ATP synthase subunit c
- Known as:
- adenosine triphosphate synthase active sequence peptide c
- Catalog number:
- AS09 591
- Product Quantity:
- 0.1 ml
- Category:
- -
- Supplier:
- ACR
- Gene target:
- ATP synthase subunit
Related genes to: ATP synthase subunit c
- 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
Related products to: ATP synthase subunit c
(2-5')oligo(A) synthase 1B,2-5A synthase 1B,2'-5'-oligoadenylate synthase 1B,2'-5'-oligoadenylate synthase-like protein 1,Mouse,Mus musculus,Oas1b,Oias2(2-5')oligo(A) synthase 2,2-5A synthase 2,2'-5'-oligoadenylate synthase 2,Homo sapiens,Human,OAS2,p69 OAS _ p71 OAS,p69OAS _ p71OAS(Biotin Conjugates) Phospho-calcium channel 2A subunit Immunogen: peptide Host: Rabbit(cAMP free) Protein Kinase A regulatory subunit-I A Recombinant(cAMP free) Protein Kinase A regulatory subunit-I A Recombinant(FITC-conjugates) Phospho-calcium channel 2A subunit Immunogen: peptide Host: Rabbit([125I]-Tyr0)-Inhibin a-Subunit (1-32) (human)([125I]-Tyr0)-Inhibin a-Subunit (1-32) (human)([125I]-Tyr0)-Inhibin a-Subunit (1-32) (human), CE-marked, Liquid([125I]-Tyr0)-Inhibin a-Subunit (1-32) (human), CE-marked, Liquid([125I]-Tyr0)-Inhibin a-Subunit (1-32) (human), CE-marked, Liquid([125I]-Tyr0)-Inhibin a-Subunit (1-32) (human), CE-marked, Lyophilized([125I]-Tyr0)-Inhibin a-Subunit (1-32) (human), CE-marked, Lyophilized([125I]-Tyr0)-Inhibin a-Subunit (1-32) (human), CE-marked, Lyophilized([125I]-Tyr0)-Inhibin a-Subunit (1-32) (human)CE-markedLiquid Related articles to: ATP synthase subunit c
- C1GALT1 plays a pivotal role in colorectal cancer (CRC) development and progression through its involvement in various molecular mechanisms. This enzyme is central to the O-glycosylation process, producing tumor-associated carbohydrate antigens (TACA) like Tn and sTn, which are linked to cancer metastasis and poor prognosis. The interaction between C1GALT1 and core 3 synthase is crucial for the synthesis of core 3 O-glycans, essential for gastrointestinal health and mucosal barrier integrity. Aberrations in this pathway can lead to CRC development. Furthermore, C1GALT1's function is significantly influenced by its molecular chaperone, Cosmc, which is necessary for the proper folding of T-synthase. Dysregulation in this complex interaction contributes to abnormal O-glycan regulation, facilitating cancer progression. Moreover, C1GALT1 affects downstream signaling pathways and cellular behaviors, such as the epithelial-mesenchymal transition (EMT), by modifying O-glycans on key receptors like FGFR2, enhancing cancer cell invasiveness and metastatic potential. Additionally, the enzyme's relationship with MUC1, a mucin protein with abnormal glycosylation in CRC, highlights its role in cancer cell immune evasion and metastasis. Given these insights, targeting C1GALT1 presents a promising therapeutic strategy for CRC, necessitating further research to develop targeted inhibitors or activators. Future efforts should also explore C1GALT1's potential as a biomarker for early diagnosis, prognosis, and treatment response monitoring in CRC, alongside investigating combination therapies to improve patient outcomes. - Source: PubMed
Publication date: 2024/04/18
Tian HongYu Jia-LiChu XiaoliGuan QiLiu JuanLiu Ying - Core 1β1,3-galactosyltransferase 1 (C1GALT1) exhibits elevated expression in multiple cancers. The present study aimed to elucidate the clinical significance of C1GALT1 aberrant expression and its impact on radiosensitivity in lung adenocarcinoma (LUAD). - Source: PubMed
Publication date: 2024/04/25
