ITM1 Mouse Monoclonal Antibody
- Known as:
- ITM1 Mouse Monoclonal Antibody
- Catalog number:
- BIN-003703-M02
- Product Quantity:
- 0.1mg
- Category:
- -
- Supplier:
- Zyagen
- Gene target:
- ITM1 Mouse Monoclonal Antibody
Related genes to: ITM1 Mouse Monoclonal Antibody
- Gene:
- STT3A NIH gene
- Name:
- STT3 oligosaccharyltransferase complex catalytic subunit A
- Previous symbol:
- ITM1
- Synonyms:
- TMC, MGC9042, STT3-A
- Chromosome:
- 11q24.2
- Locus Type:
- gene with protein product
- Date approved:
- 1996-08-01
- Date modifiied:
- 2019-01-25
Related products to: ITM1 Mouse Monoclonal Antibody
Related articles to: ITM1 Mouse Monoclonal Antibody
- Osteoarthritis (OA) is a heterogeneous joint disease characterized by cartilage degeneration. The interplay between extracellular matrix (ECM) remodeling, endoplasmic reticulum (ER) stress, and inflammatory signaling in OA pathogenesis remains incompletely understood. This study aimed to identify robust diagnostic biomarkers and explore the mechanistic convergence of key genes in OA cartilage through an integrated transcriptomic framework. - Source: PubMed
Publication date: 2026/06/15
Lv XueyaYu YangFan JiawenGuo LianjiangZhu XiangLi Xingye - Viral fusion proteins decorate their antigenic surface with N-linked glycans which support processes such as protein folding, cell-specific interactions and shielding of vulnerable antibody epitopes. Asparagine-linked glycosylation is catalyzed by the oligosaccharyltransferase (OST) complexes containing the catalytic subunits STT3A or STT3B, which act predominantly co- and post-translationally, respectively. Here, we investigated the contributions of STT3A and STT3B to glycan attachment to recombinant SARS-CoV-2 Spike (S) and influenza A (H3N2) virus hemagglutinin (HA). Soluble proteins and pseudotyped viruses were produced in wild-type and STT3A or STT3B-knockout (KO) 293T cells. Site-specific glycan analysis of the recombinant proteins revealed significant changes at only a limited number of glycosylation sites upon deletion of either STT3A or STT3B, indicating partial redundancy in maintaining overall site occupancy. However, STT3A-KO reduced glycosylation at N717 and N1074 on the SARS-CoV-2 S protein, while STT3B KO reduced glycosylation at N483 on influenza HA, suggesting isoform-specific preferences for distinct glycosylation sequons. Infectivity assays further suggested that the glycosylation of both SARS-CoV-2 and influenza A (H3N2) viral glycoproteins are more dependent on STT3A, with STT3B contributing to a lesser but detectable extent. These findings highlight distinct, context-dependent and site-specific contributions of STT3A and STT3B to viral glycoprotein glycosylation, with implications for vaccine antigen design. - Source: PubMed
Publication date: 2026/04/09
Atabey TugbaNewby Maddy LHulme Katina DNemanichvili Nikolozvan Groeningen Laura ERussell Colin AAllen Joel DCrispin MaxSanders Rogier W - Congenital disorders of glycosylation (CDGs) are a phenotypically diverse group of genetic conditions arising from pathogenic variants in various glycosylation pathways. The most prevalent are N-glycosylation disorders. Here, we present clinical and biochemical data on two siblings with a neurodevelopmental disorder and a pathogenic homozygous nonsense variant in ribophorin I (RPN1), an essential component of the oligosaccharyltransferase (OST) complex. Both affected individuals showed a classical type I serum transferrin profile, while lymphoblasts revealed that the variant resulted in a truncated RPN1 protein with reduced levels. The protein stability of other essential OST complex components, including STT3 OST complex catalytic subunit A (STT3A), RPN2, and dolichyl-diphosphooligosaccharide (DDOST), was also significantly reduced. Structural modeling of both OST-A and OST-B complexes shows that RPN1 truncation eliminates a C-terminal four-helix bundle, which interacts with the translating ribosome. This interaction is necessary and specific for the co-translational activity of the OST-A complex. Supporting this observation, hypoglycosylation of an OST-A-specific substrate protein was observed, while OST-B-specific substrates were unaffected. These data convey that a rare loss-of-function RPN1 variant causes an autosomal recessive CDG characterized by neurodevelopmental deficits. - Source: PubMed
