Host-Defense Models
LL37 is studied as an endogenous antimicrobial peptide involved in epithelial and immune host-defense pathways.
Overview
What is LL37?
LL37 is a human cathelicidin antimicrobial peptide studied in innate immunity, epithelial barrier biology, microbial interaction models, and inflammation signaling. Research focuses on membrane interactions, immune-cell chemotaxis, cytokine modulation, and host-defense pathways in vitro and in animal models.
LL37 (Human Cathelicidin Antimicrobial Peptide LL-37) is supplied strictly as a reference material for in vitro and preclinical investigation. All characterization data described here is drawn from peer-reviewed literature and laboratory analysis; nothing herein constitutes a claim of clinical effect in humans.
Investigational Scope
Documented Research Areas
The following domains summarize directions explored across published studies and laboratory models. Each reflects observations reported in rodent models, in vitro systems, or the peer-reviewed record.
Microbial Membrane Interaction
Laboratory assays examine LL37 interaction with lipid membranes and microbial envelope models.
Cytokine and Chemotaxis Research
Studies investigate LL37 effects on immune-cell migration, cytokine signaling, and inflammatory pathway modulation.
Epithelial Response Models
Research includes epithelial wound models, barrier signaling, and interaction with nucleic acid immune complexes.
Proposed Mechanism
Mechanistic Pathway
Mechanistic steps below are hypothesized from in vitro assays and animal-model data reported in the literature. They describe biochemical interactions observed under controlled experimental conditions.
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1
Amphipathic Helix Formation
LL37 can form amphipathic alpha-helical structures that interact with negatively charged membranes.
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2
Membrane Disruption Models
The peptide is studied for pore formation, membrane perturbation, and microbial envelope interaction under assay conditions.
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3
Immune Receptor Signaling
LL37 can influence immune signaling pathways, including interactions with formyl peptide receptors and nucleic acid sensing systems.
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4
Chemotactic Activity
Research examines LL37-mediated recruitment and activation of immune cells in innate-defense models.
Technical Data
Molecular Specifications
| Amino Acid Sequence | Leu-Leu-Gly-Asp-Phe-Phe-Arg-Lys-Ser-Lys-Glu-Lys-Ile-Gly-Lys-Glu-Phe-Lys-Arg-Ile-Val-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg-Asn-Leu-Val-Pro-Arg-Thr-Glu-Ser |
|---|---|
| Molecular Weight | 4,493.3 g/mol |
| Molecular Formula | C205H341N61O52 |
| CAS Number | 154947-66-7 |
| Storage | -20°C long-term, protected from moisture |
References
Selected Literature
The following peer-reviewed references informed the research summaries on this page. Citations are provided for scientific context only.
- Dürr UHN, et al. (2006). LL-37, the only human member of the cathelicidin family of antimicrobial peptides. Biochimica et Biophysica Acta, 1758(9), 1408-1425.
- Nizet V, et al. (2001). Innate antimicrobial peptide protects the skin from invasive bacterial infection. Nature, 414(6862), 454-457.
- Zanetti M. (2004). Cathelicidins, multifunctional peptides of the innate immunity. Journal of Leukocyte Biology, 75(1), 39-48.
- Kahlenberg JM & Kaplan MJ. (2013). Little peptide, big effects: the role of LL-37 in inflammation and autoimmune disease. Journal of Immunology, 191(10), 4895-4901.
- Vandamme D, et al. (2012). A comprehensive summary of LL-37, the factotum human cathelicidin peptide. Cellular Immunology, 280(1), 22-35.
Research Disclaimer
This product is intended strictly for laboratory research purposes only. It is not a drug, food, cosmetic, or dietary supplement and is not intended to diagnose, treat, cure, or prevent any disease. It is not for human or animal consumption. All information presented is derived from published scientific literature and is provided for educational reference only. By purchasing, the buyer affirms they are a qualified researcher or institution and assume full responsibility for the safe and lawful handling of this material.