Porcine Thromboxane synthase ELISA kit
- Known as:
- Porcine Thromboxane synthase Enzyme-linked immunosorbent assay test reagent
- Catalog number:
- e07t0553
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Blue gene shanghai
- Gene target:
- Porcine Thromboxane synthase ELISA kit
Related genes to: Porcine Thromboxane synthase ELISA kit
- Gene:
- C1GALT1 NIH gene
- Name:
- core 1 synthase, glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- Previous symbol:
- -
- Synonyms:
- C1GALT, T-synthase
- Chromosome:
- 7p22.1-p21.3
- Locus Type:
- gene with protein product
- Date approved:
- 2005-01-26
- Date modifiied:
- 2018-02-13
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- Aberrant mucin-type O-glycosylation is a common feature of pancreatic ductal adenocarcinoma (PDAC), yet its functional contribution to pancreatic tumorigenesis remains incompletely defined. In particular, whether defective core 1 O-glycan maturation cooperates with oncogenic KRAS during early pancreatic neoplasia has not been fully resolved. Here, we addressed this question by deleting Cosmc (C1galt1c1), the obligate molecular chaperone for T-synthase (C1galt1), in a pancreas-specific Kras-driven mouse model. Analysis of human PDAC tissue microarrays revealed frequent expression of the truncated O-glycan epitopes Tn and sialyl-Tn, supporting the clinical relevance of impaired O-glycan elongation in pancreatic cancer. In vivo, pancreas-specific Cosmc loss in the setting of oncogenic Kras accelerated pancreatic tumor progression, enhanced tissue proliferation, altered acidic mucin-associated glycosylation, and promoted pronounced stromal remodeling. Lectin histochemistry and biochemical analyses confirmed robust accumulation of Tn antigen in Cosmc-deficient pancreatic tumors. To define molecular programs associated with this phenotype, we performed transcriptomic and proteomic profiling of tumor-derived PDAC cell lines together with VVA-enriched glycoproteomic analysis of pancreatic tissues and cell lines. These approaches identified coordinated remodeling of pathways linked to extracellular matrix organization, adhesion, cytoskeletal regulation, stress adaptation, and metabolic reprogramming. Together, these data identify Cosmc-dependent O-glycosylation as a regulator of Kras-driven pancreatic carcinogenesis. Our findings support a model in which truncated O-glycans contribute to PDAC progression in association with remodeling of the tumor glycoproteome and stromal architecture during Kras-driven pancreatic tumor evolution. - Source: PubMed
Publication date: 2026/07/31
Mercanoglu BarisSchraps NinaGiannou Anastasios DZhou JingxuanKind SimonReinecke MayaKarstens Karl-FrederickDreyer BenjaminHarder SönkeZhang SiwenPapazoglou Eleftherios DGüngör CenapMelling NathanielSchlüter HartmutWagener ChristophBockhorn MaximilianHackert ThiloWolters-Eisfeld Gerrit - The mucin barrier is essential for postnatal gut homeostasis, but whether galacto-oligosaccharides (GOS) regulate mucin glycosylation remains unclear. Here, we investigated the effects of early-life GOS supplementation on mucin -glycans and intestinal barrier development in piglets using UPLC, MALDI-TOF-MS, immunofluorescence, lectin staining, and histomorphological analyses. GOS supplementation significantly increased jejunal villus width, mucosal thickness, goblet cell numbers, and MUC2 expression during early life. Glycomic profiling revealed selective remodeling of mucin -glycans, characterized by increased core 1/3 and α2,3-sialylated glycans and reduced core 2/4 and α2,6-sialylated structures. These alterations were accompanied by upregulation of , , and , and downregulation of and . Lectin staining further confirmed enhanced α2,3-sialylation and reduced α2,6-sialylation. Collectively, these results demonstrate that dietary GOS promotes intestinal barrier development and selectively modulates the composition and sialylation of mucin -glycans, providing novel mechanistic insight into how prebiotics support gut health in early life. - Source: PubMed
Publication date: 2026/06/12
Xu LaipengLi XuanFan WenluSun WeileMeng ChengmingLiu LiVoglmeir JosefMu ChunlongZhu Weiyun - Black soldier fly larvae (Hermetia illucens L., BSFL) efficiently degrade lignocellulosic waste despite lacking endogenous lignocellulolytic enzymes, indicating a critical dependence on gut-associated microbiota. However, how BSFL are associated with the enrichment and spatial organization of lignocellulose-degrading symbionts within the gut remains poorly understood. - Source: PubMed
Publication date: 2026/06/09
Xiang Fang MingTang Xiao TianBrandón María GómezHenawy Ahmed RJiang ShuoYunXu XinHuaChen XueXinZhang ZhiJian - IgA nephropathy (IgAN) is a common primary glomerulonephritis characterized by glomerular immune-complex deposits with (co)dominant IgA. These deposits are enriched for IgA1 glycoforms with some -glycans deficient in galactose (Gd-IgA1). Circulating Gd-IgA1 is bound by IgG autoantibodies to form immune complexes, some of which deposit in glomeruli. Genomic and immunologic studies indicate involvement of pro-inflammatory signaling pathways in the production of Gd-IgA1 in IgAN. Genomic studies identified multiple genetic loci associated with IgAN and suggested a convergence on the NF-κB pathway, including , the gene encoding the NF-κB subunit p65. However, the mechanisms by which NF-κB pathways may affect -glycosylation in IgA1-producing cells are unknown. Using EBV-immortalized B cells derived from peripheral-blood mononuclear cells of IgAN patients and healthy controls that have constitutively activated NF-κB, we report that inhibition of NF-κB/p65 by a selective IKKβ inhibitor TPCA-1 reduced phosphorylation of NF-κB/p65 at S536 and decreased production of IgA1 and, conversely, increased Gd-IgA1 production. This was likely related to reduced expression of gene that encodes the enzyme responsible for galactosylation of IgA1 -glycans. Flow-cytometry imaging revealed changes in nuclear translocation and co-localization of the NF-κB/p65 with co-transcriptional factor SP1, a transcriptional activator of , suggesting that NF-κB pathway affects IgA1 -glycosylation via SP1 transcriptional control of expression. Furthermore, prolonged IKKβ inhibition altered B cell subpopulations, enhancing generation of cells with a plasmablast-like phenotype, characterized by high SSC MFI and CD138 expression. Together, these findings provide functional evidence for involvement of NF-κB/p65 and its transcriptional partners in IgA1 -glycosylation. - Source: PubMed
Publication date: 2026/05/05
Person TaylorPhillips MaggieRice TerriHall StacyJulian Bruce ARizk Dana VNovak JanReily Colin - Aberrant O-linked glycosylation of the IgA hinge segment resulting in galactose-deficient IgA1 (Gd-IgA1) is frequently observed in patients with IgA nephropathy (IgAN), and it is hypothesized to be pathogenic. Here, we genetically disrupted the expression of galactosyltransferase 1 (C1galt1) to elevate Gd-IgA1 levels in mice and examine its role in glomerular deposition. - Source: PubMed
Publication date: 2026/03/27
Wu JingyiXie TongZhang ZhaoLiu XingziZhou XujieZhang YongTian WenminGale Daniel PZhu ShuBarratt JonathanJin JingZhang YuemiaoZhang HongLv Jicheng