Chen YongJi YanyanShen LinLi YingRen YueShi HongcanLi YueWu Yunjiang - Chemical systems glycobiology requires experimental and computational tools to make possible big data analytics benefiting genomics and proteomics. The impediment to tool development is that the nature of glycan construction and mutation is not template driven but rests on cooperative glycosyltransferase (GT) catalytic synthesis. What is needed is the collation of kinetics and inhibition data in a standardized form to make possible analytics of glycan and glycoconjugate synthesis, mechanism extraction, and pattern recognition. Currently, kinetics assays in use for GTs are not universal in processing nucleoside phosphate UDP, GDP, and CMP donor-based glycosylation reactions due to limitations in accuracy and large substrate volume requirements. Here we present a universal glycosyltransferase continuous (UGC) assay able to measure the declining concentration of the NADH reporter molecule through fluorescence spectrophotometry and, therefore, determine reaction rate parameters. The development and parametrization of the assay is based on coupling the nucleotide released from GT reactions with pyruvate kinase, via nucleoside diphosphate kinase (NDK) in the case of NDP-based donor reactions. In the case of CMP-based reactions, the coupling is carried out via another kinase, cytidylate kinase in combination with NDK, which phosphorylates CMP to CDP, then CDP to CTP. Following this, we conduct kinetics and inhibition assay studies on the UDP, GDP, and CMP-based glycosylation reactions, specifically C1GAlT1, FUT1, and ST3GAL1, to represent each class of donor, respectively. The accuracy of calculating initial rates using the continuous assay compared to end point (noncontinuous) assays is demonstrated for the three classes of GTs. The previously identified natural product soyasaponin1 inhibitor was used as a model to demonstrate the application of the UGC assay as a standardized inhibition assay for GTs. We show that the dose response of ST3GAL1 to a serial dilution of Soyasaponin1 has time-dependent inhibition. This brings into question previous inhibition findings, arrived at using an end point assay, that have selected a seemingly random time point to measure inhibition. Consequently, using standardized values taken from the UGC assay study, ST3GAL1 was shown to be the most responsive enzyme to soyasaponin1 inhibition, followed by FUT1, then C1GALT1 with IC values of 37, 52, and 886 μM respectively. - Source: PubMed
Publication date: 2024/04/05
Nashed AbdullateefNaidoo Kevin J - The role of glycosyltransferase (GT) genes in lung adenocarcinoma (LUAD) needs further elucidation. Thus, our study aims to identify the prognostic gene signature of LUAD and explore its molecular functions. - Source: PubMed
Publication date: 2024/04/09
Zhou JiejunZhang KunYang TianLi AnqiLi MengPeng XiaojingChen Mingwei - Novel therapeutic strategies are urgently required for osteosarcoma, given the early age at onset and persistently high mortality rate. Modern transcriptomics techniques can identify differentially expressed genes (DEGs) that may serve as biomarkers and therapeutic targets, so we screened for DEGs in osteosarcoma. We found that osteosarcoma cases could be divided into fair and poor survival groups based on gene expression profiles. Among the genes upregulated in the poor survival group, siRNA-mediated knockdown of the glycosylation-related gene C1GALT1 suppressed osteosarcoma cell proliferation in culture. Gene expression, phosphorylation, and glycome array analyses also demonstrated that C1GALT1 is required to maintain ERK signaling and cell cycle progression. Moreover, the C1GALT1 inhibitor itraconazole suppressed osteosarcoma cell proliferation in culture, while doxycycline-induced shRNA-mediated knockdown reduced xenograft osteosarcoma growth in mice. Elevated C1GALT1 expression is a potential early predictor of poor prognosis, while pharmacological inhibition may be a feasible treatment strategy for osteosarcoma. - Source: PubMed
Publication date: 2024/04/15
Watanabe KentaroTasaka KeijiOgata HidetoKato ShotaUeno HirooUmeda KatsutsuguIsobe TomoyaKubota YasuoSekiguchi MasahiroKimura ShunsukeSato-Otsubo AikoHiwatari MitsuteruUshiku TetsuoKato MotohiroOka AkiraMiyano SatoruOgawa SeishiTakita Junko