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Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

Hendra henipavirus Nucleocapsid (F5N9K) Rabbit mAb #32952

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  • WB
  • IHC

    Supporting Data

    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

    Hendra henipavirus Nucleocapsid (F5N9K) Rabbit mAb recognizes transfected levels of total Hendra henipavirus nucleocapsid protein.

    Species Reactivity:

    Virus

    Source / Purification

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

    Background

    Hendra virus (HeV) is a highly pathogenic zoonotic paramyxovirus belonging to the Henipavirus genus. It possesses 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 is a major structural component of the virus and a key player in its replication cycle. The primary function of the HeV N protein is the encapsidation of the 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 Hendra henipavirus N protein is critical for developing targeted antiviral therapies against this and other highly pathogenic viruses in the Paramyxoviridae family (3).
    For Research Use Only. Not for Use in Diagnostic Procedures.
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