LL-37 is the 37-residue C-terminal peptide released from the human cathelicidin precursor protein hCAP18. It is the only cathelicidin-derived peptide identified in humans, and it is supplied here as a research compound for controlled laboratory work.
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Research Use Only
This product is intended strictly for laboratory research use within Canada. It is not approved by Health Canada for the diagnosis, treatment, cure, or prevention of any disease. Not for human or veterinary use.
By purchasing, you confirm the material will be used solely for lawful research purposes in accordance with applicable Canadian regulations.
LL-37 is the 37-residue C-terminal peptide released from the human cathelicidin precursor protein hCAP18. It is the only cathelicidin-derived peptide identified in humans, and it is supplied here as a research compound for controlled laboratory work.
In scientific literature, LL-37 is examined for its amphipathic helical structure, its interaction with microbial membranes, and its participation in host defense and immune signaling processes studied under in vitro and preclinical conditions.
LL-37 adopts an amphipathic alpha-helical conformation that has been characterised in studies of its association with anionic membrane surfaces and lipopolysaccharide. Research has described membrane permeabilisation as one mode of antimicrobial activity, alongside reported interference with biofilm formation and with established biofilm structures in bacterial culture models. Processing of the hCAP18 precursor and the regulatory role of vitamin D signaling in its production have also been investigated.
Beyond direct antimicrobial endpoints, experimental work has evaluated LL-37 in immunomodulatory contexts: chemotactic signaling, receptor-mediated effects on immune cell populations, and involvement in neutrophil extracellular trap formation and nucleic acid complex recognition. Additional research frameworks have examined LL-37 in oral and periodontal tissue models, bone and osteoblast cell models, cardiovascular and myocardial injury models, autoimmune pathophysiology including systemic lupus erythematosus, tumour immunity, and antiviral screening including HIV. Published findings in several of these areas are mixed, with both pro-inflammatory and resolving activity and, in some cell models, cytotoxicity reported depending on concentration and system.
History
LL-37 was identified as the active peptide liberated from human cathelicidin antimicrobial protein hCAP18, the single cathelicidin family member described in humans. Early characterisation focused on its structure and on its capacity to disrupt microbial membranes, which established it as a reference molecule in antimicrobial peptide research.
Subsequent literature broadened the record considerably. Reviews have tracked its expression in oral tissues and periodontium, its regulation by vitamin D, its role in NETosis and in autoimmune disease models, its examination in cardiac and myocardial infarction research, and its evaluation against biofilms and viral targets. The compound is well represented by review literature, and much of the primary evidence remains in vitro or preclinical.
Key Research Areas
Laboratory investigations into LL-37 span antimicrobial mechanism studies, including membrane interaction and antibiofilm models, and immunological frameworks examining chemotaxis, neutrophil extracellular trap formation, and nucleic acid complex signaling. Further research models have evaluated the peptide in oral and periodontal tissue, bone and osteoblast systems, cardiovascular and myocardial injury contexts, autoimmune pathophysiology, and antiviral and tumour immunity screening under controlled experimental conditions.
4 of the 5 areas below are addressed directly by a paper cited on this page.
Antimicrobial membrane interaction models
Addressed on this page by Neshani 2025, Svensson 2025. Each is linked to its source record in the references below, so what was measured — and in what system — can be read rather than taken on trust.
Neshani, A. et al. (2025) — Decoding LL-37: Structure and antimicrobial mechanisms against microbial threats
Svensson, D. et al. (2025) — Human antimicrobial/host defense peptide LL-37 may prevent the spread of a local infection through multiple mechanisms: an update
Bacterial biofilm research
Addressed on this page by Memariani 2023. Each is linked to its source record in the references below, so what was measured — and in what system — can be read rather than taken on trust.
Addressed on this page by Radic 2022. Each is linked to its source record in the references below, so what was measured — and in what system — can be read rather than taken on trust.
