登录 | 注册    关注公众号  
微信公众号
搜索
 >  Protein>Nucleocapsid protein >NUN-C52Hu

SARS-CoV-2 Nucleocapsid protein, His Tag (BA.2*&BA.3*/Omicron)

分子别名(Synonym)

Nucleocapsid protein,NP,Protein N

表达区间及表达系统(Source)

SARS-CoV-2 Nucleocapsid protein, His Tag (BA.2*&BA.3*/Omicron) (NUN-C52Hu) is expressed from human 293 cells (HEK293). It contains AA Met 1 - Ala 419 (Accession # QHO62115.1(P13L, ERS31-33del, R203K, G204R, S413R)). The nucleocapsid mutations are identified on the SARS-CoV-2 Omicron variant (Pango lineage: BA.2; GISAID clade: GRA; Nextstrain clade: 21L & Pango lineage: BA.3; GISAID clade: GRA; Nextstrain clade: 21M).

Predicted N-terminus: Met 1

Request for sequence

蛋白结构(Molecular Characterization)

This protein carries a polyhistidine tag at the C-terminus.

The protein has a calculated MW of 47.1 kDa. The protein migrates as 30-35 kDa and 60-66 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

内毒素(Endotoxin)

Less than 1.0 EU per μg by the LAL method.

纯度(Purity)

>95% as determined by SDS-PAGE.

制剂(Formulation)

Lyophilized from 0.22 μm filtered solution in PBS, 0.2 M Arginine, pH7.4 with trehalose as protectant.

Contact us for customized product form or formulation.

重构方法(Reconstitution)

Please see Certificate of Analysis for specific instructions.

For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

存储(Storage)

For long term storage, the product should be stored at lyophilized state at -20°C or lower.

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:

  1. -20°C to -70°C for 12 months in lyophilized state;
  2. -70°C for 3 months under sterile conditions after reconstitution.

质量管理控制体系(QMS)

  1. 质量管理体系(ISO, GMP)
  2. 质量优势
  3. 质控流程
 

电泳(SDS-PAGE)

Nucleocapsid protein SDS-PAGE

SARS-CoV-2 Nucleocapsid protein, His Tag (BA.2*&BA.3*/Omicron) on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95%.

 

活性(Bioactivity)-ELISA

Nucleocapsid protein ELISA

Immobilized SARS-CoV-2 Nucleocapsid protein, His Tag (BA.2*&BA.3*/Omicron) (Cat. No. NUN-C52Hu) at 1 μg/mL (100 μL/well) can bind Anti-SARS-CoV-2 Nucleocapsid Antibody, Human IgG1 (Cat. No. NUN-CH14) with a linear range of 0.1-2 ng/mL (QC tested).

Protocol

 
评论(0)
 
ACRO质量管理体系
 
 

背景(Background)

Nucleocapsid (N) protein is the most abundant protein found in coronavirus. CoV N protein is a highly immunogenic phosphoprotein important for viral genome replication and modulation of cell signaling pathways. It was first identified by a research team while they were screening for ADP-ribosylated proteins during coronavirus (CoV) infection (Grunewald M. E., et al. 2017, Virology; 517: 62-68). The array of diverse functional activities accommodated in N protein makes it more than a structural protein but also an interesting target in the development of antiviral therapeutics. Because of the conservation of N protein sequence and its strong immunogenicity, N protein of coronavirus is chosen as a diagnostic tool.

 

