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Influenza A H3N2 (A/California/7/2004) Hemagglutinin / HA Protein (His Tag)

HA

Catalog Number P40118-V08B
Organism Species H3N2
Host Baculovirus-Insect cells
Synonyms HA
Molecular Weight The recombinant hemagglutinin of Influenza A virus (A/California/7/2004(H3N2)) comprises 525 amino acids and has a predicted molecular mass of 59.2 kDa. The apparent molecular mass of the protein is approximately 70.6 kDa in SDS-PAGE under reducing conditions.
predicted N Gln 17
SDS-PAGE
Purity > 95 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the Influenza A virus (A/California/7/2004(H3N2)) hemagglutinin (ABW80975.1) (Met1-Trp530) was expressed with a C-terminal polyhistidine tag.
Bio-activity 1. Measured by its ability to bind with Neu5Aca2-3Galb1-4GlcNAcb-PAA-biotin (01-077) using the Octet RED System.
2. Measured by its ability to bind with Neu5Aca2-6GalNAca-PAA-biotin (01-059) using the Octet RED System.
3. Measured by its ability to agglutinate guinea pig red blood cells. HA titer is 0.2-0.8 ng/mL for 1% GRBC.
Research Area Microbiology |Pathogenic microorganism |viruses |animal virus |viral illness |Viral tract respiratory illness |
Formulation Lyophilized from sterile 20 mM Tris, 500 mM NaCl,10 % glycerol, pH 7.0.
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background
Reference
  • White JM, Hoffman LR, Arevalo JH, et al. (1997). "Attachment and entry of influenza virus into host cells. Pivotal roles of hemagglutinin". In Chiu W, Burnett RM, Garcea RL. Structural Biology of Viruses.
  • Suzuki Y (March 2005). "Sialobiology of influenza: molecular mechanism of host range variation of influenza viruses". Biol. Pharm. Bull. 28 (3): 399–408.
  • Senne DA, Panigrahy B, Kawaoka Y, et al. (1996). "Survey of the hemagglutinin (HA) cleavage site sequence of H5 and H7 avian influenza viruses: amino acid sequence at the HA cleavage site as a marker of pathogenicity potential". Avian Dis. 40 (2): 425–37