LARGE BEAKERS: POLYSTYRENE:1000 ml
- Known as:
- LARGE BEAKERS: POLYSTYRENE:1000 milliliter
- Catalog number:
- B1000-100
- Product Quantity:
- 100/Cs
- Category:
- -
- Supplier:
- EThermo
- Gene target:
- LARGE BEAKERS: POLYSTYRENE:1000
Related genes to: LARGE BEAKERS: POLYSTYRENE:1000 ml
- Gene:
- LARGE1 NIH gene
- Name:
- LARGE xylosyl- and glucuronyltransferase 1
- Previous symbol:
- LARGE
- Synonyms:
- KIAA0609
- Chromosome:
- 22q12.3
- Locus Type:
- gene with protein product
- Date approved:
- 1999-06-02
- Date modifiied:
- 2019-04-23
Related products to: LARGE BEAKERS: POLYSTYRENE:1000 ml
Related articles to: LARGE BEAKERS: POLYSTYRENE:1000 ml
- α-Dystroglycan (α-DG) is a central component of the dystrophin-glycoprotein complex, with the characteristic O-mannosyl glycan modification, which binds to several extracellular matrix proteins such as laminin. Disruption in the synthesis of laminin-binding glycan on α-DG is related to muscular dystrophies. In addition, loss of this glycan is frequently observed in many cancers, including pancreatic ductal adenocarcinoma (PDAC), correlating with poor prognosis. However, the significance of this glycan in the pathology of cancer remains unclear. This study aimed to clarify the biological significance of laminin-binding O-mannosyl glycan on α-DG in PDAC cells. Since a tumor-derived cancer cell line consists of cells with diverse characteristics, we first obtained several single-cell-derived clones using MIA PaCa-2, a commonly used undifferentiated PDAC cell line, and found that the laminin-binding glycan modification level on α-DG differs among the various clones. The glycan modification level correlated well with the mRNA expression level of LARGE1, the enzyme that synthesizes the laminin-binding structure on the glycan. We analyzed several PDAC cell properties, such as cellular morphology, proliferation and migration/invasion abilities, and examined their correlation with the glycan modification. We found that a high level of laminin-binding O-mannosyl glycan modification on α-DG correlated with the elongated cell morphology, high invasion ability, and low membrane blebbing activity, and vice versa. Furthermore, manipulation of the laminin-binding O-mannosyl glycan synthesis confirmed that this glycan partially contributed to these properties. Overall, this study provides valuable insights into the roles of the laminin-binding glycan on α-DG in PDAC. - Source: PubMed
Publication date: 2026/01/16
Imae RiekoShichi YuukiNinagawa SatoshiIshiwata ToshiyukiManya Hiroshi - Grain size has long been recognized as a key determinant of yield potential in crops. Understanding the mechanisms governing grain size is critical for breeding high-yielding varieties. In a previous work, we revealed that the RNA-binding protein LARGE1 acts as a negative regulator of grain size and weight in rice. LARGE1 interacts with GSK2 (GLYCOGEN SYNTHASE KINASE2) and is phosphorylated by GSK2. Here, we report that LARGE1 physically interacts with an atypical non-DNA-binding bHLH protein PGL2 that positively influences grain size. Biochemical analyses show that PGL2 binds to APG, a typical DNA-binding bHLH protein that negatively regulates grain size. PGL2 suppresses the transcriptional activation activity of APG by forming the PGL2/APG heterodimer. Strikingly, LARGE1 can repress the formation of the heterodimer PGL2/APG by competitively binding PGL2, thereby releasing the inhibitory effect of PGL2 on the transcriptional activation activity of APG. Genetic evidence and RNA-seq analyses support that LARGE1 and PGL2 act in a common pathway to regulate grain size in rice. Our findings uncover a novel regulatory module GSK2-LARGE1-PGL2/APG that fine-tunes grain size, suggesting a promising target for improving seed size and weight in crops. - Source: PubMed
