BRD2 antibody - C-terminal region (ARP34211_T100)
- Known as:
- BRD2 (anti-) - C-terminal region (ARP34211_T100)
- Catalog number:
- arp34211_t100
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- BRD2 antibody - C-terminal region (ARP34211_T100)
Related genes to: BRD2 antibody - C-terminal region (ARP34211_T100)
- Gene:
- BRD2 NIH gene
- Name:
- bromodomain containing 2
- Previous symbol:
- BRD2-IT1
- Synonyms:
- KIAA9001, RING3, D6S113E, NAT, FSRG1
- Chromosome:
- 6p21.32
- Locus Type:
- gene with protein product
- Date approved:
- 2000-07-25
- Date modifiied:
- 2017-01-12
Related products to: BRD2 antibody - C-terminal region (ARP34211_T100)
Related articles to: BRD2 antibody - C-terminal region (ARP34211_T100)
- The engineered formation of ternary complexes, in which two proteins are bridged by small molecules such as PROTACs or molecular glues, is a prerequisite for the targeted enzymatic degradation of pathogenic proteins; however, the combined analysis of these ternary interactions during the drug discovery process remains challenging. Here, we introduce a proximity binding assay for the simultaneous measurement of binary and ternary interaction kinetics on a biosensor surface. Target proteins and the substrate binding subunit of ubiquitin E3 ligase are tethered to mobile swivel arms of a Y-shaped DNA scaffold. The Y-structure induces spatial proximity between the proteins and presents them to PROTAC analytes flown across the sensor. PROTAC-induced ternary complex formation is measured by fluorescence energy transfer (FRET), while binary interactions are detected by fluorescence quenching. The assay is applied to cereblon (CRBN) and von Hippel-Lindau (VHL) as E3 ligase substrate receptors, a range of compounds including AT1, MZ1, dBETs, and ARV-825 as PROTACs, and the two bromodomains of BRD2, BRD3, BRD4, and BRDT proteins as targets. Automated workflows enable the measurement of 384 real-time sensorgrams in a single run using picomole sample quantities. The insights into proximity-mediated binding kinetics can enable the development of PROTACs and molecular glues with improved properties for targeted protein degradation. - Source: PubMed
Publication date: 2026/04/21
Ponzo IreneSoldà AliceCrowe CharlotteDahl GöranJahodová TerezaHeerwig AndreasGeschwindner StefanCiulli AlessioRant Ulrich - Transforming growth factor-β (TGF-β) is a multifunctional cytokine that regulates cell proliferation, differentiation, migration, and apoptosis. It is generally accepted that TGF-β induces cellular responses through Smad-dependent gene transcription. However, the underlying mechanisms that modulate the transcriptional activities of Smads are not yet fully understood. Here, we identify BRD2, a member of the bromodomain and extraterminal (BET) family, as a key transcriptional coactivator for Smad3. BRD2 physically interacts with Smad3 through a newly identified Smad3-binding region (SBR). This BRD2-Smad interaction enhances Smad's association with chromatin and amplifies its transcriptional activity, playing a vital role in TGF-β transcriptional and tumor-suppressive responses. Our findings establish BRD2 as an important modulator of TGF-β signaling and suggest that it may serve as a potential target for TGF-β-related diseases. - Source: PubMed
Publication date: 2026/04/15
Tian ShuaiGu ShuchenSun ShuangwuWang ZhaoyangZhao YingmingYuan BoLiu XiaZhao BinXu PinglongCao JinXiao MuYu YiFeng Xin-Hua - Targeted protein degradation (TPD) is a powerful strategy for controlling protein abundance. Here, we establish FBXO31 as a TPD-competent E3 ligase by exploiting its recognition of C-terminal amide-bearing degrons. Using an amidated Ala-Phe motif as a chemical recruiter, multiple small-molecule binders can be transformed into FBXO31-dependent degraders that induce the rapid and potent degradation of FKBP12, multiple kinases, and BET proteins BRD2, BRD3, and BRD4. Mechanistic studies confirm FBXO31-mediated ternary complex formation and identify key residues in FBXO31 required for recruiter engagement and target degradation. - Source: PubMed
Publication date: 2026/04/10
