B3GNT2
- Known as:
- B3GNT2
- Catalog number:
- Y213783
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- B3GNT2
Related genes to: B3GNT2
- Gene:
- B3GNT2 NIH gene
- Name:
- UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2
- Previous symbol:
- B3GNT1
- Synonyms:
- B3GNT-2, BETA3GNT, B3GN-T2, B3GN-T1
- Chromosome:
- 2p15
- Locus Type:
- gene with protein product
- Date approved:
- 2001-05-14
- Date modifiied:
- 2017-01-17
Related products to: B3GNT2
Related articles to: B3GNT2
- The richness of our somatosensory experience is reflected in the functional diversity of somatic sensory neurons. Single-cell RNA sequencing of sensory neurons has revealed a molecular basis for such diversity. However, sensory neuron diversity has yet to be captured at the level of the proteome. Here, we combined electrophysiology with deep visual proteomics to quantify over 6000 proteins from phenotypically-defined sensory neurons in mice and identified proteomic markers of sensory neuron subtypes. Comparative analysis revealed both concordance and meaningful divergence between transcriptomes and proteomes. We further show that up to 3000 proteins can be quantified from one-fourth of a single neuron, demonstrating subset-specific protein signatures. In culture, nociceptive neurons can be acutely sensitized to mechanical stimuli by nerve growth factor (NGF) which normally drives inflammatory pain in vivo. Indeed, overnight exposure of peptidergic nociceptors to NGF and a protein kinase C (PKC) activator produced functional sensitization associated with proteome changes. Functional knockdown experiments identified the up-regulated B3GNT2 enzyme as a potential effector of nociceptor sensitization. In summary, we present a high-resolution proteomic resource linking molecular identity to function, enabling the discovery of mechanisms underlying somatic sensation and pain sensitization. - Source: PubMed
Publication date: 2026/04/11
Chakrabarti SampurnaMakhmut AnuarMohammadi AtenaLuo WenhanWang LinLewin Gary RCoscia Fabian - Most causal variants for complex diseases are expected to affect gene regulation in a cell- and context-specific manner. Hence, identification of such dynamically functioning variants requires functional readouts in disease-relevant tissues and context. In this study, we prioritized causal variants for psoriasis by adding functional annotations from disease-relevant cells. We demonstrate that disease-relevant immune cells, unlike most other tissues, possess functional annotations that match candidate causal SNPs. Specifically, we identified an eQTL, rs4672505, that reduces B3GNT2 gene expression only in Th1/Th17 cells with a memory phenotype, i.e., antigen-experienced T helper cells. This eQTL, a likely causal variant, also matched an enhancer chromatin mark exclusive to memory T helper cells and absent in other tissues. A disease-risk allele A at the eQTL correlates with reduced expression of the B3GNT2 glycosyltransferase. B3GNT2 deficiency in murine models reduces the glycosylation of the CD28 co-receptor involved in the CD28/B7 co-stimulation pathway and results in increased T cell activation upon antigen stimulation. We hypothesize that the risk allele A in patients increases the activation of memory Th1/Th17 cells upon re-exposure to antigens, which constitutes "signal 1". Increased reactivity to antigens depends on "signal 2" via CD28/B7 co-stimulation from antigen-presenting cells that need to encounter microbial products. Hence, this genetic risk mechanism lies at the nexus of the response to specific antigens and microbial exposure, for instance, infection or vaccination, both of which are known to exacerbate psoriasis. - Source: PubMed
Publication date: 2026/03/11
Yunusbayev BayazitRyakhovsky SergeiAltinbaev RadickKislova AnastasiaDanilko KseniyaKraeva LiudmilaYunusbaeva Milyausha - Adenomyosis is a chronic gynecological disorder characterized by the invasion of endometrial tissues into the myometrium of the uterus, with pathophysiology linked to chronic inflammation and metabolic dysregulation. However, the understanding of the molecular mechanisms and underlying pathologies remains limited. This study aims to elucidate the metabolic reprogramming and immune dysregulation within the eutopic endometrium from patients diagnosed with adenomyosis, and identify potential therapeutic targets or diagnostic indicators. - Source: PubMed
Publication date: 2025/11/20
Bian XuejiaoSun ZheLai JunliangLi BoyuDong XinyiGuan HengyuVankelecom HugoSun Yun - Human induced pluripotent stem cell (iPSC)-derived neurons are often heterogeneous, posing challenges for disease modeling and cell therapy. We previously developed single-cell glycan and RNA sequencing (scGR-seq) to analyze the glycome and transcriptome simultaneously. Here, we applied scGR-seq to examine heterogeneous populations of human iPSC-derived neurons. We identified four subpopulations: mature neurons, immature neurons, undifferentiated neural progenitor cells (undiffNPCs), and mesenchymal cells (MCs). Lectin-binding patterns indicated high α1,3-fucose expression in undiffNPCs. MCs exhibited strong binding of a poly-LacNAc-recognizing lectin (rLSLN) and high expression of B3GNT2, a poly-LacNAc synthetic enzyme. Pseudotime analysis revealed that a subpopulation of NPCs acquired mesenchymal features and differentiated into MCs. Immunocytochemistry confirmed the specific detection of undiffNPCs and MCs using anti-Lewis X (α1,3-fucosylated glycan) antibodies and rLSLN. Beyond identifying cell heterogeneity, scGR-seq enables the discovery of glycan markers and detection probes for iPSC-derived cells, aiding in their further cell processing and manipulation. - Source: PubMed
Publication date: 2025/09/04
Odaka HarukiTateno Hiroaki - Sulfation of -acetylglucosamine (GlcNAc) moieties of glycans is a common modification that has been implicated in many biological and disease processes. Glycans having sulfate replaced by a stable analogue may find use as glycomimetic drugs. Here, we describe the synthesis of analogues of UDP-GlcNAc in which C-6 hydroxyl is replaced by a thiol or disulfide-protected thiol. It was found that UDP-GlcNAc-6-deoxy-6-SH is a donor substrate for GCNT1 and UDP-GlcNAc-6-deoxy-6-S-SMe for B3GnT2, allowing the preparation of glycopeptides and oligo-LacNAc derivatives having a GlcNAc-6-deoxy-6-S- moiety, respectively. The disulfide can be reduced to a thiol, which can easily be oxidized to the corresponding sulfonates. Furthermore, oligosaccharides having a sulfonate or disulfide at C-6 are appropriate substrates for glycosyltransferases, providing access to a panel of glycomimetics. The sulfonates and several reference glycans and glycopeptides were printed as a glycan microarray that was used to examine binding selectivities of several lectins, Siglecs, and hemagglutinins of influenza A viruses. It was found that sulfonates can either be tolerated, enhance binding as in the case of Siglec-4, or abolish recognition as for Siglec-9. Molecular modeling studies of the complex of Siglec-4 with sulfated and sulfonated sialyl LacNAc indicate that plasticity of the binding site of the protein and a great charge on oxygens of a sulfonate are responsible for the higher binding affinity. Introduction of a 6-sulfonate gives better step economy than conventional enzymatic sulfation, is simpler to operate, provides compounds resistant to hydrolysis by sulfatases, and can modulate binding selectivities. - Source: PubMed
Publication date: 2025/06/15
Wu YunfeiWeber JuliaKimpel Anne L MUnione LucaUslu Elifde Vries Robert PBoons Geert-Jan