Polyclonal Rabbit B3GALTL Antibody
- Known as:
- Polyclonal Rabbit B3GALTL Antibody
- Catalog number:
- KA0363
- Product Quantity:
- 100ul
- Category:
- -
- Supplier:
- KareBay
- Gene target:
- Polyclonal Rabbit B3GALTL Antibody
Related genes to: Polyclonal Rabbit B3GALTL Antibody
- Gene:
- B3GLCT NIH gene
- Name:
- beta 3-glucosyltransferase
- Previous symbol:
- B3GALTL
- Synonyms:
- B3GTL, B3Glc-T
- Chromosome:
- 13q12.3
- Locus Type:
- gene with protein product
- Date approved:
- 2006-03-23
- Date modifiied:
- 2016-02-01
Related products to: Polyclonal Rabbit B3GALTL Antibody
Related articles to: Polyclonal Rabbit B3GALTL Antibody
- Source: PubMed
- The indigenous Afrikaner and composite Bonsmara cattle breeds are hardy and adapted to the diverse South African climate and biomes. Both breeds have been successfully used in the South African stud and commercial industries. This study explored the genomic diversity and population structure, as well as identified selection signatures within and between the Afrikaner and Bonsmara breeds with a focus on signatures related to adaptation traits. Short-read whole genome sequencing data of 42 Afrikaner and 43 Bonsmara cattle were analysed. Diversity analysis revealed comparable nucleotide diversity levels in the Afrikaner and Bonsmara populations, with the Bonsmara having weaker average linkage disequilibrium between adjacent single nucleotide polymorphisms as well as having fewer runs of homozygosity. Furthermore, genetic structure analysis revealed distinct clustering of both populations, with the exception of a subset of Afrikaner individuals having been infused with Bonsmara genetics. Between and within breed selection signatures were detected using the fixation index and integrated haplotype score approaches, respectively. Several gene ontology terms were described based on the detected selection signatures, with the most significant being nervous system development and multicellular organismal processes. Finally, functional annotation of the candidate genes from the within-breed selection signature analysis revealed several genes (, , , ) relating to adaptive traits in both populations. The location of the within and between breed selection signatures in this study population is consistent with the performance and adaptive characteristics of both breeds and may enhance future breeding strategies with the inclusion of these breeds in crossbreeding programs. Furthermore, a comprehensive genomic characterization of these breeds through whole genome sequencing data is important as these adapted breeds are valuable reservoirs of genetic variation. - Source: PubMed
Publication date: 2026/02/17
Alberts Dvan Marle-Köster EJoubert FBerry D P - Peters-Plus syndrome is a rare autosomal recessive disorder caused by biallelic pathogenic variants in the B3GLCT gene and characterized by multisystem involvement. Fewer than 100 cases have been reported to date, and only a limited number have been diagnosed prenatally. Prenatal identification is challenging due to the variable and non-specific nature of fetal findings and the frequent absence of detectable ocular anomalies during routine ultrasound. We report a prenatal diagnosis of Peters-Plus syndrome in a monochorionic diamniotic twin pregnancy, based on the progressive identification of early-onset intrauterine growth restriction, rhizomelic limb shortening, craniofacial dysmorphism, and mild central nervous system abnormalities. Standard cytogenetic and chromosomal microarray analyses were normal, prompting extended genetic testing. Prenatal exome sequencing identified a homozygous pathogenic splice-site variant (c.660+1G>A) in in both fetuses, confirming the diagnosis. This case highlights the importance of recognizing suggestive multisystem prenatal findings and the crucial role of advanced genetic testing in achieving an accurate prenatal diagnosis. Early molecular confirmation enables appropriate parental counseling regarding prognosis, recurrence risk, and future reproductive options. - Source: PubMed
Publication date: 2026/01/08
Fortún Agud MarinaMonís Rodríguez SusanaNarbona Arias IsidoroAndérica Herrero José RamónGómez Muñoz CristinaBlasco Alonso MartaJiménez López Jesús S - Peters-Plus syndrome (PTRPLS) is an autosomal recessive congenital disorder of glycosylation caused by biallelic pathogenic variants in the ß 1,3-glucosyltransferase gene (). To date, homozygous or compound heterozygous splicing, truncating, missense variants, and whole gene deletions have been reported in the gene. Our aim was to investigate the role of small copy number variations (CNVs) in this condition alongside the clinical features of the patients. - Source: PubMed
Publication date: 2025/04/11
Akalın AkçahanAvcı Durmuşalioğlu EniseÖzkalkak ŞervanYıldırım RukenÖz VeyselÜnal EdipHazar LeylaTurkut Tan TürkanDoğan Yusuf CanAtik TahirÇoğulu ÖzgürIşık Esra - Thrombospondin 1 (THBS1) is a secreted extracellular matrix glycoprotein that regulates a variety of cellular and physiological processes. THBS1's diverse functions are attributed to interactions between the modular domains of THBS1 with an array of proteins found in the extracellular matrix. THBS1's three Thrombospondin type 1 repeats (TSRs) are modified with O-linked glucose-fucose disaccharide and C-mannose. It is unknown whether these modifications impact trafficking and/or function of THBS1 in vivo. The O-fucose is added by Protein O-fucosyltransferase 2 (POFUT2) and is sequentially extended to the disaccharide by β3glucosyltransferase (B3GLCT). The C-mannose is added by one or more of four C-mannosyltransferases. O-fucosylation by POFUT2/B3GLCT in the endoplasmic reticulum has been proposed to play a role in quality control by locking TSR domains into their three-dimensional fold, allowing for proper secretion of many O-fucosylated substrates. Prior studies showed the siRNA knockdown of POFUT2 in HEK293T cells blocked secretion of TSRs 1-3 from THBS1. Here we demonstrated that secretion of THBS1 TSRs 1-3 was not reduced by CRISPR-Cas9-mediated knockout of POFUT2 in HEK293T cells and demonstrated that knockout of Pofut2 or B3glct in mice did not reduce the trafficking of endogenous THBS1 to secretory granules of platelets, a major source of THBS1. Additionally, we demonstrated that all three TSRs from platelet THBS1 were highly C-mannosylated, which has been shown to stabilize TSRs in vitro. Combined, these results suggested that POFUT2 substrates with TSRs that are also modified by C-mannose may be less susceptible to trafficking defects resulting from the loss of the glucose-fucose disaccharide. - Source: PubMed
Berardinelli Steven JSillato Andrew RGrady Richard CNeupane SanjivIto AtsukoHaltiwanger Robert SHoldener Bernadette C