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MERS Nucleocapsid protein, His Tag

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NUN-M52H5-100ug
$410.00
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NUN-M52H5-1mg
$2,945.00
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NUN-M52H5
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Product Details
Performance Data
Reviews & Citations
Resources
  • Product Details
  • Performance Data
  • Reviews & Citations
  • Important Statement
  • Resources
Synonyms

Nucleocapsid protein, NP, Protein N

Source

MERS Nucleocapsid protein, His Tag (NUN-M52H5) is expressed from human 293 cells (HEK293). It contains AA Met 1 - Asp 413 (Accession # K0BVN3-1).

Predicted N-terminus: Met 1

Molecular Characterization
Other Tags and Version Biotin & Other Labeled Version

This protein carries a polyhistidine tag at the C-terminus. This protein contains a furin cleavage site, 251-RHKR-254, and is partially processed into N and C-terminal fragment with calculated MW of 17.1 kDa and 19.7 kDa respectively. The protein migrates as 23-25 kDa (C-terminus) and 46-73 kDa (full length) under reducing (R) condition (SDS-PAGE) due to glycosylation.

Endotoxin

Less than 1.0 EU per μg by the LAL method / rFC method.

Purity

>90% as determined by SDS-PAGE.

Formulation

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

Contact us for customized product form or formulation.

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.

Shipping and Storage

This product is shipped at ambient temperature.

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:
  • -20°C to -70°C for 12 months in lyophilized state;
  • -70°C for 3 months under sterile conditions after reconstitution.
ACRO Quality Management System

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.