SARS Nucleocapsid
- Known as:
- SARS Nucleocapsid
- Catalog number:
- ANT-180
- Product Quantity:
- 100µg
- Category:
- -
- Supplier:
- Prospecbio
- Gene target:
- SARS Nucleocapsid
Related genes to: SARS Nucleocapsid
- Gene:
- SARS NIH gene
- Name:
- seryl-tRNA synthetase
- Previous symbol:
- -
- Synonyms:
- SERS
- Chromosome:
- 1p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 1995-06-09
- Date modifiied:
- 2014-11-18
- Gene:
- SARS2 NIH gene
- Name:
- seryl-tRNA synthetase 2, mitochondrial
- Previous symbol:
- SARSM
- Synonyms:
- FLJ20450, mtSerRS, SerRSmt, SARS, SERS, SYS
- Chromosome:
- 19q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 2002-10-09
- Date modifiied:
- 2016-11-09
Related products to: SARS Nucleocapsid
62 kDa RNA-binding protein,Oryctolagus cuniculus,Rabbit,SARS,Serine--tRNA ligase,SerRS,SERS,Seryl-tRNA synthetase, cytoplasmic,Seryl-tRNA(Ser_Sec) synthetaseSARS coronavirus N Protein monoclonal antibody, clone 38j4SARS coronavirus N Protein monoclonal antibody, clone 8k5hA' SARS-CoV, Spike Antibody (OAMA02852)A' SARS-CoV, Spike Antibody (OAMA02863)A'SARS-CoV, M protein (NT) antibodyA'SARS-CoV, M protein (NT) antibody Polyclonal Antibodies Primary antibodiesA'SARS-CoV, M protein (NT) antibody Polyclonal Antibody Host: RabbitACE2 (SARS Receptor) Antibody (C-term)ACE2 (SARS Receptor) Antibody (C-term)ACE2 (SARS Receptor) Antibody (C-term) Blocking PeptideACE2 (SARS Receptor) Antibody (C-term) Blocking PeptideACE2 (SARS Receptor) Antibody (C-term) Purified Rabbit Polyclonal Antibody (Pab) Applications WB, IHC, EACE2 (SARS Receptor) Antibody (C-term) Purified Rabbit Polyclonal Antibody (Pab) Applications WB, IHC, EACE2 (SARS Receptor) Antibody (Center) Related articles to: SARS Nucleocapsid
- To explore the risk factors of Long COVID and to construct a nomogram to predict the occurrence of Long COVID. - Source: PubMed
Publication date: 2026/07/24
Haojing ZhangLin KanDianzhu Pan - Changes in cell type composition play an important role in human health and disease. Recent advances in single-cell technology have enabled the measurement of cell type composition at increasing cell lineage resolution across large cohorts of individuals. Yet this raises new challenges for statistical analysis of these compositional data to identify changes in cell type frequency. We introduce crumblr ( DiseaseNeurogenomics.github.io/crumblr ), a scalable statistical method for analyzing count ratio data using precision-weighted linear mixed models incorporating random effects for complex study designs. Uniquely, crumblr performs statistical testing at multiple levels of the cell lineage hierarchy using a multivariate approach to increase power over tests of one cell type. In simulations, crumblr increases power compared to existing methods while controlling the false positive rate. We demonstrate the application of crumblr to published single-cell RNA-seq datasets for aging, tuberculosis infection in T cells, bone metastases from prostate cancer, and SARS-CoV-2 infection. - Source: PubMed
Publication date: 2026/09/23
Hoffman Gabriel ERoussos Panos - Resolving genomes at the haplotype level for viral populations is crucial for understanding the prevalence of viral diseases and for the development of effective therapeutic treatments. However, viral haplotype reconstruction still presents challenges, such as an unknown number of strains, high inter-strain similarity, repetitive regions, and difficulties in abundance estimation. Here, we develop virCHap, a new reference-based haplotype phasing algorithm for viruses, which applies graph partitioning followed by iteratively quantifiable cluster merging on long-read sequencing data. Benchmarking on simulated and real datasets demonstrates that virCHap outperforms current tools in terms of recall, accurate abundance estimates and read clustering accuracy. On the simulated large-genome VZV experiment, virCHap has a 96% recall, 13.6% higher than the second-best method, and has the most accurate abundance estimates. On a real 5-strain PVY dataset, virCHap has a precision exceeding 94.4%, a recall of over 97%, and a read clustering accuracy of 93.4%, outperforming the second-best method by 33%. On a real 6-strain SARS-CoV-2 dataset, virCHap achieves >96.7% accuracy, and the most accurate abundance estimates within the spike gene. - Source: PubMed
