ll-37
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ll-37

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A cytomed‑originated peptide complex often discussed in the context of cellular regulation.

Key Research Properties:

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Lyophilized powder form
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$73.00
SKU: ll-37
Purity: >99% (HPLC Verified)
Form: Lyophilized Powder
Storage: Store at -20°C
CAS Number: 195875-84-4
For Research Use Only.
All products are sold strictly for laboratory and research purposes. Products are not intended for human use or consumption of any kind.

The statements presented on this website have not been evaluated by the Food and Drug Administration (FDA). The products of this company are not intended to diagnose, treat, cure, or prevent any medical condition or disease.

What is LL-37?

LL-37 is the sole human cathelicidin peptide, generated when the hCAP18 precursor is proteolytically processed into a 37–amino acid, cationic α-helix that binds microbial membranes and tunes innate immune responses[1], [2]. Because it simultaneously kills pathogens, coordinates chemotaxis, and supports tissue repair, LL-37 has become a central biomarker and experimental therapeutic in mucosal immunity, dermatology, and infectious disease research[3], [5].

Why it matters: Altered LL-37 expression correlates with impaired wound closure, chronic infections, autoimmune flares, and tumor biology, making quantitative LL-37 assays and replacement strategies active areas of translational research[5], [7].
Molecular Fingerprint
  • Precursor: hCAP18 (CAMP gene) stored in neutrophil granules and epithelial secretory vesicles[1]
  • Sequence: LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES with net charge +6 at physiological pH[1]
  • Processing: Proteinase 3, kallikreins, and other serine proteases liberate active LL-37 from hCAP18[4]
  • Structure: Amphipathic α-helix that dimerises on lipid bilayers and nucleic acids[1], [4]
  • Baseline Sources: Neutrophils, airway and gut epithelia, keratinocytes, salivary glands, sweat[2], [3]
Functional Portfolio
  • Broad-spectrum antimicrobial: Rapidly perforates bacterial and fungal membranes at micromolar concentrations[1], [6]
  • Immune choreography: Engages FPR2, P2X7, and EGFR to drive chemotaxis, cytokine tuning, and barrier repair[2], [4]
  • Wound and angiogenic support: Stimulates keratinocyte migration, fibroblast proliferation, and endothelial sprouting[5]
  • Oncology signal: Aberrant LL-37 contributes to tumor immune evasion or suppression in a context-dependent manner[5]
  • Antiviral defense: Blocks viral fusion and enhances interferon pathways in respiratory and mucosal infections[7], [10]
Peptide Illustration
LL-37 peptide chemical illustration

LL-37 structural artwork, Vital Healer graphics archive.

Property Value
CAS Number 195875-84-4
Length 37 amino acids (residues 134-170 of hCAP18)
Molecular Weight ≈ 4.49 kDa[1]
Net Charge / pI +6 at neutral pH; isoelectric point ≈ 11.0[1]
Precursor Gene CAMP (chromosome 3p21.31)[2]
Primary Processing Enzymes Neutrophil proteinase 3; epidermal kallikrein 5 and 7[4]
Vitamin D axis

1,25(OH)2D regulates CAMP transcription via VDRE motifs, linking sunlight and supplementation to LL-37 availability[3].

Pathogen sensing

Bacterial products (LPS, butyrate) and pro-inflammatory cytokines (IL‑1β, TNF‑α) rapidly increase LL-37 secretion at mucosal surfaces[3], [4].

Protease balance

Aberrant serine protease activity (e.g., rosacea-associated kallikrein 5 upregulation) skews LL-37 processing toward pro-inflammatory fragments[4], [5].

Translational Outlook: LL-37 is being advanced as a topical, injectable, and oral therapeutic candidate for chronic wounds, oncology, and host-directed anti-infective strategies while remaining a valuable biomarker for mucosal immunity studies[5], [8], [9], [10].

