HA is derived from influenza virus, erythrocyte lectin surface epitope has little effect on the spatial structure of the target protein.
HA Peptide (HA tag) is a nine amino acids peptide derived from the human influenza hemagglutinin (HA). HA Peptide is extensively used to isolate, purify, detect, and track the protein of interest in cell biology and biochemistry.
The HA-tagged complex consists of plasmid DNA, transferrin-polylysine, and influenza virus hemagglutinin HA-2 subunit N-terminal sequence-derived polylysine-conjugated peptides for the transfer of luciferase or β-galactosidase-tagged genes into K562 cells, HeLa cells, and BNL CL.2 hepatocytes. The presence of HA-conjugated polypeptides in the DNA complex allows the complex to disrupt membrane structures, allowing transferrin-polylysine-mediated gene transfer into cells.
In influenza viruses, the hemagglutinin (HA) protein mediates the binding of the virus to the cell surface and the subsequent fusion of the virus to the cell membrane. HA consists of the receptor-binding subunit HA1 and the membrane-fusion subunit HA2. The presence of the HA1yHA2 complex on the surface of the virus is inactive, and membrane fusion is regulated by the conformational state of the HA protein. When endosomes are in an acidic environment, HA proteins switch from their native conformation (non-membrane fusion) to fusion-active (membrane fusion) conformation. The native structure of HA is in a metastable state, and the membrane fusion conformation is obtained after destabilization of the native structure.