FUT8 antibody Polyclonal Antibodies Primary antibodies
- Known as:
- FUT8 (anti-) Polyclonal Antibodies Primary antibodies
- Catalog number:
- orb100150
- Product Quantity:
- 100
- Category:
- -
- Supplier:
- Biorb
- Gene target:
- FUT8 antibody Polyclonal Antibodies Primary antibodies
Related genes to: FUT8 antibody Polyclonal Antibodies Primary antibodies
- Gene:
- FUT8 NIH gene
- Name:
- fucosyltransferase 8
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 14q23.3
- Locus Type:
- gene with protein product
- Date approved:
- 1997-12-23
- Date modifiied:
- 2016-10-05
Related products to: FUT8 antibody Polyclonal Antibodies Primary antibodies
Related articles to: FUT8 antibody Polyclonal Antibodies Primary antibodies
- Glycosyltransferases that biosynthesize glycans and their genes (glycogenes) play important roles in health and disease. In general, pathophysiological changes are defined by comparing knock-out (KO) or knock-in mice generated using CRISPR-Cas9 and other technologies to normal mice. Next, target molecules such as glycoproteins, glycolipids, and proteoglycans to which various biosynthetic glycans bind were identified. As a result, we found that N-glycan branches biosynthesized by glycosyltransferases are intrinsically involved in Alzheimer's disease, cancer metastasis, epithelial mesenchymal transition (EMT)/mesenchymal epithelial transition (MET), type 2 diabetes, chronic obstructive pulmonary disease (COPD), and ulcerative colitis. For example, the addition of core fucose biosynthesized by α1,6-fucosyltransferase (Fut8) leads to dysregulation of TGF-β receptors. Bisecting N-acetylglucosamine (GlcNAc) biosynthesized by β-1,4-GlcNAc transferase III (GnT-III) affects the subcellular localization of Beta-site Amyloid Precursor Protein Cleaving Enzyme 1 (β-secretase 1, referred to as BACE1). β1,6GlcNAc branching biosynthesized by GnT-V leads to the modification of matrix metalloproteinase (MMP). Identification and characterization of N-glycan structures on these proteins were performed using a glycoproteomic approach based on lectin blotting, western blotting, liquid chromatography-electron spray ionization mass spectrometry, and histochemical staining. Recently, studies concerning redox regulation of N-glycans, termed Glyco-Redox, have emerged as a promising approach. Functional and pathophysiological glycan studies are one of the main goals of glycobiology research. In this review, we describe the role of N-glycan branching glycosyltransferases and their biosynthesized glycans in relation to various diseases, such as cancer metastasis, COPD, Alzheimer's disease, and ulcerative colitis. - Source: PubMed
Publication date: 2026/03/17
Taniguchi NaoyukiOhkawa YukiNakano MiyakoGu JianguoTakahashi Motoko - Core fucosylation, a critical post-translational modification mediated by α1,6-fucosyltransferase (Fut8), is vital in regulating cellular functions and signaling pathways. This glycosylation process is particularly significant in the context of the central nervous system (CNS), where it influences neurodevelopment, synaptic functionality, and the neuroinflammatory response. Aberrations in core fucosylation have been implicated in the pathogenesis of various neuroinflammatory conditions, underscoring its potential as a therapeutic target for neurological disorders. Core fucosylation affects several important signaling molecules and receptors, such as the transforming growth factor-β (TGF-β) receptor, vascular endothelial growth factor receptor (VEGFR), epidermal growth factor receptor (EGFR), integrins, and glycoprotein 130 (gp130). These molecules are essential for maintaining CNS homeostasis and responding to injury or disease. Furthermore, the dysregulation of core fucosylation has been associated with altered microglial and astrocytic responses to inflammatory stimuli, affecting the progression of neurodegenerative diseases. The modulation of core fucosylation pathways presents a promising avenue for developing novel therapeutic strategies to control neuroinflammation and improve outcomes in patients with neurodegenerative disorders. In conclusion, the intricate relationship between core fucosylation and neuroinflammation offers insights into the molecular mechanisms underlying CNS pathologies and highlights the importance of further research in this area to identify new targets for therapeutic intervention. - Source: PubMed