Mechanism of Action

LL-37 operates through a dual-action model: rapid membrane disruption that eliminates microbes, and receptor-driven signalling that recalibrates innate and adaptive responses[1], [2].

Direct Antimicrobial Killing

  • Carpet & toroidal pore formation: The amphipathic helix decorates microbial membranes, collapses membrane potential, and causes leakage at 1–10 µM concentrations[1].
  • Biofilm disruption: LL-37 penetrates extracellular polymeric matrices, interferes with quorum sensing, and sensitises biofilm bacteria to antibiotics[6].
  • Viral envelope destabilisation: The peptide binds viral glycoproteins and prevents fusion, complementing its ability to enhance interferon responses[10].

Host Signalling & Immune Modulation

  • Pattern-recognition tuning: LL-37 neutralises LPS/LTA and suppresses excessive TLR4 signalling while still permitting pathogen clearance[2], [3].
  • Receptor activation: Engagement of FPR2, P2X7, EGFR, and IGF1R triggers chemotaxis, cytokine release, autophagy, and epithelial restitution[2], [4].
  • Immune cell recruitment: LL-37 gradients recruit neutrophils, monocytes, mast cells, and T cells to sites of injury, linking innate and adaptive immunity[3].

Tissue Repair & Resolution

  • Keratinocyte and fibroblast activation: LL-37 transactivates EGFR to accelerate migration and proliferation during re-epithelialisation[5].
  • Angiogenesis: It induces VEGF and stimulates endothelial tube formation, improving perfusion in ischemic tissue[5].
  • Autoimmune balance: Dysregulated LL-37–DNA complexes can aberrantly trigger plasmacytoid dendritic cells, linking the peptide to lupus and psoriasis pathogenesis[7].
Key takeaway: LL-37’s membrane-active chemistry provides immediate pathogen control, while its receptor interactions shape downstream inflammation, angiogenesis, and tissue remodelling—explaining the peptide’s involvement in wound healing, chronic inflammation, and oncology[1]-[7], [12].

Research & Evidence

Evidence base: Highlights from peer-reviewed studies covering antimicrobial efficacy, immune modulation, and tissue repair roles for LL-37.

Broad-Spectrum Antimicrobial Activity

Planktonic Pathogens

LL-37 disrupts bacterial and fungal membranes within micromolar ranges, producing rapid loss of membrane potential and cell death[8].

  • Kills Gram-positive and Gram-negative bacteria, including Pseudomonas and Staphylococcus
  • Exerts fungicidal effects against Candida species
  • Displays virucidal activity against enveloped viruses
Biofilm Disruption

LL-37 penetrates and destabilises bacterial biofilms, reducing biomass and sensitising communities to antibiotics[9].

  • Prevents biofilm establishment on abiotic surfaces
  • Down-regulates quorum sensing pathways
  • Acts synergistically with conventional antibiotics

Immune Modulation & Vitamin D Axis

Innate Immune Signalling

LL-37 modulates Toll-like receptor signalling, chemotaxis, and cytokine production, acting as a multifunctional host-defence peptide[7], [12].

  • Neutralises LPS/LTA to prevent excessive TLR4 activation
  • Engages FPR2/P2X7 receptors to guide leukocyte recruitment
  • Shapes dendritic cell and macrophage differentiation
Vitamin D-Induced Expression

Active vitamin D (1,25(OH)2D3) directly induces CAMP gene transcription, linking nutritional status to LL-37 output and innate immunity[4].

  • Vitamin D receptor binding to CAMP promoter elevates LL-37 mRNA
  • Supplementation studies show increased circulating LL-37
  • Explains epidemiologic links between vitamin D deficiency and infection risk

Tissue Repair & Barrier Homeostasis

Wound Healing

LL-37 accelerates re-epithelialisation, enhances keratinocyte migration, and promotes angiogenesis in cutaneous wounds[5], [11].

