Mouse Anti Human CD57 FITC CD57 FITC
- Known as:
- Mouse Anti Human CD57 fluorecein CD57 fluorecein
- Catalog number:
- ant-289
- Product Quantity:
- 500
- Category:
- -
- Supplier:
- Prospecbio
- Gene target:
- Mouse Anti Human CD57 FITC
Related genes to: Mouse Anti Human CD57 FITC CD57 FITC
- Gene:
- B3GAT1 NIH gene
- Name:
- beta-1,3-glucuronyltransferase 1
- Previous symbol:
- CD57, LEU7
- Synonyms:
- GlcAT-P, HNK-1, NK-1
- Chromosome:
- 11q25
- Locus Type:
- gene with protein product
- Date approved:
- 2000-01-07
- Date modifiied:
- 2014-11-19
Related products to: Mouse Anti Human CD57 FITC CD57 FITC
Related articles to: Mouse Anti Human CD57 FITC CD57 FITC
- - Source: PubMed
Publication date: 2026/04/21
Wang JiagangZhu LifanWeng FengbiaoZeng JincaiXu LiangChen YuweiShi Yuhui - N-glycans are essential components of glycoproteins, influencing their properties and functions. While biochemical pathways of glycosylation are well-characterized, their genetic regulation remains poorly understood. This study utilizes matrix-assisted laser desorption/ionization-mass spectrometry (MALDI-MS) and ultra-high performance liquid chromatography-fluorescence detection (UHPLC-FD) to strengthen replication and further characterize previously identified genome-wide association signals for the total human plasma N-glycome (TPNG). Univariate and multivariate genetic association meta-analyses involved 3385 samples across 143 N-glycome traits from the Hoorn Diabetes Care System and DiaGene cohorts as well as 3224 samples across 117 N-glycome traits from TwinsUK, CEDAR, QMDiab and SABRE cohorts. We successfully replicated ten previously identified but not replicated glycosylation quantitative trait loci (glyQTLs) and prioritized five high-confidence putative causal genes, including the glycosyltransferase MGAT4B and inflammation-related genes - C3 and FCGR2B. The linkage-specific sialic acid derivatization in MALDI-MS enabled delineation of genetic effects on α2,3- and α2,6-sialylation. Mass spectrometry analysis, triggered and guided by association to a locus containing B3GAT1 glucuronosyltransferase, provided evidence for hexuronic acid-containing glycans in human blood plasma. These findings advance our understanding of the genetic regulation of protein N-glycosylation and highlight the complementarity of different analytical approaches in glycomics research. - Source: PubMed
Publication date: 2026/04/20
Timoshchuk AnnaNaber AnnemiekeSlieker RoderickSoplenkova AnnaMaslov DenisPotapova Nadezhda ANicolardi SimoneElders P J MSijbrands Eric J GSharapov SodboHart Leen M 'tHoek MandyWuhrer ManfredAulchenko Yurii S - Mammalian cells are decorated with a large variety of glycans. Although the biosynthetic enzymes for most glycan structures have been identified, it remains unclear how glycan levels are regulated in cells. Recently, some cellular glycans and their biosynthetic enzymes were found to be loaded into a subset of small extracellular vesicles (sEVs) and transferred to recipient cells, suggesting uncharacterized sEV-mediated mechanisms for glycan remodeling. Here, we found that a brain-specific glycan involved in learning and memory, human natural killer-1 (HNK-1), and its major biosynthetic enzyme, GlcAT-P (B3GAT1), are included in sEVs. Size exclusion chromatography and immunoisolation experiments suggested that the sEVs containing GlcAT-P and glycoproteins with HNK-1 are similar in size but distinct from the tetraspanin-rich sEV subtype. We also found that GlcAT-P in the sEVs is a cleaved form and enzymatically active. Incubation of the HNK-1- and GlcAT-P-loaded sEVs rendered recipient cells positive for HNK-1, whereas sEVs containing GlcAT-P but not HNK-1 did not induce HNK-1 expression in the recipient cells, suggesting that the transfer of HNK-1 but not its biosynthetic enzyme is necessary for recipient cells to be positive for HNK-1. Our findings shed light on a non-genetic pathway for increasing the level of a specific neural glycan via sEV-mediated cell-cell communication. - Source: PubMed
Publication date: 2026/01/12
Tokoro YukoKizuka Yasuhiko - The glycocalyx serves as the skeletal structure of the outer layer of endothelial cells and regulates the function of endothelial cells. Porphyromonas gingivalis (P. gingivalis) outer membrane vesicles (OMVs) exhibit the fundamental biological traits of bacteria, such as inducing inflammatory responses, damaging host cells, and delivering virulence factors to distal tissues like the cardiovascular system. This study aimed to investigate the role of P. gingivalis OMVs in vascular endothelial glycocalyx injury. - Source: PubMed
Publication date: 2026/01/09
Yin ShouchengQiao QihuiLi ZhaorongLu LijieJiang MuzhouGao HanyuGe ZimingLi ChenPan YapingLin Li - Glioma is an immunologically evasive tumor with a lymphocyte-deficient tumor immune landscape, suggesting an unknown failure in tumor-stroma interaction. The human natural killer-1 glycan (HNK-1) is present on neurons and immune cells, suggesting a potential source of glioma-stroma interaction, cross-talk, and immune regulation. Immunohistochemical staining of a human glioma microarray showed that HNK-1 progressively decreased with increasing tumor grade. However, similar immunohistochemical staining for β-1,3-glucuronic acid transferase (B3GAT1), the predominant enzyme responsible for HNK-1 synthesis, showed no change with glioma progression, indicating that the loss of HNK-1 was not due to changes in B3GAT1 expression. However, Kaplan-Meier analysis showed that B3GAT1 levels positively correlated with survival. In the syngeneic GL261 murine glioblastoma model, HNK-1 knockdown by two B3gat1 shRNAs accelerated glioma growth and reduced mouse survival in vivo. B3gat1-knockdown tumors had increased numbers of regulatory T cells, and decreased numbers of effector CD8 T cells, which correlated with increased CD8 T-cell apoptosis. In co-cultures of CD8 T cells with B3gat1-knockdown GL261 cells, we observed reduced T-cell-induced glioma Ca signaling and intracellular perforin accumulation, along with increased perforin release into the culture medium, compared to CD8 T-cell co-culture with wild-type GL261 cells. FACS analysis showed loss of co-stimulatory CD80, an immune synapse component, following B3gat1 knockdown. These results suggest that loss of HNK-1 expression contributes to tumor immune escape through loss of immune recognition and attack via downregulation of tumor cell surface co-stimulatory molecules, leading to reduced CD8 T-cell activation and immune synapse formation, and increased T-cell apoptosis. - Source: PubMed
Publication date: 2025/12/02
Duan JinLin YilinHe ZeweiSchachner MelittaLin Stanley L