A4GALT
- Known as:
- A4GALT
- Catalog number:
- 000858A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- A4GALT
Related genes to: A4GALT
- Gene:
- A4GALT NIH gene
- Name:
- alpha 1,4-galactosyltransferase (P blood group)
- Previous symbol:
- P1
- Synonyms:
- A14GALT, Gb3S, P(k)
- Chromosome:
- 22q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 2002-02-06
- Date modifiied:
- 2019-04-23
Related products to: A4GALT
Related articles to: A4GALT
- Tumor lipid metabolism has emerged as a critical, yet underexplored, determinant of cancer progression with clinical and prognostic importance. A membrane lipid species of particular interest is globotriaosylceramide (Gb/CD77), a glycosphingolipid that serves as cellular receptor for the bacterial Shiga toxins, and is upregulated in various malignancies. While preclinical studies have suggested a pro-tumorigenic role for Gb, the regulatory drivers of its biosynthesis in human tumors have remained elusive. - Source: PubMed
Publication date: 2026/01/27
Hirsch Noah-DavidPerl MarkusHolzinger SimonBarz ChristophEnßle StefanJohannes WidyaConrad AnjaUnterholzner Jonas JObermeier ViktoriaTschurtschenthaler MarkusJohannes LudgerJanssen Klaus-Peter - The P1PK blood group system in humans, composed of three glycosphingolipid antigens, plays a significant role in transfusion medicine. These antigens are synthesized by the enzyme α1,4-galactosyltransferase, encoded by the A4GALT gene, and also act as receptors for Shiga toxins, which are key virulence factors produced by pathogenic strains of Escherichia coli. Birds are known to be resistant to the effects of Shiga toxins, yet the molecular basis of this resistance has remained unclear. This study aimed to investigate the presence, expression, and functional role of P1PK antigens in birds, particularly in relation to their exposure to human-associated bacteria. - Source: PubMed
Publication date: 2025/12/17
Bereznicka AnnaDuk MariaKapczynska KatarzynaModlinska AnnaPiasecki TomaszLink-Lenczowski PawełHeidorn-Czarna MałgorzataPasikowski PawelCzerwinski MarcinKaczmarek Radoslaw - The rare p phenotype, characterized by the absence of P, P1, and P antigens, produces anti-PP1P that can cause severe hemolytic reactions and recurrent miscarriages. This phenotype is rare globally but shows notable prevalence in the Swedish population. This study focuses on the molecular characterization of 6 Indian patients to provide further insight into the genetic basis of the p phenotype. - Source: PubMed
Publication date: 2025/10/02
Kshirsagar PoojaRaval GouthamBhatnagar NidhiBonagiri ShanthiNoushad ShahidaMadkaikar ManishaKulkarni Swati - - Source: PubMed
Publication date: 2025/12/08
Jin YuelinLi TongtongYang JinlinWu QileiDeng HongSu ShengyeJia ShuangshuangLiu KaiqiangJi Yanli - Glycosylation of proteins can impact their folding, stability, trafficking and enzymatic activity. Human Gb3/CD77 synthase (α1,4-galactosyltransferase, A4galt) has two occupied N-glycosylation sites. Previously, we demonstrated that the activity of recombinant enzyme relies on its N-glycosylation. In this study, we produced soluble recombinant catalytic domain of human Gb3/CD77 synthase in two expression hosts known for different glycosylation patterns: Trichoplusia ni insect cells (High Five) and human embryonic kidney cells (Expi293F™). The High Five cells generate short oligomannose structures, while the Expi293F™ cells synthesize complex type glycans. We evaluated the activity of High Five-derived and Expi293F™-derived enzymes, characterized the structures of their N-glycans and showed that High Five cells provide a higher amount and activity of the enzyme. Moreover, we used the Expi293F™ cells to evaluate the N- and C-terminal location of the 6xHis-tag and found that only the N-terminally tagged Expi293F™-derived enzyme demonstrated activity. In contrast, the enzyme produced in High Five cells was active despite carrying a C-terminal tag. These findings highlight the role of glycosylation pattern and tag position in the activity of human recombinant glycosyltransferase produced in different hosts. - Source: PubMed
Publication date: 2025/08/18
Mikolajczyk KrzysztofSzymczak-Kulus KatarzynaBereznicka AnnaKaczmarek RadoslawSobala Lukasz FilipJakubiak-Augustyn AnnaCzerwinski Marcin