LL-37

99.167%
LL37-5-601
5.53mg
$94.00

LL-37 is a human cathelicidin antimicrobial peptide used in research related to immune modulation and host-defense pathways.

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Disclaimer
For Research Use Only. Not for human consumption or therapeutic treatment.

About LL-37

LL-37 is a naturally occurring 37-amino-acid peptide produced by immune and epithelial cells as part of the body’s innate defense system. It is frequently studied in antimicrobial, inflammatory, and wound-environment research models. LL-37 has demonstrated broad interactions with bacterial membranes, immune receptors, and cytokine signaling pathways, making it a valuable tool for studying host-pathogen dynamics. Researchers often explore LL-37 for its multifunctional roles in immunity, cellular communication, and environmental stress response.

Product Specifications
LL-37 Lyophilized Powder in 3ml vial
Application
Host-defense and immune pathway research
Appearance
Solid, white powder in 3mL glass ampule
Chemical Formula
C203H404N72O45
CAS number
259954-53-6
Molecular Weight
~4491.3 g/mol

FAQs

What is LL-37 peptide?
LL-37 is a 37-amino acid peptide and the only member of the human cathelicidin family. It is encoded by the CAMP gene and processed from the precursor protein hCAP18. The peptide forms an amphipathic alpha-helical structure under physiological conditions, with a net positive charge of +6 at physiological pH. It was first characterized in neutrophils and is also produced by epithelial cells, macrophages, and other immune cells.
LL-37 is studied for its antimicrobial activity against gram-positive and gram-negative bacteria, fungi, and certain viruses. Research published in Scientific Reports and Frontiers in Immunology also examines its role in immune modulation, including chemoattraction of neutrophils, monocytes, and T cells via the formyl peptide receptor-like 1 (FPRL-1). Additional areas of study include biofilm disruption, wound re-epithelialization, and angiogenesis.
LL-37 targets bacterial membranes through electrostatic interaction between its positively charged residues and the negatively charged lipid components of bacterial cell walls. Studies published in Nature Scientific Reports show that LL-37 perforates both the inner and outer membranes of E. coli in a time-dependent and concentration-dependent manner. The peptide forms oligomeric structures on membrane surfaces, which is a distinct mechanism compared to other antimicrobial peptides.
Yes. LL-37 activates multiple receptor pathways studied in immunology, including FPRL-1, the purinergic receptor P2X7, and the epidermal growth factor receptor. Research in the journal Cell Immunology describes LL-37 as an immunomodulator that stimulates cytokine release, suppresses neutrophil apoptosis at sub-micromolar concentrations, and forms complexes with DNA that activate plasmacytoid dendritic cells and type I interferon production.
Limitless Peptides sells LL-37 as a lyophilized powder in a sealed 3mL glass ampule. The product is Janoshik verified for identity, potency, and purity. LL-37 is sold for research use only and is not approved for human consumption. The product page includes a link to the third-party Janoshik verification report and the certificate of analysis from the manufacturer.