombinant Monoclonal Antibody

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Target Background