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AB273168

HRP Anti-SARS-CoV-2 nucleocapsid protein antibody [1A6] - Human IgG1 (Chimeric)

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(1 Publication)

Human Recombinant Monoclonal NCAP antibody - conjugated to HRP. Suitable for ELISA and reacts with SARS-CoV-2 samples. Cited in 1 publication.

View Alternative Names

Nucleoprotein, N, Nucleocapsid protein, NC, Protein N

1 Images
ELISA - HRP Anti-SARS-CoV-2 nucleocapsid protein antibody [1A6] - Human IgG1 (Chimeric) (AB273168)
  • ELISA

Supplier Data

ELISA - HRP Anti-SARS-CoV-2 nucleocapsid protein antibody [1A6] - Human IgG1 (Chimeric) (AB273168)

The binding activity of ab273168 with SARS-CoV-2 nucleocapsid protein.

Measured by its binding activity in a functional ELISA. Immobilized SARS-CoV-2 nucleocapsid protein at 2 μg/ml can bind ab273168 with an EC50 of 161.9 to 214.8 ng/ml.

  • Unconjugated

    Anti-SARS-CoV-2 nucleocapsid protein antibody [1A6] - Human IgG1 (Chimeric)

Key facts

Host species

Human

Clonality

Monoclonal

Clone number

1A6

Isotype

IgG1

Conjugation

HRP

Excitation/Emission
Carrier free

No

Reacts with

SARS-CoV-2

Applications

ELISA

applications

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Reactivity data

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Product details

Anti-SARS-CoV-2 nucleocapsid protein antibody [1A6] - Chimeric (ab272852) is a recombinant human/mouse chimeric monoclonal antibody consisting of Mouse scFv fused with human IgG1.

As the Fc region is human, an anti-Human secondary antibody should be used for detection.

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification
Storage buffer
pH: 7.4 Preservative: 0.03% Proclin 300 Constituents: PBS, 50% Glycerol (glycerin, glycerine)
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle|Store in the dark
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The SARS-CoV-2 nucleocapsid protein also known as N protein plays a central role in the packaging and replication of the viral RNA genome. It functions mechanically by binding to the viral RNA to facilitate its replication and encapsidation. The nucleocapsid protein is expressed within the virus-infected cells particularly in the cytoplasm. It is a highly conserved structural protein of the virus and has a molecular weight of approximately 50 kDa. Additionally the nucleocapsid protein aids in RNA binding and is essential for the virus's structural stability.
Biological function summary

The nucleocapsid protein of SARS-CoV-2 is involved in maintaining the integrity of the viral genome. It forms a ribonucleoprotein complex with the viral RNA which is necessary for viral replication. The nucleocapsid protein is integral in the formation of the virus's structure and assists in the assembly and release of new virus particles. It interacts with other viral proteins contributing to the stability and functioning of the virus.

Pathways

The nucleocapsid protein is involved in the viral life cycle and replication pathways. The protein participates in the RNA replication and transcription complex working alongside proteins such as the RNA-dependent RNA polymerase and other non-structural proteins. These interactions within the pathways are essential for the efficient replication of the viral genome and production of new viral particles which are key steps in the virus's lifecycle.

The nucleocapsid protein is directly linked to COVID-19 the disease caused by the SARS-CoV-2 virus. It is a target for various diagnostic tests such as the COVID ELISA test and corona IgA test due to its immunogenic properties. The presence of nucleocapsid antibodies in patients is often measured through tests like the ELISA test which helps in diagnosing COVID-19. The nucleocapsid protein's involvement in COVID-19 progression connects it with other viral proteins highlighting its significance in disease mechanisms and potential therapeutic targeting.
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Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:
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Target data

Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M (PubMed : 33264373). Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. Attenuates the stress granules formation by reducing host G3BP1 access to host mRNAs under stress conditions (PubMed : 34901782, PubMed : 36534661).. May block host chemokine function in vivo, facilitating viral replication and transmission (PubMed : 35921414). Acts by being secreted into the extracellular space where it competes to host chemokines for binding to host glycosaminoglycans (GAG) (PubMed : 35921414).. May induce inflammasome responses in cultured cells and mice. Acts by interacting with host NLRP3 to facilitate inflammasome assembly, which induces cytokine release that may play a role in COVID lung injury.
See full target information N
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Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Molecular diagnosis & therapy 27:583-592 PubMed37462793

2023

Development of an Affordable ELISA Targeting the SARS-CoV-2 Nucleocapsid and Its Application to Samples from the Ongoing COVID-19 Epidemic in Ghana.

Applications

Unspecified application

Species

Unspecified reactive species

Kesego Tapela,Precious C Opurum,Franklin Y Nuokpem,Becky Tetteh,Godfred K Siaw,Maria V Humbert,Sylvia Tawiah-Eshun,Anna Ibrahim Barakisu,Kwame Asiedu,Samuel Kojo Arhin,Aaron A Manu,Sekyibea N A Appiedu-Addo,Louisa Obbeng,Darius Quansah,Sylvester Languon,Claudia Anyigba,Daniel Dosoo,Nelson K O Edu,Daniel Oduro-Mensah,William Ampofo,Emmanuel Tagoe,Osbourne Quaye,Irene Owusu Donkor,Jewelna Akorli,Yaw Aniweh,Myron Christodoulides,Joe Mutungi,Yaw Bediako,Julian C Rayner,Gordon A Awandare,Christopher J McCormick,Peter Kojo Quashie
View all publications
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