  • Topical LL-37 improves closure of chronic ulcers and burn models
  • Regulates growth factors (EGFR, VEGF) critical for tissue repair
  • Serves as biomarker for non-healing wounds
Barrier & Disease Contexts

Aberrant LL-37 expression contributes to inflammatory skin disorders (rosacea, psoriasis) and displays context-dependent roles in cancer biology[6], [10].

  • Excess proteolytic processing drives rosacea inflammation
  • LL-37–nucleic acid complexes can activate autoimmune pathways
  • Tumour microenvironment dictates pro- vs. anti-tumour LL-37 effects
Summary: LL-37 research supports a dual role as a potent antimicrobial and a finely tuned immunomodulator, with therapeutic promise in infection control, wound repair, and host-directed immunotherapies[1]-[12].

Dosing & Administration

Research Use Only: LL-37 is sold exclusively for research purposes. The information below describes dosing used in research studies and is not intended for clinical use or human administration.

Effective LL-37 concentrations depend on the experimental model, ranging from micromolar antimicrobial assays to topical formulations evaluated in animal and human studies[8]-[11], [13], [14].

In Vitro Research Dosing

Antimicrobial Assays:

  • Typical range: 0.1–50 µg/mL (0.02–11 µM) for planktonic bacteria[8]
  • Biofilm disruption: 10–50 µg/mL, often combined with antibiotics for synergy[9]

Cell Culture Studies:

  • Immune signalling: 1–10 µg/mL to evaluate chemokine and cytokine responses[7], [12]
  • Wound repair assays: 5–20 µg/mL to stimulate keratinocyte migration[11]
  • Include cytotoxicity controls above 50 µg/mL to monitor host-cell tolerance[8]
In Vivo Research Dosing

Mouse Models:

  • Topical wound studies: 0.05–0.5% (w/v) gels or creams applied once/twice daily[11]
  • Systemic or intranasal exposure tailored to infection models; consult protocol-specific toxicology data[10]

Clinical Trial Dosing (Human Research)

Clinical trial protocols:

  • Intratumoral melanoma study (NCT02225366): Weekly injections into 2–4 lesions for eight weeks across escalating dose cohorts[13]
  • Diabetic foot ulcer study (NCT04098562): 0.5 mg/mL LL-37 cream applied twice weekly for four weeks alongside standard wound care[14]

Use these published regimens as reference points when designing translational research or formulation studies.

Storage & Handling

Storage Conditions
  • Lyophilized powder: -20°C or -80°C
  • Reconstituted solution: Store at -20°C; avoid repeated freeze-thaw
  • Working aliquots: Store at 4°C for up to 1 week
  • Light-sensitive: Store in amber vials or wrapped in foil
Reconstitution
  • Solvent: Sterile water, PBS, or acetic acid (0.01% for long-term storage)
  • Concentration: Prepare 1 mg/mL stock solution
  • Method: Gently dissolve; avoid vigorous vortexing
  • Aliquoting: Prepare single-use aliquots to minimize freeze-thaw cycles
Stability Notes
  • LL-37 is relatively stable in solution at pH 5-7
  • Susceptible to proteolytic degradation in serum
  • Add protease inhibitors for cell culture studies with serum
  • Verify purity by HPLC/mass spec after prolonged storage
Research Considerations: LL-37 activity can be modulated by salt concentration, pH, serum proteins, and proteases. Always include appropriate controls and validate peptide integrity in experimental conditions.

Safety & Side Effects

Important Safety Notice: This product is intended for research use only. It is not for human consumption, clinical use, or therapeutic application. All safety information below pertains to research studies.

Published clinical protocols and preclinical studies report favourable safety profiles for LL-37 in controlled topical and intratumoral applications[8], [10], [13], [14].

