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SARS-CoV-2 Nucleocapsid protein, His Tag (BQ.1/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 (BQ.1/Omicron) (NUN-C52Hx) is expressed from human 293 cells (HEK293). It contains AA Met 1 - Ala 419 (Accession # QHO62115.1 (P13L, ERS31-33del, E136D, R203K, G204R, S413R)). The mutations are identified on the SARS-CoV-2 Omicron variant (Pango lineage: BQ.1; GISAID clade: GRA).

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 55-60 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 (BQ.1/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 (BQ.1/Omicron) (Cat. No. NUN-C52Hx) at 1 μg/mL (100 μL/well) can bind Anti-SARS-CoV-2 Nucleocapsid Antibody, Chimeric mAb, Human IgG1 (Cat. No. NUN-CH15) with a linear range of 0.1-2 ng/mL (QC tested).

Protocol

Nucleocapsid protein ELISA

Immobilized SARS-CoV-2 Nucleocapsid protein, His Tag (BQ.1/Omicron) (Cat. No. NUN-C52Hx) 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 (Routinely tested).

Protocol

 
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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

Ni/Fe-MOF Electrochemical Transistor Biosensors with 3D Debye Space for Ultrasensitive Detection of Coronavirus Nucleocapsid Protein
Tan, Shen, Zheng et al
Small (2025)
Abstract: Electrochemical transistor (ECT) biosensors can achieve ultrahigh sensitivity, while keeping challenges for large biomolecules due to their sizes over the thickness of the electric double layer (EDL) causing a failure of sensing reaction. Here, wafer-level Ni/Fe-metal-organic framework (MOF) films and corresponding ECT biosensors are fabricated for the detection of coronavirus nucleocapsid protein, which realize an ultralow detection limit of 1 fg mL-1 and a wide detection range of 1 fg mL-1 to 100 pg mL-1. A 3D Debye space, originating from the unique stacking structure of nanosheets and nanoparticles in Ni/Fe-MOF film, is proposed to explain such ultrahigh sensitivity, which ensures the immune-binding and sensing process of the nucleocapsid protein large molecules located in the effective EDL space. Moreover, an appropriate Ni/Fe molar ratio is optimized to enhance the transmission of carriers, thus improving the signal-to-noise ratio and the sensing response. The Ni/Fe-MOF-ECT biosensors will find applications in highly sensitive detection for large biomolecules, and the 3D Debye space may be a design model for constructing other biosensors.© 2025 Wiley‐VCH GmbH.
Conserved Cysteines of a Putative Zinc Finger Motif in P48 Are Important for the Nuclear Egress of Nucleocapsids and the Envelopment of Occlusion-Derived Virions
Ma, Li, Wang et al
Viruses (2025) 17 (3)
Abstract: The open reading frame 103 (p48) of Autographa californica multiple nucleopolyhedrovirus (AcMNPV) is one of the 38 core baculovirus genes. p48 has been shown to be essential for the production of infectious budded virions (BVs), nuclear egress of nucleocapsids, envelopment of the nucleocapsid, and embedding of occlusion-derived virions (ODVs) into occlusion bodies (OBs). However, the structure-function relationship of P48 remains unclear. In this study, we showed that four conserved cysteines (C127, C130, C138, and C141) in P48 may form a zinc finger motif based on a predicted structure analysis, and we investigated the roles of these cysteines in P48 function. AcMNPV bacmids lacking p48 or containing mutated p48 were generated. Transfection/infection assays showed that C127, C130, C138, and C141 in P48 were crucial for infectious BV production. Electron microscopy analysis further confirmed that these four cysteines played critical roles in the transport of nucleocapsids out of the nucleus for BV production, and in ODV envelopment. These results demonstrate that the conserved cysteines C127, C130, C138, and C141, related to the putative zinc finger motif, are critical for P48 function in baculovirus infection.
Colorimetric Reverse Transcription Loop-Mediated Isothermal Amplification with Xylenol Orange Targeting Nucleocapsid Gene for Detection of Feline Coronavirus Infection
Khumtong, Rapichai, Saejung et al
Viruses (2025) 17 (3)
Abstract: Feline infectious peritonitis (FIP), a devastating disease with near-complete mortality, is caused by the feline coronavirus (FCoV) and affects domestic cats worldwide. Herein, we report the development of a reverse transcription loop-mediated isothermal amplification (RT-LAMP) assay incorporating xylenol orange (XO) as a visual indicator for FCoV detection. The assay employed six oligonucleotide primers targeting regions of the nucleocapsid (N) gene. Under optimized conditions (65 °C, 60 min), amplification products were detected through pH-dependent colour changes in the XO dye. The RT-LAMP-XO assay exhibited high specificity for FCoV, with no cross-reactivity against other common feline viral pathogens. While the detection limit (1.7 × 101 copies/µL) was an order of magnitude higher than that of qPCR, the method offered advantages in simplicity and speed compared to existing diagnostic approaches. Although less sensitive than qPCR, the RT-LAMP-XO assay may serve as a rapid screening tool when used in combination with additional primer sets. These findings demonstrate the potential utility of XO-based RT-LAMP as a simple, visual detection method for FCoV infection.
Emergence of Equine-like G3P[8] Rotavirus Strains Infecting Children in Venezuela
Vizzi, Rosales, Piñeros et al
Viruses (2025) 17 (3)
Abstract: Rotavirus alphagastroenteritidis is the leading cause of acute gastroenteritis worldwide in young humans and animals. In 2023-2024, a relatively high rotavirus detection rate (34.5%) was detected in children with diarrhea in Caracas. All rotavirus strains were typed as P[8], using a multiplex RT-PCR assay, while the G-type was not identified. This unusual pattern, not previously observed in Venezuela, prompted the VP7 gene sequencing of nineteen strains, which displayed a high sequence identity (99.3-100%) compatible with the G3 genotype. These strains clustered into a well-supported lineage IX encompassing human reassortants of equine-like G3P[8] strains described elsewhere, showing a very close genetic relationship (99.0-99.9%). Old G3 rotavirus isolates obtained from diarrheic samples in the past were included in the analysis and grouped into lineage I together with ancestral reference G3 strains. The novel G3P[8]s carry amino acid changes in VP7-neutralizing epitopes, compared with the RotaTeq-WI78-8-vaccine strain. Full genome sequencing of a representative strain revealed a genotype constellation including an equine-like G3P[8] in a DS-1-like backbone (I2-R2-C2-M2-A2-N2-T2-E2-H2), confirming the role of animal strains as a source of diversification, and the importance of unceasingly revising molecular typing strategies and vaccine efficacy to guarantee their success.
Showing 1-4 of 56484 papers.
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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
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