Liu YapeiZhang HaoGao YingXi XingniZhang YuhanLyu JiaZhang LiminLi Yunhai - Matriglycan is a linear glycan (xylose-β1,3-glucuronate), which binds proteins in the extracellular matrix that contain laminin-globular domains and Lassa Fever Virus. It is indispensable for neuromuscular function. Matriglycan of insufficient length can cause muscular dystrophy with abnormal brain and eye development. LARGE1 (Like-acetylglucosaminyltransferase-1) uniquely synthesizes matriglycan on dystroglycan. The mechanism of matriglycan synthesis is not obvious from cryo-EM reconstructions of LARGE1. However, by reconstituting activity in vitro on recombinant prodystroglycan we show that the presence of the dystroglycan N-terminal domain (DGN), phosphorylated core M3, and a xylose-glucuronate primer are necessary for matriglycan polymerization by LARGE1. By introducing active site mutations, we demonstrate that LARGE1 processively polymerizes matriglycan on prodystroglycan, with its length regulated by the dystroglycan prodomain, DGN. Our enzymatic analysis of LARGE1 uncovers the mechanism of matriglycan synthesis on dystroglycan, which can form the basis for therapeutic strategies to treat matriglycan-deficient neuromuscular disorders and arenaviral infections. - Source: PubMed
Publication date: 2025/10/10
Joseph SoumyaSchnicker Nicholas JSpellmon NicholasXu ZhenYan RuiYu ZhihengDavulcu OmarYang TiandiHopkins JesseAnderson Mary EVenzke DavidCampbell Kevin P - The distinctive geography and climate of Gansu Province have given rise to three indigenous cattle breeds-Zaosheng, Anxi, and Yangba. Renowned for their superior meat quality and remarkable adaptability, these breeds are crucial for maintaining genetic diversity. However, they are under threat from intensive farming practices, environmental degradation, and genetic drift, which could lead to an irreversible loss of genetic resources. Thanks to natural and artificial selection, these breeds possess genetic markers that enhance their adaptation to extreme environments and improve key economic traits. By integrating comprehensive genome data from multiple breeds, this study aims to analyze population genetics, detect composite selection signals, and perform functional enrichment to uncover the mechanisms behind genetic differentiation and adaptive evolution. This research is pivotal for developing resilient breeds and ensuring sustainable resource management. - Source: PubMed
Publication date: 2025/07/01
Cai BaoKang YandongXiong LinPei JieGe QianyunWu XiaoyunGan ManyuGuo Xian - Dystroglycan (DG) binds to extracellular matrix via its O-glycans, which are sequentially modified in a specific order by DG-specific enzymes: POMGNT2, B3GalNT2, and POMK in the endoplasmic reticulum (ER), followed by FKTN, FKRP, TMEM5, B4GAT1 and LARGE1 in the Golgi apparatus. However, there have been no comprehensive and systematic studies on the major localization of these enzymes. Here, we expressed fluorescent fusion proteins of DG-specific modifying enzymes under the control of short CMV promoter and observed their primary localization using the latest microscopy along with localization markers: mEGFP-KDEL for the ER, GM130 and GRASP55 for the cis-/medial-Golgi, and TGN46 and GCC1 for the trans-Golgi network. As a result, POMGNT2 and B3GalNT2 were localized to the ER as expected, but POMK was localized predominantly to the cis-/medial-Golgi showing co-localization with GRASP55. FKTN, FKRP and TMEM5 were partially co-localized with both cis-/medial- and trans-Golgi network markers. Though B4GAT1 did not co-localize with GM130 or TGN46, it co-localized with GCC1 another trans-Golgi network marker, indicating Golgi subcompartmentalization. LARGE1, the final glycosyltransferase involved in the modification of DG's O-glycan, was localized in the cis-/medial-Golgi, but did not overlap with trans-Golgi network markers. An EndoH sensitivity assay demonstrated that DG-specific enzymes interacting with DG were localized in the early secretory pathway. Our results reveal that POMK and B4GAT1 function at locations distinct from their major localization and support the conclusion that the modification of matriglycan on DG is completed at the cis-/medial-Golgi. - Source: PubMed
Aso ShinyaLowe MartinMori KazutoshiNinagawa Satoshi