Zhang ChenluJin XiaokangZhou ChenJenkins M JamalRiha Isabella AZhang Xiaoyu - Bromodomain (BD) and extra-terminal domain (BET) proteins are key regulators of RNA polymerase II (Pol II)-mediated transcription and their BDs represent promising drug targets. Yet, the interplay between histone acetylation and the chromatin dynamics of individual BET proteins with respect to transcriptional regulation is not fully understood. Here in mouse embryonic stem cells, we uncover an essential role of BRD2 in maintaining Pol II recruitment at promoters through its interaction with TFIID, which becomes particularly critical under the conditions of impaired pause release. Combining rapid protein degradation, chemogenomics and super-resolution microscopy, we show that MOF-mediated histone H4 acetylation promotes BRD2 chromatin association, which in turn enables BRD2 clustering. Accordingly, MOF depletion or deletion of the BRD2's intrinsically disordered region largely recapitulates defects in promoter enrichment and clustering of the transcription machinery observed upon BRD2 loss. Thus, these findings support a model in which histone acetylation-dependent spatiotemporal dynamics of BRD2 coordinate the transcription machinery to regulate transcription initiation. - Source: PubMed
Publication date: 2026/04/09
Erdogdu Niyazi UmutGuhathakurta SukanyaOellers RonaldShvedunova MariaMorin Jose APatrick Eric MSeyfferth JanineDeboutte WardGomez-Auli AlejandroMittler GerhardCissé Ibrahim IAkhtar Asifa - The devastating COVID-19 pandemic has urged continuous efforts to uncover innovative intervention measures through a thorough understanding of viral and associated host protein functions. In this study, we investigate the interaction of coronavirus E protein with BRD2, a member of the bromodomain and extra-terminal (BET) protein family, and the mechanism underlying the regulatory role of BRD2 in promoting pro-inflammatory responses during coronavirus infection, based on the reported potential interaction of BRD2 with severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) E protein and our transcriptomic assay. We show that coronavirus infection significantly upregulates the expression of pro-inflammatory cytokines and BET family genes and activates the NF-κB pathway, although the ion channel (IC) activity of the avian infectious bronchitis virus (IBV) E protein only minimally affects the upregulation of BRD2 transcription. Furthermore, BRD2 was verified to interact with the E protein from IBV, SARS-CoV, and SARS-CoV-2, via the BDII-containing C-terminal region of BRD2 and the C-terminal region of the E protein. This interaction resulted in the partial translocation of BRD2 from the nucleus to the cytoplasm in IBV-infected cells and its close association with viral particles. Overexpression of BRD2 and IBV E protein independently induced the expression of pro-inflammatory cytokines, and a synergistic role was demonstrated in cells co-expressing the two proteins. BRD2 was further found to activate the NF-κB signaling pathway and enhance the expression of pro-inflammatory cytokines IL-6, IL-8, and TNF-α at the mRNA level. Conversely, knockdown of BRD2 promotes viral replication and apoptosis. These findings underscore the interaction between BRD2 and E protein, elucidating their roles in regulating coronavirus replication and promoting the pro-inflammatory response.IMPORTANCESevere coronavirus infections usually result in excessive secretion of inflammatory cytokines and chemokines, leading to cell death and ultimately collapse of the immune system with fatal outcomes. So far, intensive studies on host-pathogen interactions have partially elucidated the immunopathogenesis of COVID-19 and other coronavirus infections. This study reveals that coronavirus infection induces the expression of BRD2 and activates the NF-κB pathway. BRD2 interacts with coronavirus E protein, and the two proteins work together to play a synergistic role to promote pro-inflammatory response during coronavirus infection. Furthermore, BRD2 was shown to independently activate the NF-κB pathway and enhance the expression of IL-6, IL-8, TNF-α, and several other proteins related to the pro-inflammatory and inflammatory responses. The interaction of BRD2 with coronavirus E protein and its regulatory role in inflammation would make it a potential therapeutic target for severe coronavirus infections. - Source: PubMed
Publication date: 2026/03/03
Li ShuminLiu Ding Xiang