This antibody is specific for the seasonal H1N1 influenza NP and will not recognize the corresponding NP sequence from the swine-origin H1N1 influenza (A/California/14/2009 (H1N1)).
Purification
Seasonal H1N1 Nucleocapsid Protein Antibody is affinity chromatography purified via peptide column.
Immunogène
NP antibody was raised against a synthetic peptide from the seasonal H1N1 NP protein. The immunogen is located within amino acids 350 - 400 of Seasonal H1N1 Nucleocapsid Protein.
NP
Reactivité: Influenza A Virus, Virus
WB, IHC (fro), IHC (p)
Hôte: Lapin
Polyclonal
unconjugated
Indications d'application
NP antibody can be used for the detection of the NP protein from the H1N1 strain of Seasonal Influenza A in ELISA.
Restrictions
For Research Use only
Format
Liquid
Concentration
1 mg/mL
Buffer
Seasonal H1N1 Nucleocapsid Protein Antibody is supplied in PBS containing 0.02 % sodium azide.
Agent conservateur
Sodium azide
Précaution d'utilisation
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Stock
-20 °C,4 °C
Stockage commentaire
Seasonal H1N1 Nucleocapsid Protein antibody can be stored at 4°C for three months and -20°C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.
Seasonal H1N1 Nucleocapsid Protein Antibody: Influenza A virus is a major public health threat, killing more than 30, 000 people per year in the USA. In early 2009, a novel swine-origin influenza A (H1N1) virus (S-OIV) was identified in specimens obtained from patients in Mexico and the United States. The influenza A virus polymerase transcribes and replicates eight virion RNA (vRNA) segments, among which the nucleocapsid protein (NP), thought to control whether mRNA or cRNA is produced. The nucleoprotein (NP), which has multiple functions during the virus life cycle, possesses regions that are highly conserved among influenza A, B, and C viruses. It was recently found several NP mutations that affected the efficient incorporation of multiple viral-RNA (vRNA) segments into progeny virions even though a single vRNA segment was incorporated efficiently. This indicates that the respective conserved amino acids in NP may be critical for the assembly and/or incorporation of sets of eight vRNA segments.