Recombinant Influenza A Virus H3N2 Hemagglutinin Protein, CF

When Recombinant Human Galectin-1 (1152-GA) immobilized at 10.00 μg/mL, 100 μL/well, the concentration of Recombinant Influenza A Virus H3N2 Hemagglutinin His-tag (Catalog # 10944-HA) that produces 50% of the optimal binding response is 0.35 - 3.50 μg/mL.

2 μg/lane of Recombinant Influenza A Virus H3N2 Hemagglutinin His-tag Protein (Catalog # 10944-HA) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 80-90 kDa.

• Reactivity: V
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Influenza A Virus H3N2 Hemagglutinin Protein, CF Summary

• Additional Information: His-tag
• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human Galectin-1 (Catalog # 1152-GA) immobilized at 10.00 μg/mL, 100 μL/well, the concentration of Recombinant Influenza A Virus H3N2 Hemagglutinin His-tag (Catalog # 10944-HA) that produces 50% of the optimal binding response is 0.35-3.50 μg/mL.
• Source: Human embryonic kidney cell, HEK293-derived influenza a virus h3n2 Hemagglutinin protein
  Gln17-Trp530, with a C-terminal 6-His tag
• Accession #: Q91MA7.1
• N-terminal Sequence: No results obtained: Gln17 predicted
• Protein/Peptide Type: Recombinant Enzymes
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
• Endotoxin Note: <1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 58 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 80-90 kDa, under reducing conditions.

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
• Reconstitution Instructions: Reconstitute at 100 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Influenza A Virus H3N2 Hemagglutinin Protein, CF

• HA
• Hemagglutinin

Background

Influenza A (H3N2) has predominated recent influenza seasons, which caused several hospitalizations in many countries (1). H3N2 viruses have been in circulation since the onset of the 1968 pandemic (2). This strain was a reassortant, composed of the six gene segments from H2N2 viruses, but with the hemagglutinin and polymerase basic protein 1 segments derived from an avian source (3, 4). The hemagglutinin protein of the Influenza A virus (strain A/Hong Kong/1/1968 H3N2) is composed of 550 residues, which includes the Hemagglutinin chains HA1 and HA2 (5).   Hemagglutinin (HA) and Neuraminidase (NA) and are the two predominant membrane glycoproteins found on the surface of influenza virus. HA is a lectin that binds sialic acid on host cell membrane. NA is a sialic acid hydrolase that specifically clips off terminally located sialic acid on host cell surface. The two proteins are essential for the infectious cycle of the influenza virus.  Galectin-1 can bind to the envelope glycoproteins of influenza virus and inhibit viral infectivity, which may be attributed to the multivalent binding and cross-linking activities of galectin-1. Furthermore, galectin-1 may also be explored for targeting other viruses with glycoproteins on their surface (6).

1. Wan, H. et al. (2019) Nat. Microbiol. 4:2216.
2. Krause, J.C. et al. (2012) J. Virol. 86:6334.
3. Kawaoka, Y. et al. (1989) J. Virol. 63:4603.
4. Alymova, I.V. et al. (2011) J. Virol. 85:12324.
5. Brown, E.G. et al. (2001) Proc. Natl. Acad. Sci. USA 98:6883.
6. Yang, M.L. et al. (2011) J. Virol. 85:10010.

Bioinformatics

• Uniprot:
  • Q91MA7.1()