Recombinant Bovine Cathelicidin-4 (CATHL4) is produced through an E. coli expression system and includes an N-terminal 6xHis-SUMO tag. This protein represents the full-length mature protein sequence, spanning amino acids 131-143. SDS-PAGE analysis shows purity levels exceeding 90%, and this product is intended strictly for research applications, which appears to support consistent experimental outcomes.
Cathelicidin-4 functions as an antimicrobial peptide within the innate immune response, primarily helping defend against pathogens. It seems to play an important role in immune system regulation by breaking down microbial membranes. Given its apparent significance in innate immunity, CATHL4 has become a notable focus for researchers studying host defense and antimicrobial resistance.
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. Antimicrobial Peptide Structure-Function Studies
This recombinant bovine CATHL4 fragment (131-143aa) may prove useful for examining the structural elements that determine cathelicidin antimicrobial activity. Comparing it with other cathelicidin family members could reveal interesting patterns. The N-terminal 6xHis-SUMO tag makes purification straightforward and allows for immobilization during biophysical studies like circular dichroism spectroscopy and NMR analysis. Scientists can conduct targeted mutagenesis on this specific peptide region to identify which amino acid residues are critical for antimicrobial function. The high purity level (>90%) suggests it should work well for detailed biochemical tests examining how peptides interact with membranes and form secondary structures.
2. Antibody Development and Immunoassay Applications
The recombinant CATHL4 protein can function as an immunogen for creating specific antibodies against bovine cathelicidin-4 in research contexts. The N-terminal His-SUMO tag simplifies purification and offers options for oriented attachment to surfaces when developing ELISAs and screening antibodies. This protein appears suitable for creating research-grade immunoassays that detect and measure CATHL4 expression in bovine tissue samples or cell cultures. The specific expression region (131-143aa) provides a well-defined epitope target for producing region-specific antibodies for research purposes.
3. Protein-Protein Interaction Studies
The His-SUMO tagged CATHL4 can be used in pull-down assays to discover potential binding partners or target molecules that interact with this cathelicidin domain. The tag system allows attachment to nickel-affinity matrices for systematic screening of protein libraries or cell extracts. Scientists might use this protein in surface plasmon resonance or bio-layer interferometry experiments to characterize binding kinetics with possible interaction partners. The purified protein may work well for co-immunoprecipitation studies when investigating CATHL4-associated protein complexes in bovine cellular systems.
4. Comparative Cathelicidin Family Analysis
This bovine CATHL4 fragment could be valuable for comparative biochemical studies alongside other recombinant cathelicidin family members to better understand species-specific differences in this antimicrobial peptide family. The consistent expression system and purification method should allow direct comparison of physicochemical properties between different cathelicidin variants. Scientists can use this protein in phylogenetic and evolutionary studies that examine cathelicidin diversity across mammalian species. The defined peptide region enables focused comparative analysis of sequence-activity relationships within the broader cathelicidin superfamily.
