BTN2A1 Pre-design Chimera RNAi
- Known as:
- BTN2A1 Pre-design Chimera RNAi
- Catalog number:
- H00011120-R01
- Product Quantity:
- 20 nmol
- Category:
- -
- Supplier:
- Abno
- Gene target:
- BTN2A1 Pre-design Chimera RNAi
Related genes to: BTN2A1 Pre-design Chimera RNAi
- 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 Pre-design Chimera RNAi
Related articles to: BTN2A1 Pre-design Chimera RNAi
- 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 - Anti-GD2 monoclonal antibody effectively treats high-risk neuroblastoma (HR-NB) by recruiting NK cells for antibody-dependent cellular cytotoxicity (ADCC). We recently developed a cell product containing mature, cytotoxic γδ T and NK cells (GADEKILL), and its potential use as a novel immunotherapy for HR-NB has been investigated. - Source: PubMed
Publication date: 2026/01/30
Morandi FabioDella Lastra MartinaPastorino FabioCiampi EleonoraFaraci MauraBrignole ChiaraGiardino StefanoAiroldi Irma - Phosphoantigens (pAgs) are phosphate-containing small molecules that elicit an immune response. The pAgs bind to the intracellular domain of butyrophilin 3 (BTN3), enabling interactions with other butyrophilins to form complexes that trigger the T cell receptor (TCR) of Vγ9Vδ2 (γ9δ2) T cells. Despite multiple reports on this process, the conditions that regulate pAg levels leading to their detection remain unclear. Here we reveal a novel stress detection pathway, a type of lymphoid stress-surveillance response, in which mild cold stress triggers endogenous pAgs to engage with BTN family proteins, leading to the activation of γ9δ2 T cells. This stress response is dependent upon endogenous pAgs, as inhibition of HMG-CoA reductase abrogates the effect. It is also dependent upon BTN proteins, as depletion of BTN3A1 reduces the response. The ability of BTN2A1/BTN3A1 to respond is enhanced by the presence of BTN3A2 or BTN3A3. Furthermore, the internal domains of BTN2A1, BTN3A1, and BTN3A3 display differing abilities to dimerize, with BTN2A1 a constitutive dimer, BTN3A1 a monomer, and BTN3A3 a concentration dependent dimer. Full length BTN2A1/3A1 hybrid proteins additionally reveal that appropriately spaced multimers of BTN2A1 and BTN3A1 are critical in engaging the γ9δ2 TCR. In summary, our study uncovers a novel γ9δ2 T cell activation pathway mediated by cell stress and mevalonate pathway intermediates and highlights the critical roles of the BTN family members and their spacing in this process. - Source: PubMed
Publication date: 2026/01/22
Jin YimingNguyen KhiemBashir SidraPawge GirijaStrand Reagan MHsiao Chia-Hung ChristineVinogradova OlgaWiemer Andrew J