Abcam, ab316332, Anti-MERS-Cov Nucleocapsid protein antibody [abd211]

Size: 10µg-TRIAL / 20µg / 100µg / 1mg
Human Recombinant Monoclonal NCAP antibody. Suitable for WB, ICC/IF, I-ELISA and reacts with Recombinant fragment - MERS-CoV, Transfected cell lysate - MERS-CoV, Transfected cell line - MERS-CoV samples.
Key facts
Host species:Human,
Clonality:Monoclonal,
Clone number:abd211,
Isotype:IgG1,
Carrier free:No,
Reacts with:MERS-CoV,
Applications:I-ELISA, WB, ICC/IFSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:The exact immunogen used to generate this antibody is proprietary information.,
Specificity:This antibody does not cross-react with recombinant Human coronavirus NL63 nucleocapsid, SARS-CoV nucleocapsid, Human coronavirus OC43 nucleocapsid, Human coronavirus HKU1-Cov nucleocapsid and Human coronavirus 229E nucleocapsid.

Product details:
What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:
- High batch-to-batch consistency and reproducibility
- Improved sensitivity and specificity
- Long-term security of supply
- Animal-free batch production
For more information, read more on
recombinant antibodies
Want a custom formulation?
This antibody clone is manufactured by Abcam. If you require a custom buffer formulation or conjugation for your experiments, please contact orders@abcam.com

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-pH: 7.2 - 7.4Preservative: 0.01% Sodium azideConstituents: PBS, 40% Glycerol (glycerin, glycerine), 0.05% BSA, 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

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
The MERS-CoV Nucleocapsid protein also called the N protein plays an important role in the assembly process of the Middle East Respiratory Syndrome Coronavirus (MERS-CoV). The N protein is a structural component that packages the viral RNA genome into a helical ribonucleocapsid which assists in protecting the RNA. This protein which has a mass of approximately 48 kDa is expressed during the viral infection in the host cells particularly in the cytoplasm where it facilitates the encapsulation of the viral genome.
Biological function summary
The MERS-CoV Nucleocapsid protein interacts closely with other viral proteins including the membrane (M) protein to ensure successful viral replication and assembly. This protein does not work alone; it is part of the larger ribonucleoprotein complex which plays an essential role in stabilizing the viral RNA. Its interaction with the M protein helps in localizing the N protein to specific sites in the host cell preparing the components necessary for virion assembly and release.
Pathways
The MERS-CoV Nucleocapsid protein engages in processes important for viral pathogenesis and host cell interaction. The protein is part of the coronavirus replication and transcription complex pathway. Within this matrix it associates with non-structural proteins like the RNA-dependent RNA polymerase to enhance RNA synthesis. Additionally it partakes in modulation of host processes to evade the immune response a pivotal aspect of how coronaviruses maintain infection and propagate within the host.
The MERS-CoV Nucleocapsid protein is intimately associated with Middle East Respiratory Syndrome (MERS) a severe respiratory illness. This protein aids the virus in evading the host immune response potentially contributing to disease severity. N protein interactions with host cellular machinery combined with the immune evasion tactics offer insights into viral pathogenicity and might reveal potential therapeutic targets. Understanding these interactions can shed light on how interventions might disrupt the viral life cycle and ameliorate disease impact.