LL-37
Cathelicidin Antimicrobial Peptide
LL-37 is the active fragment of the human cathelicidin antimicrobial peptide, studied in research for antimicrobial and immunomodulatory activity.
This product is intended strictly for laboratory research use within the United States. It is not approved by the FDA 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 U.S. federal, state, and local regulations.
LL-37 is the active fragment of the human cathelicidin antimicrobial peptide, studied in research for antimicrobial and immunomodulatory activity.
Experimental models examine its membrane interactions and pleiotropic signaling under controlled laboratory conditions.
Third-party tested for purity, ID, quantity.
LL-37 is a 37-residue amphipathic peptide derived from the cathelicidin precursor hCAP18. Research has characterized its direct antimicrobial action alongside pleiotropic host-defense roles, including immunomodulation, angiogenesis, and wound-repair signaling.
Studies span antimicrobial, sepsis, and cardiovascular research models under structured conditions.
LL-37 was identified as the proteolytically released active fragment of human cathelicidin, the only cathelicidin expressed in humans.
Research has since characterized its broad antimicrobial spectrum and its expanding roles in innate immunity and tissue repair.
Research into LL-37 focuses on antimicrobial and host-defense signaling. Frameworks evaluate membrane-disruption mechanisms, immunomodulation, and tissue-repair endpoints under controlled in vitro and preclinical conditions.
2 of the 4 areas below are addressed directly by a paper cited on this page.
Antimicrobial membrane-interaction models
Addressed on this page by Fabisiak 2016, Nagaoka 2020. 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.
- Fabisiak, A. et al. (2016) — LL-37: Cathelicidin-related antimicrobial peptide with pleiotropic activity
- Nagaoka, I. et al. (2020) — Therapeutic Potential of Cathelicidin Peptide LL-37, an Antimicrobial Agent, in a Murine Sepsis Model
Innate-immunity and immunomodulation research
No paper cited on this page reports on innate, immunity or immunomodulation. This heading marks where LL-37 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.
Wound-repair signaling studies
No paper cited on this page reports on wound or repair. This heading marks where LL-37 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.
Cardiovascular and sepsis research frameworks
Addressed on this page by Nagaoka 2020. 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.
- Nagaoka, I. et al. (2020) — Therapeutic Potential of Cathelicidin Peptide LL-37, an Antimicrobial Agent, in a Murine Sepsis Model
The references section of this page cites 3 primary papers published between 2016 and 2024 — a thin 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.
Research compounds attract claims that outrun their evidence. Below are the ones most often encountered for LL-37, 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.
LL-37 is also referred to as cathelicidin.
LL-37 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, innate-immunity and immunomodulation research and wound-repair signaling studies.
The 3 papers cited on this page, published between 2016 and 2024 (1 in animal models) 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.
Every lot of LL-37 is independently assayed before it is released, and the certificate for the lot shipped is published rather than summarised. Where a certificate for a current lot is not yet posted, the lot has not yet been released against it.
Researchers who buy LL-37 in the United States through Eppix Labs receive a batch-labelled vial whose certificate is published against that lot code, so the material can be matched to its analysis rather than to a generic specification.
- Lyophilized storage
- −20 °C long-term; stable at room temperature in transit
- After reconstitution
- 2–8 °C
- Light
- Protect from UV and direct light
- Freeze-thaw
- Avoid repeated cycles
- Vehicle
- Bacteriostatic water in most published protocols
- Format
- Lyophilized powder
LL-37 is supplied as lyophilized powder. In the dry state the material is comparatively stable, which is why it ships at ambient temperature without a cold chain; once reconstituted it is a peptide in solution and the handling constraints tighten considerably. At 37 residues it is short enough to be produced by solid-phase synthesis, and the published sequence on this page is what an identity assay is checked against.
Repeated freeze-thaw cycling is the handling error most likely to degrade material of this class, because each cycle concentrates solutes at the ice boundary. Where a protocol calls for the same vial across multiple sessions, the published literature generally describes aliquoting after reconstitution rather than re-freezing the whole volume.
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 glass vial in the strength selected (5mg / Single Vial, 5mg / 5-Pack, 5mg / 10-Pack available), batch-labelled
- Batch documentation for the lot shipped, once its certificate is published
- Discreet outer packaging with no product names on the exterior
- FedEx, tracked, typically 1–3 business days domestically
- Bacteriostatic water or any other reconstitution vehicle
- Syringes, needles or filters
- Dosing, administration or protocol guidance of any kind
Reconstitution materials are sourced separately. The reconstitution calculator on this site works out concentrations for a given volume, but it is an arithmetic tool for laboratory record-keeping and not a protocol.
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. Independent third-party analysis verifies purity, identity, and net content per batch.
The unit contains only the research compound. Any laboratory materials required for reconstitution or experimental procedures must be sourced separately.
Duration depends entirely on research design, storage conditions, and laboratory protocol.
LL-37: Cathelicidin-related antimicrobial peptide with pleiotropic activity
PubMedTherapeutic Potential of Cathelicidin Peptide LL-37, an Antimicrobial Agent, in a Murine Sepsis Model
PubMedCathelicidin peptide LL-37: A multifunctional peptide involved in heart disease
PubMedRelated
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