BRD3 (29-145), His, Human Proteins
- Known as:
- BRD3 (29-145), histidine, Human Proteins
- Catalog number:
- Z03186-100
- Product Quantity:
- 100ug
- Category:
- Proteins
- Supplier:
- Genscript
- Gene target:
- BRD3 (29-145) His Human Proteins
Related genes to: BRD3 (29-145), His, Human Proteins
- Gene:
- BRD3 NIH gene
- Name:
- bromodomain containing 3
- Previous symbol:
- -
- Synonyms:
- RING3L, ORFX, KIAA0043
- Chromosome:
- 9q34.2
- Locus Type:
- gene with protein product
- Date approved:
- 2000-07-25
- Date modifiied:
- 2016-10-05
Related products to: BRD3 (29-145), His, Human Proteins
Related articles to: BRD3 (29-145), His, Human Proteins
- AG1-IA is a major soil-borne pathogen responsible for sheath blight in rice, causing significant yield losses globally. Early, rapid, and accurate detection is essential for effective disease management, as traditional methods are time-consuming and less sensitive. In this study, we developed and validated a highly specific molecular marker, BrD3 targeting the bromodomain-containing Major Facilitator Superfamily (MFS) gene. This marker was successfully employed in PCR, quantitative PCR (qPCR), and Loop-mediated Isothermal Amplification (LAMP) assays for the detection of the pathogen in infected rice plants and soil samples. The PCR assay detected as low as 100 pg of DNA, while the qPCR assay demonstrated higher sensitivity, detecting 10 pg of DNA with high efficiency and accuracy (R > 0.99). Further, marker was utilized for the resistance evaluation against sheath blight disease of rice where highest copy no. of target gene was detected in susceptible rice variety Pusa Basmati 1121, and minimum copy no. was detected in resistant variety Tetep under inoculated conditions. The LAMP assay, optimized at 63°C with Hydroxy Naphthalol Blue (HNB) dye, provided rapid visual detection with a sensitivity of 1 ng DNA and no cross-reactivity with other rice pathogens. All three assays were validated in infected plants across multiple rice genotypes and soil samples of rice-wheat cropping system. The integrated diagnostic approach presented here offers a robust, specific, and field-deployable system for early detection and soil population monitoring of (AG1-IA) facilitating timely disease management. - Source: PubMed
Publication date: 2026/05/21
Singh AsmitaTadasanahaller Prashantha SSharma SapnaSubbaiyan Gopala KrishnanAggarwal RashmiShanmugam VSaharan Mahender SBashyal Bishnu Maya - We previously showed that AlphaFold2 can be used to screen for peptide-binding epitopes targeting the extraterminal (ET) domain of Bromodomain and Extraterminal (BET) proteins from candidate protein partners identified in pull-down experiments. However, such approaches require large numbers of AlphaFold2 calculations, making exhaustive screening impractical for larger datasets, such as viral proteomes that may target the ET domain. In many cases, identifying a substantial fraction of binders-even without exhaustive coverage-would already provide valuable biological insight into these interaction networks. Here, we show that an active learning strategy based on Thompson sampling (TS) can efficiently explore peptide sequence space. Using a library derived from BRD3 pull-down experiments, TS recovers 50% of all binders using 15% of the queries required by exhaustive sampling (3.3 times improvement over random sampling). Moreover, TS consistently identifies experimentally known binding epitopes with substantially fewer queries. Because the approach relies only on binary labels, it is readily transferable to other protein-peptide systems where AF-based binding classification is applicable, as well as to peptide-property predictors for properties such as solubility or aggregation propensity. - Source: PubMed
Publication date: 2026/04/18
Gaza JokentSantos Jherome Brylle WoodySingh BhumikaMiranda-Quintana Ramón AlainPerez Alberto - 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 - The bromodomain and extraterminal domain (BET) family uses its conserved ET domains to recognize diverse peptide motifs, yet exhibits paralog-specific binding preferences whose structural origins remain poorly understood. Using extensive molecular dynamics (MD) simulations of BRD3-ET and BRD4-ET and experimental data for the unbound and peptide-bound states, we show that paralog selectivity arises not from large structural rearrangements but from subtle differences in the dynamics of the α2-α3 loop. Two divergent residues at positions 35 and 36 in this loop modulate the formation of flanking helices (η1 and η2), which in turn control the opening of the peptide-binding cavity and determine how each paralog accommodates distinct binding modes. These sequence-encoded dynamical differences shape the number, stability, and geometry of accessible binding modes and provide a structural rationale for paralog-specific targeting of BET proteins. - Source: PubMed
Publication date: 2026/04/15
Alvarez GuadalupeSebastian ElizabethMondal ArupRoth Monica JMontelione Gaetano TPerez Alberto - 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