Recombinant Leiurus quinquestriatus hebraeus Alpha-insect toxin LqhaIT is produced in E. coli and contains the complete mature protein sequence from amino acids 20 to 85. The protein carries an N-terminal 6xHis-SUMO tag, which makes purification and detection more straightforward. SDS-PAGE analysis indicates purity levels above 90%, making this product appropriate for research applications that demand high-quality protein preparations.
Alpha-insect toxin LqhaIT comes from the Yellow scorpion and appears to play an important role in modulating ion channels—particularly those that control insect neuronal signaling. Researchers studying neurotoxicology and ion channel pharmacology may find this toxin especially valuable, as it could provide insights into how insects become paralyzed and potentially help develop new pest control approaches.
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.
Leiurus quinquestriatus hebraeus Alpha-insect toxin LqhaIT is a scorpion toxin that requires precise folding, proper disulfide bond formation (typically with multiple conserved disulfide bonds), and specific tertiary structure for its functional activity in ion channel binding. The E. coli expression system cannot provide the eukaryotic folding environment or oxidative conditions for correct disulfide bond formation. The large N-terminal 6xHis-SUMO tag (∼15 kDa) is significantly larger than the toxin itself (∼7 kDa) and may sterically interfere with the protein's functional domains and ion channel-binding interfaces. While the full-length mature protein (20-85aa) contains all functional domains, the probability of correct folding with functional activity is extremely low.
1. Antibody Development and Immunoassay Applications
This application is highly suitable as antibody development relies on antigenic sequence recognition rather than functional protein folding. The full-length mature protein provides comprehensive epitope coverage for generating antibodies against LqhaIT. The high purity (>90%) ensures minimal contamination-related issues.
2. Biochemical Characterization and Stability Studies
Basic biophysical characterization can be performed, but will not reflect native toxin properties. Techniques like circular dichroism may assess secondary structure but cannot verify functional disulfide bonding. The SUMO tag will dominate the protein's physical properties.
Final Recommendation & Action Plan
This SUMO-tagged scorpion toxin expressed in E. coli is unsuitable for functional studies due to the severe steric interference from the large tag relative to the small toxin size and the inability of the expression system to support proper disulfide bond formation. Avoid all interaction-based applications. Application 1 (antibody development) can proceed immediately. For reliable toxin research, use tag-free toxin produced by chemical synthesis or eukaryotic expression systems that support proper disulfide bond formation and preserve native conformation.
