This recombinant human acetylcholine receptor subunit alpha (CHRNA1) comes from a baculovirus expression system and spans amino acids 21 to 255 of the protein. A C-terminal 6xHis tag is included to make purification and detection more straightforward. The product achieves high purity levels—over 90% as confirmed by SDS-PAGE—which should provide reliable results in research settings.
The acetylcholine receptor subunit alpha (CHRNA1) plays a central role in acetylcholine receptor formation, making it crucial for neuromuscular junction signaling. This subunit helps bind acetylcholine, which enables neurotransmission to occur. Studying CHRNA1 appears essential for grasping how muscle activation works and may prove critical in research on neuromuscular diseases and synaptic physiology.
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 Human CHRNA1 is expressed in a Baculovirus expression system (insect cells), which is a eukaryotic system capable of producing properly folded proteins with some post-translational modifications. The protein is expressed as a partial fragment (21-255aa) representing approximately 90% of the mature protein but lacking the C-terminal transmembrane and intracellular domains. Since activity is unverified, the protein cannot be assumed to be correctly folded or bioactive. While the baculovirus system increases the probability of correct folding compared to prokaryotic systems, the absence of the full-length sequence (particularly the transmembrane domains essential for receptor function) and lack of co-expression with other receptor subunits significantly reduces the likelihood of proper nicotinic acetylcholine receptor function. The protein may be correctly folded at the domain level but is unlikely to exhibit ligand binding activity without the complete receptor complex.
1. Antibody Development and Validation Studies
This application is appropriate. The recombinant CHRNA1 fragment can serve as an effective immunogen for generating antibodies against the extracellular domain of the acetylcholine receptor alpha subunit. The C-terminal 6xHis tag facilitates purification and immobilization for screening assays. Even if the protein is not fully functional, antibodies can recognize linear epitopes. However, antibodies produced may not recognize conformational epitopes of the native, membrane-embedded receptor without validation against full-length protein.
2. Protein-Protein Interaction Studies
This application has significant limitations. While the His-tag enables technical feasibility for pull-down assays, the partial nature of the protein (lacking transmembrane domains) means it cannot authentically represent interactions that require the full receptor complex. Interactions identified may be fragment-specific and not physiologically relevant. This approach should be used with caution and results validated with full-length protein studies.
3. Biochemical Characterization and Stability Studies
This application is well-supported. The high purity makes this protein suitable for biophysical characterization (DLS, CD spectroscopy, etc.) to study the folding and stability of the CHRNA1 extracellular domain. These studies can provide valuable information about the recombinant protein's properties, even if it lacks full biological activity.
4. In Vitro Binding Assays and Ligand Screening
This application is problematic without activity verification. While the protein contains the putative ligand-binding domain, the absence of the full receptor structure and necessary subunits (β, γ, δ) means it is unlikely to exhibit native ligand binding properties. Screening for ligands using this partial fragment may yield false positives/negatives. This application should not be pursued without validating binding capability first.
Final Recommendation & Action Plan
This recombinant CHRNA1 partial fragment is most suitable for antibody development and biochemical characterization studies, where correct tertiary structure is less critical. For protein-protein interaction studies, focus on interactions specific to the extracellular domain only, with the understanding that findings may not reflect full receptor biology. Ligand binding studies should be avoided unless binding capability is first validated against known ligands. Recommended first steps include: (1) conducting biophysical analyses (circular dichroism, size exclusion chromatography) to confirm proper folding of the expressed fragment; (2) validating antibody specificity against native receptor preparations; (3) if pursuing interaction studies, using orthogonal methods to confirm any identified interactions. For functional studies, consider obtaining the full-length receptor expressed in appropriate systems.
