AIB1 (clone 50B6) mAb
- Known as:
- AIB1 (clonality 50B6) mAb
- Catalog number:
- ASA905706100
- Product Quantity:
- 100 µg
- Category:
- -
- Supplier:
- Other suppliers
- Gene target:
- AIB1 (clone 50B6) mAb
Related genes to: AIB1 (clone 50B6) mAb
- Gene:
- NCOA3 NIH gene
- Name:
- nuclear receptor coactivator 3
- Previous symbol:
- -
- Synonyms:
- RAC3, AIB1, ACTR, p/CIP, TRAM-1, CAGH16, TNRC16, KAT13B, bHLHe42, SRC-3, SRC3
- Chromosome:
- 20q13.12
- Locus Type:
- gene with protein product
- Date approved:
- 1999-12-17
- Date modifiied:
- 2016-10-05
Related products to: AIB1 (clone 50B6) mAb
Related articles to: AIB1 (clone 50B6) mAb
- Most autoimmune disease-associated variants lie in non-coding regions, but the molecular mechanisms linking these variants to gene regulation remain poorly understood. A major unresolved challenge is to determine how disease alleles alter transcription factor (TF) binding, cofactor (COF) recruitment, and enhancer activity at scale. Here, we used the CASCADE method to profile differential binding of five TFs and ten COFs to 2,901 autoimmune disease-associated variants in Jurkat T cells, identifying 516 binding-modulating variants. Variants impacting binding were enriched among MPRA-defined expression-modulating variants and were strongly concordant with allele-specific reporter expression, linking altered TF/COF recruitment to enhancer activity. A majority of variants perturb binding of five major TF families - ETS, RUNX, SP/KLF, OVOL/MYBL, and bHLH - all of which have established roles in T cell biology. Notably, we find that ETS and RUNX factor binding is enriched at different variant functional classes, suggesting that they act through distinct regulatory mechanisms at disease loci. We describe allele-dependent regulator "switching" at several loci, where distinct complexes are found at reference and variants alleles, and we identify a recurrent regulatory module involving FOXM1 and the cofactors TIP60, BRD4, NCOA3, and NCOA1 assembling on ETS sites that tracks with gene expression. Together, this integrated biochemical and functional framework prioritizes autoimmune disease-associated variants by linking allele-specific TF/COF binding mechanisms to enhancer activity. - Source: PubMed
Publication date: 2026/05/22
Dashtiahangar MaryamSiggers Trevor - SUMOylation has emerged as a key regulator of chromatin and transcription, yet its contribution to lineage reprogramming remains unclear. To explore how chromatin SUMOylation influences cellular plasticity, we studied CEBPA-driven lineage reprogramming of human leukemic B-cells into macrophage-like cells. By integrating ChIP-seq, ATAC-seq, RNA-seq and chromatin-directed proteomics, we mapped the chromatin landscape and transcriptomic changes during early reprogramming. Lineage conversion triggered a dynamic rise in SUMO2/3 chromatin occupancy at CEBPA-bound sites, revealing a coordinated regulatory mechanism. Proteomic profiling of SUMO2/3- and CEBPA-associated chromatin uncovered extensive convergence and enrichment of differentiation-related transcription factors, chromatin remodelers and coregulators. Among these, NCOA3 displayed markedly increased SUMO2/3 association upon lineage conversion. NCOA3 co-occupied CEBPA- and SUMO2/3-bound chromatin regions, implying a SUMOylation-supported coregulatory role in lineage reprogramming. Pharmacological inhibition of SUMOylation using ML-792 (SUMOi) selectively enhanced CEBPA chromatin occupancy and chromatin accessibility, altered the CEBPA association of proteins, and modified NCOA3 binding dynamics. SUMOi also reshaped gene expression, promoting loss of B-cell identity and activation of macrophage-associated programs, including lipid metabolism. Collectively, our findings highlight chromatin SUMOylation as a dynamic and context-dependent modifier that fine-tunes lineage transitions, with implications for chromatin biology and therapeutic modulation of cell identity. - Source: PubMed
