BTN2A1 Antibody (C-term) Blocking Peptide
- Known as:
- BTN2A1 Antibody (C-terminus) Blocking Peptide
- Catalog number:
- BP16288b
- Product Quantity:
- 2
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- BTN2A1 Antibody (C-term) Blocking Peptide
Related genes to: BTN2A1 Antibody (C-term) Blocking Peptide
- Gene:
- BTN2A1 NIH gene
- Name:
- butyrophilin subfamily 2 member A1
- Previous symbol:
- -
- Synonyms:
- BT2.1, BTF1, BTN2.1
- Chromosome:
- 6p22.2
- Locus Type:
- gene with protein product
- Date approved:
- 1999-08-27
- Date modifiied:
- 2016-10-05
Related products to: BTN2A1 Antibody (C-term) Blocking Peptide
Related articles to: BTN2A1 Antibody (C-term) Blocking Peptide
- Human γ9δ2 T cells detect microbial phosphoantigens (pAg) through butyrophilin (BTN) family proteins; however, how multiple BTN paralogs assemble into functional signaling complexes remains unresolved. Because γ9δ2 T cell activation requires coordinated action of several BTN members rather than a single receptor pair, defining their organization in living cells is essential. Here, we apply a live-cell NanoBRET saturation analysis using a novel HaloTag ligand to quantitatively resolve BTN oligomerization dynamics. We found that BTN3A1 exists as higher-order basal oligomers. Coexpression of BTN3A2 or BTN3A3 redistributes these assemblies into defined BTN3 dimers. The BTN3 dimers have a baseline interaction with BTN2A1 dimers that is altered by IgV domain interactions and by classical pAgs such as ()-4-hydroxy-3-methyl-but-2-enyl diphosphate. Mutation of a BTN3A1 IgV epitope disrupts a restraint on BTN2A1 and triggers spontaneous γ9δ2 T cell activation, which is independent of pAg. In contrast, BTN3A3 forms a strong, constitutive tetramer with BTN2A1 in the absence of BTN3A1/BTN3A2. This complex potentiates detection of nonclassical pAgs such as mevalonate diphosphate, and disruption of its juxtamembrane/B30.2 intersection abolishes both complex formation and signaling. BTN3A2 suppresses both interaction and function of BTN3A3 complexes, in contrast to its stimulatory effect on BTN3A1 complexes. Together, these results reveal that γ9δ2 T cell activation is controlled by ligand-dependent activation of competing BTN complexes. More broadly, this work establishes quantitative NanoBRET analysis as a general framework for dissecting multiprotein membrane receptor organization in living cells. - Source: PubMed
Publication date: 2026/06/18
Pawge GirijaBashir SidraParikh RitikaHsiao Chia-Hung ChristineWiemer Andrew J - The plasma proteomic signatures of sleep disturbance remain poorly characterized. Using data from 43,709 predominantly European-ancestry, middle-aged and older UK Biobank participants, we depict a large-scale atlas of plasma proteomic signatures of seven self-reported sleep traits (sleep duration, chronotype, insomnia symptoms, daytime napping, daytime sleepiness, snoring, and ease of getting up in the morning) and a derived sleep health score. We identify 935 proteins associated with at least one sleep trait, converging on lipid metabolism, immune function and inflammation, cell adhesion, and neurochemical signaling. Leveraging genomic structural equation modeling to define three latent sleep factors, namely circadian preference, daytime sleep burden, and nighttime sleep adequacy, bidirectional Mendelian randomization (MR) identifies one protein (LTA) with robust cis-instrument and strong colocalization support (PP.H4 = 0.98) for a putative causal effect on nighttime sleep adequacy. Sixteen additional genetically supported candidate proteins rely primarily on trans-pQTL instruments or weaker colocalization. These genetically supported candidates are prospectively associated with incident cardiovascular disease, stroke, type 2 diabetes, dementia, chronic kidney disease, depression, and mortality over a median 13.6-year follow-up, with the strongest per-SD hazard ratio (HR) associations observed for chronic kidney disease (e.g., BTN2A1: HR = 2.33) and type 2 diabetes (e.g., RBP5: HR = 1.58). Collectively, these findings highlight the potential of large-scale proteomics in elucidating sleep pathogenesis, and generate testable hypotheses for validation in independent cohorts and experimental models. - Source: PubMed
Publication date: 2026/06/11
