EPSP synthase antibody
- Known as:
- EPSP synthase (anti-)
- Catalog number:
- 10-1402
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Fitzgerald industries international
- Gene target:
- EPSP synthase antibody
Related genes to: EPSP synthase antibody
- 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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- 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 O-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 RELA, the gene encoding the NF-κB subunit p65. However, the mechanisms by which NF-κB pathways may affect O-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 C1GALT1 gene that encodes the enzyme responsible for galactosylation of IgA1 O-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 C1GALT1, suggesting that NF-κB pathway affects IgA1 O-glycosylation via SP1 transcriptional control of C1GALT1 expression. Furthermore, prolonged IΚΚβ 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 O-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 - Premature ovarian insufficiency (POI) is a major cause of infertility, yet its underlying mechanisms remain poorly understood. The double-mutant (DM) mouse, featuring oocyte-specific deletion of mannosyl (α-1,3-)-glycoprotein β-1,2-N-acetylglucosaminyltransferase (Mgat1) and core 1 β-1,3-galactosyltransferase (C1galt1), develops early-onset POI and offers a valuable system to investigate causes. This study explored whether autoimmunity leads to POI in DM mice. We transplanted control and DM neonatal ovaries into immunocompromised hosts. Three months post-transplantation, follicular development was assessed. While both DM and control ovarian grafts contained follicles, only control ovaries showed healthy progression through to the antral stage. In contrast, DM ovaries exhibited a marked developmental block at the primary stage. In DM follicles, oocytes were smaller, and granulosa cell (GC) number and area were reduced at all follicular stages present. There was a strong correlation between oocyte growth and GC proliferation in controls, but was weaker in DM, suggesting disrupted oocyte-somatic cell communication. Analyses showed strong anti-Müllerian hormone (AMH) in Control GCs, whilst DM levels were less than half of the control, indicating compromised GC function in DM ovaries. Forkhead box L2 (FOXL2) was also reduced in DM follicles compared to control GCs. The persistence of follicular defects, including reduced AMH and FOXL2 levels, in DM ovaries even in severe combined immunodeficient mice reveals that POI is not due to autoimmunity and the phenotype results from intrinsic defects in follicular development caused by the oocyte-specific mutation. These findings underscore the role of oocyte-GC interactions in follicle development and contribute to our understanding of POI pathogenesis. - Source: PubMed
Publication date: 2026/03/18
Kuscu NilayAppeltant RuthPetrovic SergejWilliams Suzannah A - Blunt abdominal trauma (AT) can cause significant intestinal injury and act as a trigger for remote posttraumatic organ dysfunction, including the development of multi-organ dysfunction syndrome (MODS). A deeper understanding of its impact on intestinal barrier integrity and immune regulation is essential for developing therapeutic strategies that support posttraumatic recovery. - Source: PubMed
Publication date: 2026/03/17
Meisen SophieRayatdoost FarahnazOßwald KatharinaPalmer AnnetteBreunig MarkusHuber-Lang MarkusHalbgebauer Rebecca - Protein glycosylation is an essential post-translational modification. In evolutionarily conserved mucin-type -glycosylation, the most common -glycan, T antigen, is synthesized by core 1 β1,3-galactosyltransferase 1 (C1GalT1). Loss of leads to developmental defects across organisms. We previously found that mutants exhibit malformed legs, but the underlying mechanism was unclear. Here, we identify a glycan-mediated inter-tissue signaling mechanism wherein embryonic hemocytes regulate leg morphogenesis. We show that T antigen-modified Papilin (Ppn), an extracellular matrix (ECM) protein secreted by embryonic hemocytes, suppresses JAK/STAT signaling in the epidermis surrounding Keilin's organ. This repression is essential for proper tubulogenesis of the peripodial stalk anchoring the leg disc and ensuring its correct positioning during development. Disrupted mucin-type -glycosylation impairs Ppn secretion and causes mislocalized leg discs and morphogenetic defects. These findings identify Ppn carrying mucin-type -glycan as long-range modulators of epithelial signaling and underscore the role of immune-like cells in coordinating organogenesis via ECM. - Source: PubMed
Publication date: 2026/02/18
Fuwa Takashi JItoh KazuyoshiIchimiya TomomiAkimoto YoshihiroNishihara Shoko