LL-37
LL-37 (5mg)
$120USD
Third-Party Tested
Independent lab verified
Batch-Specific CoA
Publicly accessible
YPB.244
Reference number
5mg
Lyophilized vial
Human cathelicidin antimicrobial peptide. The only cathelicidin in humans. Studied for innate immunity and wound healing.
Origin
LL-37 is the sole human cathelicidin antimicrobial peptide, first identified by Zanetti, Gennaro, and colleagues in the 1990s. It is derived from the C-terminal cleavage of the precursor protein hCAP-18 (human cationic antimicrobial protein, 18 kDa) by proteinase 3. The name LL-37 refers to its 37-amino-acid length and N-terminal dileucine motif.
Research Lineage
Gudmundsson et al. first characterized hCAP-18 in 1996. Subsequent work by Agerberth, Hancock, and others established LL-37 as a multifunctional host defense peptide with roles beyond direct antimicrobial activity. It has been studied in wound healing, angiogenesis, immune cell chemotaxis, and biofilm disruption in over 2,000 published papers.
Mechanism of Action
LL-37 forms an amphipathic alpha-helix that disrupts bacterial membranes through electrostatic interaction with negatively charged lipid components. Beyond direct antimicrobial activity, it activates the FPRL1 receptor (formyl peptide receptor-like 1) to recruit immune cells. It has been observed to promote angiogenesis via VEGF-A upregulation and to modulate TLR signaling in dendritic cells.
Structural Notes
37-amino-acid alpha-helical peptide cleaved from hCAP-18 precursor. Molecular weight: 4493.33 Da. Net charge: +6 at physiological pH. Amphipathic structure essential for membrane interaction.
Key References
Gudmundsson GH et al. Eur J Biochem. 1996;238(2):325-32.
Hancock RE, Sahl HG. Nat Biotechnol. 2006;24(12):1551-7.
Research Use Only. This product is intended for laboratory research purposes only. Not for human or veterinary use. Not for sale to minors.