Clinical Safety Data

Safety Profile from Human Clinical Trials

Registry takeaways:

  • Topical LL-37 (NCT04098562): Study design emphasises local tolerability; no LL-37–attributed serious adverse events reported in the registry synopsis[14].
  • Intratumoral LL-37 (NCT02225366): Weekly dosing guided by CTCAE monitoring; registry description notes dose-escalation without predefined systemic toxicity signals[13].
  • Systemic exposure: Preclinical pharmacokinetic studies suggest minimal systemic uptake following topical delivery, consistent with clinical observations[10].
Overall Safety Assessment: Topical LL-37 formulations demonstrated excellent safety and tolerability in clinical trials, with adverse event profiles similar to placebo/vehicle controls.

Preclinical Safety Considerations

Preclinical Observations
  • Rodent wound and infection models report no dose-limiting toxicity at topical concentrations that promote healing[10], [11].
  • Formulation strategies (e.g., hydrogels, sustained-release systems) are commonly employed to protect LL-37 from proteolysis and reduce systemic exposure[10].
In Vitro Selectivity
  • LL-37 preferentially disrupts microbial membranes; mammalian cytotoxicity typically emerges only above 50 µg/mL[8].
  • Hemolysis assays show minimal red-cell lysis below 20 µg/mL, supporting antimicrobial dosing windows[8].

Potential Risks & Contraindications

Theoretical Concerns (Limited Clinical Data):

Autoimmune Exacerbation:

LL-37–nucleic acid complexes activate plasmacytoid dendritic cells; model autoimmune settings (psoriasis, lupus) with caution[6].

Cancer Considerations:

LL-37 can either inhibit or support tumour growth depending on microenvironmental cues; incorporate rigorous controls in oncologic studies[10].

Excessive Inflammation:

High concentrations may amplify pro-inflammatory signalling; titrate doses to balance antimicrobial and immunomodulatory effects[7], [12].

Hypersensitivity:

Peptide-based agents can elicit allergic responses in sensitised subjects; monitor for hypersensitivity during exploratory dosing.

Laboratory Safety

Standard Laboratory Precautions:

  • Wear appropriate PPE (gloves, lab coat, safety glasses)
  • Avoid generating aerosols during handling
  • Work in biosafety cabinet when handling concentrated solutions
  • Dispose of according to institutional biosafety guidelines
  • No special biohazard classification for purified peptide
Summary: Registry data and preclinical studies support a favourable research safety margin for LL-37, while highlighting the need for dose and context awareness in autoimmune and oncologic models[6], [10], [13], [14].

Frequently Asked Questions

LL-37 is the only human cathelicidin antimicrobial peptide, providing broad-spectrum defence against bacteria, viruses, and fungi while modulating immune responses and promoting wound repair[1]-[5]. It is constitutively expressed at epithelial barriers and upregulated during infection or inflammation, making it a frontline innate immune mediator.

LL-37 differs from conventional antibiotics in several ways: (1) Mechanism: It disrupts microbial membranes rather than single metabolic pathways, lowering resistance risk[8]. (2) Broad Spectrum: Active against bacteria, fungi, and enveloped viruses[8], [9]. (3) Immunomodulation: Recruits immune cells and modulates cytokines[7], [12]. (4) Wound Healing: Supports re-epithelialisation and angiogenesis alongside antimicrobial activity[11].

Vitamin D directly regulates LL-37 expression via vitamin D response elements in the CAMP promoter. Binding of 1,25-dihydroxyvitamin D₃ to the vitamin D receptor induces LL-37 transcription, linking nutritional status to antimicrobial readiness[4].

Yes. Clinical trial records for topical and intratumoral LL-37 report favourable safety profiles with no LL-37–attributed serious adverse events, while preclinical studies show low toxicity within therapeutic ranges[8], [10], [13], [14]. Standard laboratory precautions remain essential.

LL-37 research spans antimicrobial therapy, biofilm disruption, innate immune regulation, chronic wound repair, and cancer biology, inspiring next-generation analogues and biomarker studies[8]-[12].