Publication date: 2026/04/03
Ng Bobby GZhang WenyueNeil Jennifer EDanish MarwaMarafi DanaKamal Tarek MBastaki LailaAl Saffar MunaYang EdwardHe MiaoWalsh Christopher AMochida Ganeshwaran HFreeze Hudson H - Cervical cancer remains a major global health burden. Although PD-1/PD-L1 immune checkpoint blockade has expanded treatment options, durable responses are still limited. One key reason is that tumor cells sustain immunosuppression by maintaining high levels of mature, N-glycosylated PD-L1 on the plasma membrane. This limitation highlights the need for approaches that disrupt PD-L1 maturation and stability rather than merely blocking ligand-receptor binding. UM-6, a melittin-derived fusion peptide, addresses this need by retaining antitumor activity while exhibiting markedly lower hemolysis than native melittin. In tumor models, UM-6 slowed tumor progression, reduced proliferation, and increased apoptosis. In parallel, it reshaped the tumor immune microenvironment by enhancing cytotoxic T-cell activity and mitigating PD-1-associated T-cell exhaustion. Mechanistically, UM-6 impaired PD-L1 N-glycosylation and reduced PD-L1 association with STT3A, which led to endoplasmic-reticulum retention, increased polyubiquitination, and accelerated ERAD/proteasome-mediated degradation, ultimately reducing functional PD-L1 at the cell surface. Together, these results support UM-6 as a peptide-based, mechanistically distinct strategy that targets PD-L1 biogenesis to relieve immunosuppression in cervical cancer. - Source: PubMed
Publication date: 2026/03/23
Wang DongyingHe JiaxingWu ShuyingLiu ShanshanWang HongxinXu Tianmin - encodes the catalytic subunit of the oligosaccharyltransferase A (OST-A) complex and is classically linked to severe autosomal-recessive congenital disorder of glycosylation (CDG). To define the distinct autosomal-dominant disorder, we reviewed all published cases and integrated three previously unpublished individuals from the CDG natural history study. Across 21 individuals, abnormal transferrin glycosylation was present in nearly all individuals (20/21), and subtle facial dysmorphism was common (18/21). Neurodevelopmental involvement was frequent, including motor delay (13/21), learning difficulties (13/21), speech delay (12/21), and intellectual disability (10/21). Musculoskeletal manifestations were also common, including skeletal abnormalities (12/21), short stature (11/21), muscle cramps (8/21), and early-onset osteoarthritis in adults (6/21). Less frequent features included congenital heart defects (5/21) and coagulation factor deficiency (5/21). Importantly, the newly reported individuals expand dominant STT3A-CDG with previously unreported features, including anorectal malformation, morbid obesity, and clinically significant bleeding diathesis with von Willebrand factor and factor VIII deficiency. Biochemical signatures ranged from classic type I transferrin patterns to subtle or atypical abnormalities, emphasizing that near-normal transferrin testing does not exclude the diagnosis. Variants clustered in conserved catalytic regions, with recurrent p.Arg405 across de novo, inherited, and mosaic cases supporting a mutational hotspot and likely dominant-negative mechanism. - Source: PubMed
Publication date: 2026/03/12
Al-Shahrani HamdanSzabó EvelinStaccone CarolineMacDonald GeorgiaFuruta YutakaSchecter DanielEdmondson Andrew CMcRae AnneBaker JoshMorava EvaTinker Rory J