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Nipah/Hendra virus Nucleocapsid (F5N9K) Rabbit Monoclonal Antibody #32952

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  • WB
  • IHC

    Product Specifications

    REACTIVITY Vir
    SENSITIVITY Endogenous (IHC-P), Transfected (W)
    MW (kDa) 65
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IHC-Immunohistochemistry 
    Species Cross-Reactivity Key:
    • Vir-Virus 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunohistochemistry (Paraffin) 1:400 - 1:1600

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Nipah/Hendra virus Nucleocapsid (F5N9K) Rabbit Monoclonal Antibody recognizes endogenous levels of total Nipah/Hendra virus nucleocapsid protein. This antibody has been shown to recognize both Malaysia and Bangladesh strains of Nipah virus.

    Species Reactivity:

    Virus

    Source / Purification

    Nipah/Hendra virus Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala530 of Nipah/Hendra virus nucleocapsid protein.

    Background

    Nipah virus (NiV) and Hendra virus (HeV) are highly pathogenic zoonotic paramyxoviruses belonging to the Henipavirus genus. They both possess a non-segmented, negative-sense single-stranded RNA genome, which is tightly encapsidated by the nucleocapsid (N) protein to form a helical ribonucleoprotein (RNP) complex, the fundamental unit for viral RNA synthesis and genome protection (1). The N protein, which is largely conserved between the two viruses, is a major structural component and a key player in its replication cycle. The primary function of the NiV/HeV N protein is to encapsidate viral genomic and antigenomic RNA. Encapsidation is essential for genome protection, template assembly for RNA synthesis, and nucleocapsid assembly. It also interacts with other viral proteins, such as the viral phosphoprotein (P), which acts as a chaperone for newly synthesized N protein subunits (2). Understanding the structure and function of the NiV and HeV N protein is critical for developing targeted antiviral therapies against this and other highly pathogenic viruses in the Paramyxoviridae family (3).

    Alternate Names

    Hendra henipavirus N protein; nucleocapsid

    For Research Use Only. Not for Use in Diagnostic Procedures.
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