Chen HanWang XuemeiChen WeiXu ChenjieTan XiaoCao Zhi - Metformin, a first-line anti-diabetic agent, exhibits broad-spectrum antitumor properties, though its underlying immunomodulatory mechanisms remain incompletely characterized. Here, we demonstrate that metformin significantly upregulates BTN3A1 and BTN2A1 expression on esophageal cancer cells in an AMPK-dependent manner, thereby sensitizing them to Vγ9Vδ2 T cell-mediated cytotoxicity. This molecular priming enhanced tumor immunogenicity, leading to synergistic tumor cell killing in vitro and potent suppression of tumor growth in xenograft models. Mechanistically, metformin-induced BTN3A1/BTN2A1 upregulation promoted Vγ9Vδ2 T cell activation, and Granzyme B-mediated apoptosis in tumor tissues. The combination therapy demonstrated excellent tolerability without observable systemic toxicity. Moreover, Integrating GEPIA3 database and clinical specimen analyses, we find that BTN3A1 and BTN2A1 are highly but heterogeneously expressed in esophageal cancer tissues, and that metformin‑mediated upregulation may restore sensitivity to Vγ9Vδ2 T cell immunotherapy particularly in patients with low baseline expression-uncovering a novel immunomodulatory function of metformin that provides a compelling rationale for its repurposing as a combinatorial agent against immunologically cold tumors such as esophageal carcinoma. - Source: PubMed
Publication date: 2026/06/06
Yang ZishanLiu YadiHan YixuanTan LijunWang SuliZhang ShenglanLi ChenyangHe PiaoyiZhang YaxinJi YilongYin ZhinanLi JianRen Feng - This study conducted a meta-analysis across three large European cohorts (UKBB, FinnGen, and REPAIR), including 12,660 rheumatoid arthritis (RA) cases, 2,446 radiographic axial spondyloarthritis (r-axSpA) cases, and over 530,000 shared controls. - Source: PubMed
Publication date: 2026/04/23
Cabrera-Serrano Antonio JoséCarretero-Fernández MaríaPérez-Rojo BegoñaTer Horst RobCañadas-Garre MarisaCanhão HelenaQuartuccio LucaSorensen Signe BGlintborg BenteFilipescu IleanaPérez-Pampin EvaConesa-Zamora PabloSwierkot Jerzyden Broeder Alfons Ade Vita SalvatoreBrix Petersen Eva RabingLi YangCoenen Marieke J HBogunia-Kubik KatarzynaAndersen VibekeFonseca João EuricoLund Hetland MereteLópez Nevot Miguel ÁngelLópez-Medina ClementinaReyes-Zurita Fernando JesúsNetea Mihai GEscudero AlejandroCáliz RafaelCollantes-Estévez EduardoSánchez-Maldonado José ManuelSainz Juan - Considering that the circulating proteome represents a primary source of candidate biomarkers and therapeutic targets, we conducted a large-scale Mendelian randomization (MR) study to identify plasma proteins potentially involved in the pathogenesis and treatment of common urological cancers (UCs), including bladder cancer (BC), prostate cancer (PC), renal cell carcinoma (RCC), and testicular cancer (TC). Cis-protein quantitative trait loci (cis-pQTLs) were derived from two large-scale genome-wide association studies (GWASs) of plasma proteomes. GWAS for UCs were obtained from FinnGen and pan-UKBB meta-analysis, FinnGen and UK Biobank. Colocalization analysis and summary data-based MR (SMR) were performed to evaluate the robustness of the associations. Further evaluations involved Bulk RNA-seq differential expression and single cell-type expression analysis, protein–protein interaction, and druggability evaluation. For BC, we identified four protein markers: one associated with increased risk (PSCA) and three with decreased risk (GSTM1, GSTM3, GSTM4), which are mainly expressed in pericyte, urothelial, and NK cells in bladder tumors. Regarding PC, we found 15 protein markers: seven linked to increased risk (AGER, ALAD, CHMP2B, PEX14, ZG16B, PPP1R14A, SERPINA3) and eight to decreased risk (BTN2A1, CEACAM21, DNAJB9, MSMB, PYGL, HLA-E, SOD2, TOR1AIP1), enriched in epithelial cells, monocytes/macrophages in prostate tumors. The strongest evidence from MR and colocalization analyses supported GSTM4 (BC), SOD2 and CHMP2B (PC) as causal markers. Notably, seven identified proteins have been previously targeted by drugs for other cancers and immune disorders, indicating their potential therapeutic relevance in UCs. This study highlights several proteins with predictive value for BC and PC risk and supports their utility in biomarker discovery and drug development. - Source: PubMed
Publication date: 2026/04/27
Lyu XinyiPeng LiaoFan YangXiong YangXu XueyuanChen JiaweiLiu MengzhuChen YuanzhuoZhang ChiYang ShiqinShen SihongZhang JieZeng XiaoShen HongQin FengLin YifeiLuo Deyi