This Recombinant Influenza A virus Hemagglutinin (HA) comes from E. coli expression and covers amino acid region 18-529, representing a partial protein construct. The design includes an N-terminal 10xHis-tag that simplifies purification and detection. SDS-PAGE analysis confirms the product achieves greater than 85% purity, which appears adequate for most research applications with minimal contamination concerns.
Hemagglutinin functions as a surface glycoprotein that's central to Influenza A virus biology. The protein enables viral entry into host cells through binding to sialic acid receptors. This makes it a prime target for vaccine development and antiviral research, given its role in virus-host interactions and capacity to trigger immune responses. Researchers generally consider understanding HA's structure and function essential for moving influenza research and therapeutic strategies forward.
Potential Applications
Note: The applications listed below are based on what we know about this protein's biological functions, published research, and experience from experts in the field. However, we haven't fully tested all of these applications ourselves yet. We'd recommend running some preliminary tests first to make sure they work for your specific research goals.
Based on the provided information, the recombinant Influenza A virus Hemagglutinin (HA) protein is highly unlikely to be correctly folded or bioactive. HA is a complex viral surface glycoprotein that requires: 1) Proper glycosylation (N-linked glycans at multiple sites) for correct folding and stability; 2) Formation of specific disulfide bonds; 3) Trimerization into its functional state. The E. coli expression system cannot provide N-linked glycosylation and often fails to properly fold complex eukaryotic viral proteins. The partial length (18-529aa) likely lacks both the signal peptide and transmembrane domain, which are important for native conformation. While the N-terminal His-tag is relatively small, the combination of prokaryotic expression and missing structural elements makes correct folding improbable. The >85% purity indicates some impurities but doesn't overcome the fundamental folding limitations.
This E. coli-expressed HA protein should be limited to applications that don't require native conformation, such as generating linear epitope-specific antibodies or as a control for non-conformational assays. This recombinant HA protein can be used for antibody development but will primarily generate antibodies recognizing linear epitopes rather than conformational epitopes of native HA. The lack of glycosylation and potential misfolding means antibodies may not recognize authentic viral HA in neutralization assays. It can serve as an antigen for initial screening, but antibodies must be validated using properly glycosylated HA or whole virus. The His-tag may also induce tag-specific antibodies that don't recognize native HA.
For any functional studies, obtain HA protein expressed in mammalian or insect cell systems that provide proper glycosylation and folding. If using this specific preparation, validate any findings with eukaryotic-expressed HA controls and clearly state the limitations of the unglycosylated protein in publications. Priority should be given to obtaining properly processed HA for vaccine research, structural studies, and interaction analyses.