Xu XingFukuda TomohikoGu Jianguo - Clear cell renal cell carcinoma (ccRCC) is characterized by the loss of the von Hippel-Lindau (VHL) gene, leading to constitutive activation of hypoxia-inducible transcription factors (HIFs) and metabolic reprogramming toward aerobic glycolysis. Although core fucosylation catalysed by fucosyltransferase 8 (FUT8) is known to regulate receptor signaling and tumor malignancy, its role in metabolic regulation of ccRCC remains poorly defined. Here, we demonstrate that FUT8 knockdown significantly suppresses ccRCC proliferation and migration both in vitro and in vivo. Mechanistically, FUT8 enhances HIF-1α-driven glycolysis, increasing lactate production and promoting pan-lysine lactylation (pan-Kla). Specifically, FUT8 promotes pyruvate kinase M2 (PKM2) K115 lactylation, which boosts its enzymatic activity while reducing nuclear localization, thereby driving epithelial-mesenchymal transition and malignant progression. Collectively, our findings reveal the FUT8-HIF-1α-lactate-PKM2 axis as a key mechanism that links core fucosylation to metabolic reprogramming and malignant progression in ccRCC and highlights FUT8 as a promising therapeutic target. - Source: PubMed
Publication date: 2026/03/19
Guo ZikaiJiang HongxiaoWang XuXuan KeZhong HuidongLiu ChengxiZhang MengkaiLi ZhichaoHuang WeirenSun Yangyang - Glycosylation is a critical post-translational modification of proteins. The proper function and expression of cell-surface proteins-including receptors, transporters, and cell adhesion molecules-depends on glycosylation. Among the various forms of glycosylation, core fucose applied to N-glycans exhibits distinctive characteristics and plays a significant role in numerous biological processes. Here, we focus on the molecular targets of core fucose and review their functions involved in inflammatory signaling pathways and immune systems. Cytokine receptors and toll-like receptors are important targets of core fucosylation. Additionally, core fucosylation of immunoglobulin G (IgG) plays a significant role in regulating antibody-dependent cellular cytotoxicity (ADCC). Recent studies-including ours-also indicate that the level of core fucose of IgG could serve as a valuable biomarker for monitoring inflammatory status in individuals. Modulation with monosaccharide fucose is a small event for the target molecules, but core fucose exerts a significant impact on inflammation. - Source: PubMed
Publication date: 2026/03/13
Ohkawa YukiAbe JunpeiKuribara TaikiTaniguchi Naoyuki - High-grade serous ovarian cancer (HGSC) is the most aggressive subtype of ovarian epithelial cancer (OEC), with characters of late-stage diagnosis, high recurrence rate, and poor survival outcomes. Fucosyltransferase 8 (FUT8) is responsible for α1,6-core fucosylation biosynthesis, and aberrant FUT8/α1,6-core fucosylation level is involved in tumor progression. However, the roles and mechanisms of protein FUT8 and α1,6-core fucosylation in HGSC tumorigenesis and progression remain elusive. Here, our study confirms that elevated levels of FUT8/α1,6-core fucose in the tissues and serum of HGSC patients, and the elevation is associated with poor patient prognosis. By applying glycoproteomic assay, we globally screen and identify NCEH1 as the specific scaffold protein of α1,6-core fucosylation. Alpha 1,6-core fucose modification stabilizes NCEH1 by preventing its degradation through proteasomal pathway. Importantly, combined with non-targeted metabolomics analysis, α1,6-core fucosylated NCEH1 facilitates LPA secretion, driving M2-like polarization of tumor-associated macrophages in the tumor microenvironment, thus leading to oncogenesis and peritoneal metastasis of HGSC in vitro and in vivo. These findings broaden the understanding of FUT8/α1,6-core fucosylation/NCEH1 in HGSC progression and metastasis, and offer glycosylated diagnostic indicators and targets for therapeutic strategies in HGSC. - Source: PubMed
Publication date: 2026/03/05
Pei XiaoSongWang FeiLiu XiaominLei YuyuChen YuLiu BoSun RuixuanLi PeiyuBi JianleiLiu Shuai