LL-37

Description

LL-37 Reference Material | Human Cathelicidin Antimicrobial Peptide

LL-37 (MW 4,493.31 g/mol) is the only cathelicidin-class antimicrobial peptide expressed in humans, cleaved from the C-terminus of hCAP-18. As a lyophilized reference material, it is supplied for antimicrobial peptide (AMP) research, innate immunity studies, and membrane disruption mechanism investigations.

Mechanism of Research Interest

LL-37 exerts bactericidal activity through amphipathic alpha-helical membrane insertion and pore formation in bacterial lipid bilayers. Against gram-positive and gram-negative species, it disrupts membrane integrity independent of specific receptor binding — a mechanistically distinct mode from conventional antibiotics. In immunology research, LL-37 functions as a TLR ligand (TLR2, TLR4 activation on immune cells), chemoattractant for neutrophils and monocytes, and modulator of NF-κB signaling.

Laboratory Research Applications

• AMP membrane disruption mechanism studies (MIC/MBC determinations)
• Biofilm inhibition assays (Staphylococcus, Pseudomonas, Candida)
• TLR2/TLR4 activation and innate immune pathway research
• Antiviral research — envelope disruption and host cell binding inhibition studies
• Skin biology research — rosacea, psoriasis, and keratinocyte inflammasome activation
• Angiogenesis studies — LL-37 VEGF-independent vessel formation research

Specifications

• Molecular Weight: 4,493.31 g/mol (37 residues)
• Form: Lyophilized powder
• Purity: ≥98% (HPLC verified)
• Storage: -20°C long-term; 2–8°C working stock; avoid repeated freeze-thaw

For laboratory research use only. Not for human or veterinary use.