前沿进展

Genomic and structural insights into Jyvaskylavirus, the first giant virus isolated from Finland
Almeida, Arriaga, de Azevedo et al
Elife (2025) 13
Abstract: Giant viruses of protists are a diverse and likely ubiquitous group of organisms. Here, we describe Jyvaskylavirus, the first giant virus isolated from Finland. This clade B marseillevirus was found in Acanthamoeba castellanii from a composting soil sample in Jyväskylä, Central Finland. Its genome shares similarities with other marseilleviruses. Helium ion microscopy and electron microscopy of infected cells unraveled stages of the Jyvaskylavirus life cycle. We reconstructed the Jyvaskylavirus particle to 6.3 Å resolution using cryo-electron microscopy. The ~2500 Å diameter virion displays structural similarities to other Marseilleviridae giant viruses. The capsid comprises of 9240 copies of the major capsid protein, encoded by open reading frame (ORF) 184, which possesses a double jellyroll fold arranged in trimers forming pseudo-hexameric capsomers. Below the capsid shell, the internal membrane vesicle encloses the genome. Through cross-structural and -sequence comparisons with other Marseilleviridae using AI-based software in model building and prediction, we elucidated ORF142 as the penton protein, which plugs the 12 vertices of the capsid. Five additional ORFs were identified, with models predicted and fitted into densities that either cap the capsomers externally or stabilize them internally. The isolation of Jyvaskylavirus suggests that these viruses may be widespread in the boreal environment and provide structural insights extendable to other marseilleviruses.© 2024, Almeida et al.
The HBV large envelope protein initiates virion assembly by recruiting capsids at membrane rich domains related to late endosome
Seigneuret, Eymieux, Sarabia-Vega et al
Cell Mol Life Sci (2025) 82 (1), 128
Abstract: A crucial step of HBV (Hepatitis B Virus) virion morphogenesis is the envelopment of the nucleocapsid by the viral envelope proteins, which is triggered by an interaction between the HBV core protein and the large HBV envelope protein. To document this protein-protein interaction, we co-expressed core and large HBV envelope (LHBs) in Huh-7 cells and subjected the cells to microscopy examination by Fluorescence Resonance Energy Transfer (FRET) and Transmission Electron Microscopy (TEM). Our results show that the sole expression of the core protein leads to assembly of capsids that remain individually isolated within the whole cell, but particularly within the nucleus. In the presence of LHBs, capsids were observed as large clusters in a membrane rich region peripheral to the nucleus. In this context, core-LHBs complex co-localize with markers of the late endosome/multivesicular bodies, this co-localization being driven by LHBs. These results thus show that LHBs binds to the core proteins when preassembled into capsid, at membranes of the late endosome, where the inner capsid and the outer envelope meet to assemble a virion.© 2025. The Author(s).
In-house assays for detecting anti-SARS-CoV-2 antibodies in serum and urine: Correlation with COVID-19 severity from a cohort study in Qatar
Vaikath, Al-Nesf, Majbour et al
J Infect Public Health (2025) 18 (6), 102744
Abstract: Serological assays targeting antibodies against key viral proteins, including the Spike (S1), Receptor Binding Domain (RBD), and Nucleocapsid, play a critical role in understanding immunity and supporting diagnostic efforts during COVID-19 pandemic, and afterward. This study aimed to develop and validate in-house assays for detecting anti-SARS-CoV-2 antibodies in serum and urine.ELISA-based assay was developed to detect IgG and IgM antibodies against SARS-CoV-2. The assay was examined in serum and urine samples of two different cohort of patients affected by COVID-19 disease with different severity and compared to age and sex matched control group. Neutralizing antibody activity was evaluated using an RBD-ACE2 binding inhibition assay. Additionally, a Sengenics protein microarray platform was employed to assess epitope-specific antibody responses.The in-house ELISA assay reliably detected antibodies in both 163 serum and 64 urine samples compared to 50 serum samples from healthy control, with strong correlations observed between antibody levels in the two biofluids. Neutralizing antibody levels correlated positively with disease severity, highlighting their clinical relevance. The performance of the in-house assays was comparable to commercial kits, and the Sengenics microarray provided detailed insights into antibody profiles, identifying dominant epitopes within the Nucleocapsid core domain and RBD.The developed in-house assay demonstrated robust performance and versatility, offering a cost-effective and scalable alternative to commercial kits. Their ability to detect antibodies in both serum and urine highlighted their potential as non-invasive diagnostic tools. These findings contribute to advancing sero-diagnostic capabilities, improving understanding of immune responses to SARS-CoV-2, and supporting global efforts to monitor and manage COVID-19 effectively.Copyright © 2025. Published by Elsevier Ltd.
Increase of VEGF and Fibronectin expression and ultrastructural alterations of intercellular junctions in a swab negative patient after SARS-COV-2 infection
Simioni, Sanz, Gafà et al
Virol J (2025) 22 (1), 82
Abstract: SARS-CoV-2 infection has been responsible of COrona VIrus Disease (COVID-19) pandemia and can cause a variety of symptoms including gastrointestinal disorders, abdominal pain and liver injury. The host receptor for SARS-CoV-2, ACE2, is expressed in gut and SARS-CoV-2 infection could induce vascular damage and immune system dysregulation, creating an inflammatory and hypercoagulable state, as widely described at the lung level.This work presents the case of a middle-aged Caucasian man admitted to the Hospital Emergency Department from the University Hospital of Ferrara (Italy), complaining of pain in the upper and middle region of the abdomen. The patient tested negative to the nose-oropharyngeal swab for SARS-CoV-2 four weeks after recovering from viral infection. The patient required resection of a segment of ileum and an ulcer of the bowel wall was recognized and sampled. Previous published results had confirmed the presence of the SARS-CoV-2 nucleocapsid protein, an increased human leukocyte antigen (HLA-G) and an altered morphology of microvilli in the ulcerated ileum of the patient when compared to the non-ulcerated ileum. The present study sought to deepen the consequences of SARS-CoV-2 infection. To this end, we evaluated the expression and co-expression of Vascular Endothelial Growth Factor (VEGF) and Fibronectin by immunohistochemical techniques. VEGF immunohistochemical expression was higher in the ulcer than in the control ileum sample and the non-ulcerated ileum areas and co-expressed with the SPIKE protein. Fibronectin staining was lower in control sample than in non-ulcerated and ulcerated ileum. Electron microscopy analysis showed alterations of the integrity of the intestinal barrier in the ulcerated area when compared to the non-ulcerated ileum or to the control sample.Although the patient was tested negative to nose-oropharyngeal swab for SARS-CoV-2, the SPIKE protein was detected in his terminal ileum, especially in the ulcerated areas. The presence of the viral protein was also associated with an increase of VEGF and Fibronectin. In addition to vascular changes, the SARS-CoV-2 infection altered the junctional apparatus among epithelial cells, making the tissue even more fragile and thus susceptible to the entry of pathogens and the development of further infections.© 2025. The Author(s).
Showing 1-4 of 56467 papers.
Powered by BizGenius
 
 
货号/价格
文档
联系电话:
+86 400-682-2521(全国)
010-53681107(北京)
021-50850665(上海)
运输方式
订单邮箱:
order.cn@acrobiosystems.com
技术支持邮箱:
tech.cn@acrobiosystems.com
Nucleocapsid protein靶点信息
英文全称:Nucleocapsid proteins
中文全称:核壳蛋白
种类:Homo sapiens
上市药物数量:0详情
临床药物数量:1详情
最高研发阶段:临床一期
查看更多信息
前沿进展
点击查看详细

消息提示

请输入您的联系方式,再点击提交!

确定