Addressed on this page by Tokajuk 2022. Each is linked to its source record in the references below, so what was measured — and in what system — can be read rather than taken on trust.
Cardiovascular and autoimmune pathophysiology research
No paper cited on this page reports on cardiovascular, autoimmune or pathophysiology. This heading marks where LL-37 Spray is discussed in the category rather than a question the cited literature answers, and it is worth knowing which of these areas has work behind it and which does not.
The references section of this page cites 6 primary papers published between 2022 and 2025 — a limited but non-trivial record. Every citation is linked to its PubMed or DOI record so it can be read rather than taken on trust, and the summaries above describe what those papers report rather than what the compound is claimed to do.
LL-37 Spray is frequently listed as a peptide by suppliers in this market. It is not one. The structure published on this page is the compound's actual chemistry, and research on it should be read against its own class rather than against peptide literature.
Research compounds attract claims that outrun their evidence. Below are the ones most often encountered for LL-37 Spray, set against what the papers cited on this page actually report. Where the record is thin or contested, that is stated rather than smoothed over.
Preclinical only
LL-37 Spray is commonly described online in connection with faster healing from injury and improved recovery. In the research literature the same compound is filed under antimicrobial membrane interaction models, bacterial biofilm research and innate immune and NETosis signaling studies.
The 6 papers cited on this page, published between 2022 and 2025 (1 review) describe laboratory and animal work. None reports a controlled trial in humans. Findings in cell culture or in a rodent model describe what happened in that system; they do not establish that the same occurs in humans, and this compound is not approved for human use.
Nothing above is a statement of what this material does. It is a summary of what has been published and what has not. Eppix Labs supplies research materials only and provides no dosing, administration or protocol guidance.
Verification for LL-37 Spray is per lot, not per product. The current 5mg lot LL37-CA-26H-05 returned 99.64% purity, 5.6 mg measured, 112% of the labelled 5 mg, assayed by Janoshik. Those figures are the laboratory's, published in full rather than reduced to a badge.
The lot code printed on the vial matches the code on the certificate for LL-37 Spray. Matching the two is what confirms the unit in hand came from the batch that was tested — a certificate not tied to a lot code proves nothing about any particular unit.
Researchers who buy LL-37 Spray in Canada through Eppix Labs receive the lot described by the certificate above: the code printed on the vial label is the code on the certificate, and both are searchable on the batch verification page.
LL-37 Spray ships as a prepared solution rather than as lyophilized powder, so it is already past the point at which a powder would be reconstituted. That shortens handling but tightens storage: a compound in solution is less stable than the same compound dry, and refrigeration from arrival onward is the relevant control.
The stability window for a solution is shorter than the shelf life of a sealed lyophilized vial of the same compound. Records for laboratory work in this format should note the date the unit was opened, not only the date it was received.
Vials may appear empty on arrival. Lyophilized material collects at the base of the vial and is often not visible until the vial is inspected under direct light.
1 × sealed spray unit (1mL - 500 mcg per spray / Single Vial), batch-labelled
The batch-linked Certificate of Analysis for the exact lot shipped
Discreet outer packaging with no product names on the exterior
Canada Post Xpresspost, tracked, typically 1–2 business days from Canadian stock
Not included
Laboratory consumables of any kind
Dosing, administration or protocol guidance of any kind
No. Eppix Labs products are supplied exclusively for laboratory research. We do not provide dosing, administration, or usage guidance.
Each unit contains the labeled quantity of LL-37 peptide. Independent third-party analysis verifies purity, identity, and net content per batch.
The unit contains only the compound as supplied. Any laboratory materials required for handling, dilution, or experimental procedures must be sourced separately.
Duration depends entirely on research design, storage conditions, and laboratory protocol.
Neshani, A. et al.(2025)
Decoding LL-37: Structure and antimicrobial mechanisms against microbial threats
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Have questions about batch verification, documentation, or research specifications? Our team is available to assist with product and compliance inquiries.