Mouse Anti Human CD57 CD57
- Known as:
- Mouse Anti Human CD57 CD57
- Catalog number:
- ant-287
- Product Quantity:
- 500
- Category:
- -
- Supplier:
- Prospecbio
- Gene target:
- Mouse Anti Human CD57
Related genes to: Mouse Anti Human CD57 CD57
- 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 CD57
Related articles to: Mouse Anti Human CD57 CD57
- Natural killer (NK) cells are effector cells of the innate immune system. The cytokine microenvironment influences NK cell function. Dysregulation of NK cell cytotoxicity can manifest in reproductive disorders and is also observed in tumor-transformed tissues. The search for immunotherapies capable of regulating NK cell activity is therefore relevant. This study aimed to evaluate the effect of the TGFβ signaling pathway inhibitor and the cyclin-dependent kinase (CDK) 7/12/13 inhibitor on the transcriptional profile of NK-92 cell line. In the study, the cytokines TGFβ1, IL-12, IL-15, IL-18, and TNFα, and the TGFβ receptor type 1 (TGFβR1) inhibitor LY3200882 and the CDK7/12/13 inhibitor THZ1 were used. The cells were cultured sequentially in the presence of inhibitors and cytokines, followed by assessment of the gene expression of , , , , , , , , , , and We observed direct effects of the inhibitors on NK cells. LY3200882 increased the expression of and , and reduced . THZ1 increased the expression of , , and , while it reduced and . IL-12, IL-15, IL-18, and TNFα modified the gene expression of some phenotypic and cytotoxic receptors and transcription factors. TGFβ1 increased the expression of , , and . Blocking TGFβ-dependent signaling with LY3200882 abolished TGFβ1 effects. We assessed CD56 presence on NK-92 cell membrane and found its increase in the presence of LY3200882. After LY3200882 treatment, in the presence of TGFβ1 and choriocarcinoma cell line JEG-3, the expression of CD56 receptor on NK cell membrane decreased. Pretreating NK cells with THZ1 decreased the expression of , , and in the presence of TGFβ1. Thus, LY3200882 partially neutralized TGFβ1 effects on the expression of NK cell receptor genes. THZ1 followed by TGFβ1 treatment promoted NK cell transcriptional profile characteristic for CD56dim NK cells. Both LY3200882 and THZ1 affected the NK cell transcription even without cytokine treatment. The independent effects of synthetic inhibitors on NK cells, as well as their influence in the presence of tumor cells, should be considered. - Source: PubMed
Publication date: 2026/04/17
Mikhailova ValentinaMarko OksanaMkrtchyan EdgarSokolov Dmitry - - 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