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LL-37: Immune / Anti-Inflammatory research guide
In short: LL-37 human cathelicidin antimicrobial peptide (37 aa, +6 net charge) disrupts bacterial membranes via amphipathic alpha-helical channel formation and NF-κB modulation. It is studied in preclinical (cell and animal) research and is supplied strictly for laboratory use, not for human or clinical use.
Not medical advice. LL-37 is a research compound. This guide does not provide dosing, diagnosis, therapy recommendations, or claims about effects in humans.
LL-37 at a glance
What to know first
Details and limits sit in the sections below. Research use only.
What LL-37 is
LL-37 is the only human cathelicidin - a 37-residue amphipathic antimicrobial peptide that punches holes in bacterial membranes while simultaneously acting as an alarmin that orchestrates the innate immune response.
One-paragraph overview from our research datasheet. Still scientific, but faster to read than the full mechanism list below.
LL-37 human cathelicidin antimicrobial peptide (37 aa, +6 net charge) disrupts bacterial membranes via amphipathic alpha-helical channel formation and NF-κB modulation.
Research contexts
Peer-reviewed papers discuss LL-37 in specific lab settings. The points below reflect research questions, not health claims.
Research vs. personal use: Literature describes experiments in cells and animals. That is distinct from real-world use. Our products are for laboratory research only.
Typical study contexts
Why Immune / Anti-Inflammatory research matters
Immune-focused peptides are studied for innate responses, viral models or antimicrobial biology in controlled experiments.
Mechanisms (technical review)
Our datasheet lists mechanistic themes from preclinical work. These are research endpoints, not health claims.
Lab handling & preparation
Common Questions People Are Asking
What is LL-37 and how does it work?
LL-37 is the only human cathelicidin antimicrobial peptide - a 37-amino-acid, positively charged (net +6) amphipathic helix cleaved from the precursor hCAP-18. Its primary mechanism is physical: it binds the anionic surface of microbial membranes and disrupts them, while also neutralising bacterial endotoxin (LPS) and acting as an alarmin that signals the wider innate immune system. New-U supplies it for laboratory research only.
What does the LL-37 research actually show?
Preclinical and cell-based studies report broad-spectrum antimicrobial activity (Gram-positive and Gram-negative bacteria, fungi, enveloped viruses), inhibition of biofilm formation, and roles in wound healing and immune signalling; its dysregulation is also studied in inflammatory skin disease such as rosacea, psoriasis and atopic dermatitis (Reinholz & Ruzicka et al., 2012). These are research findings in models, not a promise of any effect in humans.
Is LL-37 legal, and is it approved for use?
LL-37 is not an FDA-approved drug; it is sold strictly as a research compound for laboratory use, not for human consumption. It has appeared in early-phase clinical research (for example topical wound-healing studies), but it remains investigational. Legal status varies by jurisdiction, so confirm your local rules before purchasing.
Can bacteria develop resistance to LL-37?
Resistance is much harder to evolve against membrane-targeting peptides than against receptor- or enzyme-targeting antibiotics, because there is no single protein for the pathogen to mutate. Some bacteria modify their outer-membrane charge to reduce electrostatic attraction, but full escape is rare - part of why antimicrobial peptides like LL-37 are such an active research area in the antibiotic-resistance era.
What is the vitamin D connection?
Cathelicidin (CAMP) gene expression is directly regulated by the vitamin D receptor. Calcitriol (the active form of vitamin D) upregulates endogenous LL-37 production, which is one of the mechanisms behind the observed relationship between vitamin D status and susceptibility to respiratory and tuberculosis infections.
Why is LL-37 dose-dependent for cytotoxicity?
Like most amphipathic antimicrobial peptides, LL-37 is selectively toxic to microbial membranes at low concentrations but loses selectivity at high concentrations, affecting host-cell membranes as well. Research protocols need to balance antimicrobial efficacy against host-cell tolerability, which is a general limitation of the class.
How should LL-37 be stored?
Keep the lyophilised powder frozen at −20 °C. After reconstitution with bacteriostatic water, refrigerate at 1-6 °C and protect from light. LL-37 is susceptible to proteolytic degradation, so use reconstituted material promptly and avoid repeated freeze-thaw cycles.
Is this page medical advice? Can I use LL-37 for my health?
No, and no. This article is educational only. We do not provide dosing, medical recommendations, or health claims. Our products are sold strictly for laboratory research, not for personal use of any kind.
Where do I find LL-37 specs, purity certificates and pricing?
Open the shop listing via “View product details.” There you will see batch specs, the Certificate of Analysis (COA), concentration, purity grade, and available SKUs with current pricing.
Related peptide guides
Other compounds researchers often read about alongside LL-37.
Scientific sources & further reading
Primary literature and registries for LL-37, plus mainstream coverage of the peptide category. Research use only - not medical advice.
Databases & literature:
Peptides in the news:
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Also known as: LL-37, Cathelicidin, hCAP-18 Active Fragment, Human Cathelicidin Antimicrobial Peptide, CAMP, Cathelicidin LL-37, Antimicrobial Peptide LL-37
PRECISION. PURITY. PERFORMANCE.
Research peptides at >99% HPLC-verified purity, third-party tested by Janoshik Analytical & Freedom Diagnostics, with Certificates of Analysis published per released batch. Supplied strictly for laboratory research use.
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Research use only (RUO). All products are sold strictly for laboratory and research purposes — not for human or veterinary consumption. Purchasers must be 21 or older.
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