About LL-37
LL-37 is the only human cathelicidin antimicrobial peptide and is widely used in immunology and innate-immunity research. Supplied as a lyophilized powder for laboratory investigations into innate immune signaling, host-defense pathway markers, and immunomodulatory mechanisms in controlled experimental models. Each batch is verified for identity and purity using HPLC and mass spectrometry. Supplied as: Lyophilized powder Purity: >95-99 (HPLC verified) Storage: Store desiccated at ?20�C for long-term. Short-term room temperature exposure (around 1 month) during shipping/handling is generally acceptable if kept sealed, dry, and protected from heat/light. Designation: FOR RESEARCH USE ONLY. Not intended for human or animal consumption.
Latest Research
Vitamin D receptor BsmI haplotype BB confers lower 25(OH)D levels during tuberculosis: a pilot cross-sectional study.
Recent research on LL-37: Vitamin D receptor BsmI haplotype BB confers lower 25(OH)D levels during tuberculosis: a pilot cross-sectional study.
Read Full Study on PubMedFull-length brain-derived α-synuclein fibril models reveal fuzzy-coat control of peptide recognition.
Recent research on LL-37: Full-length brain-derived α-synuclein fibril models reveal fuzzy-coat control of peptide recognition.
Read Full Study on PubMedAdditional Studies
Cathelicidin LL-37 inhibits angiogenesis and migration in gastric cancer via inhibition of NF-κB/IL-6 signaling.
Recent research on LL-37: Cathelicidin LL-37 inhibits angiogenesis and migration in gastric cancer via inhibition of NF-κB/IL-6 signaling.
Read on PubMedRational hybrid design and computational characterization of PA-Hyb1: a novel peptide inhibitor targeting the MexB efflux pump in Pseudomonas aeruginosa.
Recent research on LL-37: Rational hybrid design and computational characterization of PA-Hyb1: a novel peptide inhibitor targeting the MexB efflux pump in Pseudomonas aeruginosa.
Read on PubMedCalmodulin-tagging prevents aggregation and facilitates the proteolytic release of the recombinant human cathelicidin LL-37 by accommodating its hydrophobic regions.
Recent research on LL-37: Calmodulin-tagging prevents aggregation and facilitates the proteolytic release of the recombinant human cathelicidin LL-37 by accommodating its hydrophobic regions.
Read on PubMedCoordination chemistry and antimicrobial activity of LL-37, its C-terminal fragment, and a peptidomimetic analogue.
Recent research on LL-37: Coordination chemistry and antimicrobial activity of LL-37, its C-terminal fragment, and a peptidomimetic analogue.
Read on PubMedEmerging antimicrobial peptides in gastrointestinal disorders: Dual role in immunity and therapy.
Recent research on LL-37: Emerging antimicrobial peptides in gastrointestinal disorders: Dual role in immunity and therapy.
Read on PubMedTargeted delivery of antimicrobial peptide LL-37 via ferritin fusion improves antibacterial and anti-inflammatory outcomes in a murine sepsis model.
Recent research on LL-37: Targeted delivery of antimicrobial peptide LL-37 via ferritin fusion improves antibacterial and anti-inflammatory outcomes in a murine sepsis model.
Read on PubMedRelated Research
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Research Disclaimer
The research articles and studies referenced on this page are for informational purposes only. All products are sold for research use only and are not intended for human or animal consumption. The information provided does not constitute medical advice, diagnosis, or treatment. Always consult with qualified healthcare professionals before making any decisions related to health or medical treatment.
