LL-37

Recovery / Healing
Host Defense & Tissue Repair Peptide
Cathelicidin · Innate Immunity · Antimicrobial Signaling
10mg

$149.99

Availability: In stock

For research purposes only.
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Emma Lindsay

RESEARCH GUIDE

I’ve pulled together the key product details, research context, and supporting information so you can quickly decide whether this item lines up with your research goals.

Overview

LL-37 is a naturally occurring human peptide studied for its role in immune defense, inflammation, and tissue repair. In plain English, it is part of the body’s first line of defense and is researched for how it interacts with bacteria, viruses, fungi, immune cells, and damaged tissue. That has made LL-37 especially interesting in research involving wound healing, barrier protection, infection-related signaling, and the way the immune system responds to injury or microbial stress.

Scientifically, LL-37 is a cathelicidin-derived antimicrobial peptide involved in innate immune signaling and host-defense biology. Research has examined its effects on microbial membranes, immune-cell recruitment, inflammatory pathways, epithelial barrier function, angiogenesis, and wound-repair processes. Current evidence is strongest in preclinical and translational models, while human clinical evidence remains limited, so LL-37 is best positioned as an investigational research peptide rather than an established therapeutic agent.

The Science Behind LL-37
Explore how LL-37 is studied as a human cathelicidin involved in innate immunity, antimicrobial defense, inflammatory signaling, and tissue repair.

LL-37 is a 37-amino-acid peptide derived from the human cathelicidin precursor protein hCAP18 and is the best-characterized cathelicidin antimicrobial peptide in humans. It is produced by several immune and epithelial cell types and is found in tissues including the skin, respiratory tract, gastrointestinal tract, and other epithelial surfaces. LL-37 is part of the innate immune system, where it has been studied for direct antimicrobial activity as well as for broader host-defense signaling.

Its biological activity is more complex than simply disrupting microbial membranes. LL-37 has been reported to interact with bacterial membranes and endotoxins, influence chemotaxis of immune cells, modulate inflammatory responses, and participate in epithelial repair. Research also suggests roles in angiogenesis, cell migration, barrier integrity, and wound closure. Importantly, LL-37 can have both pro-inflammatory and anti-inflammatory effects depending on concentration, tissue environment, receptor activity, and disease context, which is one reason the peptide remains scientifically interesting but biologically complex.

Much of the mechanistic evidence comes from cell, tissue, and animal models rather than established therapeutic use in humans. Researchers continue to investigate how LL-37 activity changes across different concentrations and biological environments, including how it interacts with immune signaling pathways, epithelial cells, microbial membranes, and inflammatory mediators.

Is LL-37 Right for Your Research Goals?
Discover where LL-37 fits within host-defense, antimicrobial, inflammatory-signaling, and tissue-repair research.

LL-37 may be relevant to research focused on innate immunity, host-defense peptides, antimicrobial activity, epithelial biology, inflammatory signaling, wound healing, and tissue repair. It is particularly useful when the research question involves how the body coordinates direct antimicrobial activity with immune-cell recruitment and tissue-repair signaling.

Researchers have investigated LL-37 against a wide range of microbial targets and in models involving bacterial membranes, biofilms, viral interactions, fungal organisms, skin barrier function, wound closure, angiogenesis, and immune regulation. This makes LL-37 broader in scope than many peptides that are primarily associated with one receptor or one signaling pathway.

That breadth also means LL-37 should not be interpreted as universally anti-inflammatory or universally protective. Published research shows that its effects are highly context dependent. Concentration, tissue type, inflammatory environment, microbial exposure, and receptor interactions can all change the biological response. Some studies have also identified cytotoxicity at higher experimental concentrations, which remains relevant when designing or interpreting laboratory models.

Research Concentrations, Reconstitution & Storage
General research-context information on LL-37 handling, reconstitution, experimental concentrations, and peptide storage.

LL-37 research has used a wide range of experimental concentrations depending on the model, tissue type, microorganism, and endpoint being studied. Published laboratory work commonly reports concentrations in micromolar units rather than standardized human dosing. A 2025 review noted that biological and cytotoxic effects have been observed in human-cell models across low-micromolar concentration ranges, illustrating why concentration and experimental context are important when interpreting LL-37 research.

Because no standardized commercial or clinically established LL-37 dosing protocol exists, laboratory concentrations should not be converted into personal dosing recommendations. Researchers should instead base experimental design on the specific published model being replicated or investigated.

For laboratory preparation, lyophilized LL-37 may be reconstituted using an appropriate sterile research solvent according to the intended experimental protocol. Avoid vigorous shaking; gentle swirling is preferable to reduce unnecessary mechanical stress on the peptide. Once reconstituted, solutions should generally be kept refrigerated and protected from repeated temperature fluctuations and light. For longer-term experimental storage, aliquoting may help reduce repeated freeze-thaw cycles.

Use the SilverLeaf Reconstitution Calculator for concentration and volume calculations where appropriate. This information is provided for laboratory and research reference only.

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