Publication date: 2026/05/27
Valima EmmaManjur A B M KaiserSavinainen EeviVaris VeraLaunonen Kaisa-MariGraf ThomasVarjosalo MarkkuNiskanen Einari APalvimo Jorma J - MicroRNA and mRNA profiling of T cells from Acquired Aplastic Anaemia (AA) patients using both in-silico and in-vitro methods identified molecular changes, including altered immune-regulatory gene expression, linked to T-cell dysregulation and AA pathobiology. - Source: PubMed
Publication date: 2026/04/16
Rai BhuvneshSabereen GhazalaSaxena PragatiSrivastava JyotikaGupta RuchiChaturvedi Chandra Prakash - Intrinsically disordered proteins (IDPs) play essential roles in cellular signaling and regulation, often relying on transient structural elements to mediate interactions. NMR chemical shifts are widely used to detect secondary structures in IDPs, but complementary methods are needed to validate and refine these measurements. Hydrogen exchange is a powerful probe of local structure and dynamics in folded proteins, yet its accuracy for detecting small differences in transient helicity in IDPs remains understudied. Here, we systematically evaluate hydrogen exchange measured by NMR and MS (HDX-MS) in four variants of the activator for thyroid hormone and retinoid receptors (ACTR) activation domain that differ in helical propensity. Using NMR-based exchange rates, we introduce pseudo-protection factors referenced to the wild-type protein, enabling a robust comparison among variants without relying on "intrinsic" peptide-based chemical exchange rates. These pseudo-protection factors correlate strongly with helicity derived from chemical shifts, demonstrating that hydrogen exchange can resolve subtle structural differences in highly dynamic regions and vice versa. Our findings establish hydrogen exchange as a sensitive and reproducible method for characterizing transient structure in IDPs, complementing NMR chemical shift analysis. - Source: PubMed
Publication date: 2026/04/06
Cuciurean I SiminaParsbæk Christian BuchRand Kasper DMulder Frans A ATeilum Kaare - Metabolic dysfunction-associated steatotic liver disease (MASLD) and metabolic dysfunction-associated steatohepatitis (MASH) are leading causes of cirrhosis and hepatocellular carcinoma. Defects in autophagy contribute to the development of MASLD; however, the role of Unc-51-like autophagy-activating kinase 1 (ULK1) in the pathophysiology of MASLD remains unclear. Herein, we show that ULK1, a serine/threonine kinase and core autophagy protein, is significantly repressed in human MASH livers, and that hepatocyte-specific loss of ULK1 promotes, unexpectedly, hepatic steatosis and progression to liver fibrosis, without affecting basal autophagy flux. Phospho-proteomics identified the transcriptional coactivator NCOA3 as a downstream phospho-target of ULK1. Mechanistically, ULK1 phosphorylates NCOA3 to repress its transcriptional activity and restrain the CREB/CBP-mediated de novo lipogenic program. Accordingly, a phosphorylation-deficient NCOA3 mutant drives CREB/CBP-mediated lipogenesis, whereas genetic or pharmacological NCOA3 inhibition prevents steatosis, hepatic inflammation, and profibrotic signaling. Hence, ULK1-mediated NCOA3 phosphorylation is a fundamental and druggable checkpoint against the entire MASLD spectrum. - Source: PubMed
Publication date: 2026/04/02
Koo Young DoCastillo Romilia TatianaSukumaran Nair AshaGarneau MichaelGochee ChadCampbell Zachary VVakil Tashya ShreyasHa JuaMarti AlexSoto JamieDas DebajyotiMartinez-Lopez NuriaSharma ShipraDelgado YenniferPhung CallieAshley Immy AKapelczak Edmund DJacobo RashelWeatherford Eric TDai Dao-FuBenhammou Jihane NMarshall Andrea GHinton AntentorYang LingPereira Renata OTeSlaa TaraBouhaddou MehdiSingh RajatAbel E Dale