Publication date: 2026/09/23
Gao YunLiu BingqiangLi GuojunYu Ting - The ubiquitin-proteasome system (UPS) plays a pivotal role in the precise regulation of innate immunity. Within the spatiotemporal framework of coronavirus (CoV) infection, the UPS emerges as a critical arena and a molecular switch, dynamically mediating the balance between host antiviral defense and viral replication alongside immune evasion. The host leverages the UPS to activate interferon (IFN) signaling pathways and to directly target viral proteins for degradation. Conversely, CoVs have developed sophisticated mechanisms to exploit this system, either by degrading antiviral proteins or by encoding viral deubiquitinases (DUBs) to counteract host ubiquitination signals. Notably, CoV proteins themselves undergo ubiquitination, which can lead to either their functional activation or proteasomal degradation, underscoring the dual-edged nature of the UPS. In this review, we initially examined the mechanisms by which the UPS regulates the IFN system. Subsequently, we highlighted the strategies employed by CoVs to inhibit the IFN system through the manipulation of the UPS. Thirdly, we synthesized findings regarding how the UPS specifically targets and degrades the principal virulence proteins of CoVs. Finally, we investigated the potential of the UPS as a therapeutic target for developing resistance against CoV infections. - Source: PubMed
Publication date: 2026/07/24
Xiang YingjieZhu QinyuanMou ChunxiaoShi KaichuangChen Zhenhai - COVID-19 remains a global health threat due to its rapid transmission and the emergence of new variants. Despite advances in vaccines and antiviral treatments, there remains a pressing need for alternative strategies that prevent viral entry at the earliest stage. Heparin, recognized for its electrostatic affinity toward the SARS-CoV-2 spike protein, has demonstrated potential in disrupting viral attachment. In response to this challenge, the present study proposes a modeled DNA origami-linker-heparin construct that integrates a DNA origami U-shaped cage with heparin through a spermidine-based linker, designed to investigate the structural and energetic behavior of tethered heparin chains in the presence of the SARS-CoV-2 RBD. Three hybrid complexes with varying heparin lengths were designed and evaluated using all-atom molecular dynamics simulations at 300, 310, and 320 K, with 320 K considered an elevated-temperature stress condition. The findings indicate that the complex containing decasaccharide heparin exhibits the most stable structure and the strongest interaction with the RBD, as evidenced by consistently lower electrostatic and van der Waals energies. Moreover, post-MD MM/PBSA calculations provided relative binding-energy estimates and revealed the energetic contributions of molecular-mechanics, polar-solvation, and nonpolar-solvation terms. These results suggest that the predicted interaction stability of the tethered heparin-RBD complexes arises from the combined effects of electrostatic interactions, solvation contributions, and persistent intermolecular contacts. Overall, the results provide a comparative structural and energetic characterization of three tethered heparin systems and identify the decasaccharide-containing construct as having the most favorable relative interaction energetics among the modeled systems. Experimental validation and matched control simulations will be required to determine biological relevance and any scaffold-dependent advantage. - Source: PubMed
Publication date: 2026/09/23
Dastorani SadeghShariati MahmoudHasanzadeh Ghasemi Reza