Recombinant Dahlia merckii Defensin-like protein 1

Recombinant Dahlia merckii Defensin-like protein 1 is produced in E. coli and features an N-terminal 6xHis-B2M tag for easier purification and detection. The protein appears to be expressed as a full-length peptide covering amino acids 1 to 50, achieving what seems to be a purity level exceeding 90%, as verified by SDS-PAGE analysis. This product is intended for research use only.

Defensin-like proteins are small, cysteine-rich peptides that likely play a role in the innate immune response of plants. They may participate in various defense mechanisms by disrupting pathogen cell membranes. These proteins could prove valuable in research focused on plant immunity, offering insights into pathogen resistance and potential applications in agriculture.

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.

Dahlia merckii defensin-like protein 1 is a small cysteine-rich protein that requires precise folding, proper disulfide bond formation (typically with 3-4 conserved disulfide bonds), and specific tertiary structure for its antimicrobial activity. The E. coli expression system cannot provide the eukaryotic oxidative environment for correct disulfide bond formation. The large N-terminal 6xHis-B2M tag (∼12 kDa B2M plus His-tag) is significantly larger than the defensin itself (∼6 kDa) and will severely sterically interfere with the protein's functional domains and antimicrobial activity. The probability of correct folding with functional activity is extremely low.

This B2M-tagged defensin construct is fundamentally unsuitable for defensin research due to the severe steric interference from the massive tag relative to the small defensin size, combined with the inability of E. coli to form the essential disulfide bonds required for defensin functionality. All functional applications should be avoided. The only limited application is generating antibodies, though the response will be dominated by anti-tag antibodies. For reliable defensin research, use tag-free defensin produced by chemical synthesis or eukaryotic expression systems that support proper disulfide bond formation.