SARS-CoV-2 Nucleocapsid Protein, His Tag

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SARS-CoV-2 Nucleocapsid Protein, His Tag

Note: This product is for research use only.

Product Details

Target	SARS-CoV-2 Nucleocapsid
Target Type	Viral Protein
Protein Type	Recombinant
Origin	SARS-CoV-2
Source	E. coli
Purification Tag	This product is labelled with His tag.
Purity	> 90 % as determined by SDS-PAGE
Molecule Mass	The protein has a predicted MW of 46.0 kDa.
Endotoxin Level	Less than 1.0 EU per μg by the LAL method.
Formulation	Supplied as 0.2 μm filtered solution in PBS pH 7.4 containing 10% glycerol.
Application Notes	This product is specifically designed for serological test development.

Shipping & Storage Information

Shipping	This product is shipped in dry ice unless customers require otherwise.
Storage	This product can be stored stably for 3 months under sterile conditions from −20 to −80 °C. Please avoid freeze-thaw cycles.

Coronavirus Nucleocapsid Protein Background Information

The coronavirus nucleocapsid (N) protein is the most abundant protein in the virus-infected cells. It consists of two RNA-binding domains connected by a central spacer, which contains a serine- and arginine-rich (SR) region ^[1]. Its main function is to bind to the viral RNA genome to form the ribonucleoprotein core. In addition, the coronavirus nucleocapsid (N) protein has been shown to modulate the host cellular machinery and may serve regulatory roles during its viral life cycle ^[2].

Figure 1. Realistic three-dimensional illustration of COVID-19 virus structure diagram. The red box labeled part is the nucleocapsid protein, which is the main structural component of the coronavirus virion.

Since the SARS-CoV-2 pandemic, research into the detection and treatment of Coronavirus has never stopped. Alfa Chemistry is committed to providing customers with a series of antigens for diagnostics to meet the various needs of customers. If the product you are looking for is not in our catalog, please contact us. We will be happy to provide you with customized synthesis services.

References

Koetzner, C. A.; et al. Analysis of a crucial interaction between the coronavirus nucleocapsid protein and the major membrane-bound subunit of the viral replicase-transcriptase complex. Virology. 2022, 567: 1-14.
Chang, C.; et al. The SARS coronavirus nucleocapsid protein–forms and functions. Antiviral research. 2014, 103: 39-50.

Our products and services are for research use only and cannot be used for any clinical purposes.

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