Thermo Fisher Scientific SARS-CoV-2 Nucleocapsid (aa1-419), His Tag Recombinant Protein

Applications

Tested Dilution

Publications

Western Blot (WB)

Assay-dependent

-

ELISA (ELISA)

Assay-dependent

-

Functional Assay (Functional)

Assay-dependent

-

Control (Ctrl)

Assay-dependent

-

Product Specifications

Species

Virus

Expression System

E. coli

Amino acid sequence

SARS-CoV-2 Nucleocapsid, Met1-Ala419 with an N-terminal His-tag

Tag

His-tag

Molecular weight

49.4 kDa

Class

Recombinant

Type

Protein

Purity

>95% by SDS-PAGE; >95% by HPLC

Endotoxin concentration

<1.0 EU/µg

Activity

Measured by its binding ability in a functional ELISA. Immobilized Recombinant SARS-CoV-2 Nucleocapsid at 2 µg/mL (100 µL/well) can bind Anti-Nucleocapsid antibody with a linear range of 0.12-1.64 ng/mL.
Measured by its binding ability in a functional ELISA. Immobilized Recombinant SARS-CoV-2 envelope Protein at 2µg/mL (100 µL/well) can bind Recombinant SARS-CoV-2 Nucleocapsid protein, the EC50 of Recombinant SARS-CoV-2 Nucleocapsid protein is 41.10 ng/mL.

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Concentration

0.56 mg/mL

Purification

purified

Storage buffer

20mM tris, pH 8.0, with 0.1mM EDTA, 500mM NaCl, 10% glycerol

Contains

no preservative

Storage conditions

-80°C

Shipping conditions

Dry ice

Product Specific Information

Animal Origin Free

Storage: Store the lyophilized protein at -20°C to -80°C for long term. This product is stable at -70°C for up to 1 year from the date of receipt.

Target Information

SARS-CoV-2 Nucleocapsid Protein is associated with nucleic acid. It is the most abundant protein for coronavirus. Because of the strong immunogenicity of coronavirus Nucleocapsid, it is believed that SARS-CoV-2 Nucleocapsid Protein has potential value for the diagnosis of the virus. The SARS-CoV-2 N protein is an abundant RNA-binding protein critical for viral genome packaging, yet the molecular details that involve this process are poorly understood. N protein contains three dynamic disordered regions that house putative transiently-helical binding motifs. The two folded domains interact minimally such that full-length N protein is a flexible and multivalent RNA-binding protein. SARS-CoV-2 causes illnesses ranging from the common cold to severe diseases.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.