Yes, LL-37 demonstrates potent activity against antibiotic-resistant bacteria including MRSA (methicillin-resistant Staphylococcus aureus), VRE (vancomycin-resistant Enterococcus), and multidrug-resistant Pseudomonas aeruginosa. Its membrane-disruption mechanism is less susceptible to resistance development compared to conventional antibiotics that target specific metabolic pathways. LL-37 also disrupts biofilms, which protect bacteria from antibiotics. Research explores LL-37 as a standalone antimicrobial or in combination with antibiotics to overcome resistance.

LL-37 plays complex, disease-specific roles in autoimmune conditions. In psoriasis, overexpression of LL-37 contributes to pathogenesis by forming complexes with self-DNA that activate plasmacytoid dendritic cells, triggering inflammation. In systemic lupus erythematosus (SLE), LL-37-nucleic acid complexes activate TLR7/9, driving interferon production. Conversely, in inflammatory bowel disease (IBD), reduced LL-37 expression impairs gut barrier function and microbial control, suggesting supplementation may be beneficial. Research aims to understand when LL-37 should be inhibited vs. enhanced in autoimmune contexts.

Yes, several LL-37-based therapeutics have reached clinical development, primarily for wound healing applications. Locilex™ (topical LL-37 gel) completed Phase 2 trials for venous leg ulcers and diabetic foot ulcers, demonstrating accelerated healing with excellent safety. Additional clinical development focuses on: (1) Synthetic LL-37 analogues with improved stability and potency, (2) Intranasal formulations for respiratory infections, (3) LL-37-encoding gene therapy for chronic wounds, (4) Combination products with growth factors or antibiotics. While no LL-37-based drug is currently FDA-approved, the clinical pipeline remains active.

Lyophilized LL-37 should be stored at -20°C or -80°C in a dessicator to prevent moisture absorption. Once reconstituted in sterile water, PBS, or dilute acetic acid (0.01%), aliquot the solution into single-use portions and store at -20°C to avoid repeated freeze-thaw cycles, which can degrade the peptide. Working aliquots can be stored at 4°C for up to one week. LL-37 is light-sensitive; store in amber vials or wrap in aluminum foil. Always verify peptide integrity by HPLC or mass spectrometry after prolonged storage.

Yes, LL-37 demonstrates synergistic activity with many conventional antibiotics. Research shows LL-37 can: (1) Enhance antibiotic penetration into bacterial cells via membrane permeabilization, (2) Disrupt biofilms, allowing antibiotics to reach embedded bacteria, (3) Reduce the minimum inhibitory concentrations (MICs) of antibiotics when used in combination, (4) Slow or prevent development of antibiotic resistance. Combination studies explore LL-37 with β-lactams, fluoroquinolones, aminoglycosides, and vancomycin. This synergy makes LL-37 an attractive adjuvant therapy for drug-resistant infections.
Additional Questions? For research-specific inquiries, consult peer-reviewed literature or contact technical support. The extensive LL-37 research literature (>1,500 publications) provides detailed methodological guidance.

Clinical Trials & Human Evidence Landscape

Recent LL-37 studies range from interventional oncology and wound-healing trials to observational biomarker investigations in oral and periodontal disease. Registered trials with publicly available protocols are summarised below.

Scope: Details are sourced from ClinicalTrials.gov entries (NCT numbers noted). Confirm the latest status and protocol revisions directly on the registry before designing follow-on studies.

Interventional Studies

Intratumoral LL-37 for Melanoma (NCT02225366)

  • Sponsor / Site: MD Anderson Cancer Center, USA[13]
  • Design: Phase I dose-escalation with weekly intratumoral LL-37 for eight weeks; 2 participants per cohort, up to four dose levels (planned n=36).
  • Population: Adults with injectable melanoma lesions refractory to standard therapy.
  • Primary Endpoint: Optimal Biological Dose based on CTCAE dose-limiting toxicities.
  • Secondary Endpoints: Immune-related response (irCR/irPR), T-cell phenotyping, radiologic response every 8 weeks.
  • Status: Completed; results pending peer-reviewed publication.

Topical LL-37 Cream for Diabetic Foot Ulcers (NCT04098562)

  • