Recombinant Newcastle disease virus Hemagglutinin-neuraminidase (HN) is expressed in E. coli and covers the 115-473 amino acid region of the protein. This partial protein carries dual tags—an N-terminal 10xHis-tag and a C-terminal Myc-tag—which help with purification and detection. SDS-PAGE analysis confirms the product purity exceeds 85%. This product is designed for research use only and is not intended for therapeutic or diagnostic applications.
The Hemagglutinin-neuraminidase (HN) protein appears to play a critical role in Newcastle disease virus biology. It handles viral attachment to host cells and helps drive the fusion process during viral entry. HN also shows neuraminidase activity, which seems essential for viral spread through cleaving sialic acid residues. This protein has become a significant target in virology research, particularly when studying how viral infection works.
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.
1. Antigen for Anti-NDV Antibody Development
This recombinant HN protein fragment (115-473aa) may serve as an immunogen for generating polyclonal or monoclonal antibodies against Newcastle disease virus hemagglutinin-neuraminidase protein. The His and Myc tags make purification and detection straightforward during antibody screening. Researchers can immunize laboratory animals with this protein, then screen hybridoma clones or check serum antibody responses. The high purity (>85%) should minimize cross-reactivity with bacterial contaminants during immunization.
2. Protein-Protein Interaction Studies Using Tag-Based Pull-Down Assays
Both the N-terminal His-tag and C-terminal Myc-tag allow this recombinant HN protein to work in pull-down experiments aimed at identifying cellular proteins that interact with viral hemagglutinin-neuraminidase. Researchers can attach the protein to nickel-affinity resins through the His-tag or use anti-Myc antibodies for immunoprecipitation work. Cell lysates from different host species can be mixed with the immobilized HN protein to grab potential binding partners. Mass spectrometry analysis of co-purified proteins might reveal new host-pathogen interaction networks.
3. ELISA-Based Binding Assays for Receptor Studies
This tagged HN protein fragment appears useful for developing enzyme-linked immunosorbent assays to study receptor binding specificity and kinetics. The protein can coat ELISA plates and test binding to various sialic acid-containing glycoproteins or synthetic receptor analogs. The Myc-tag provides standardized detection through anti-Myc antibodies, which allows quantitative measurement of binding interactions. These assays could help researchers explore receptor binding domain characteristics within the 115-473aa region.
4. Structural and Biochemical Characterization Studies
The recombinant HN protein fragment provides material for biophysical characterization techniques like circular dichroism spectroscopy, dynamic light scattering, and analytical ultracentrifugation. The defined amino acid boundaries (115-473aa) let researchers examine folding properties and stability of this specific domain region. The dual tagging system makes protein quantification and tracking easier during biochemical assays. Such studies may offer insights into the structural properties of this particular HN domain when produced in bacterial systems.
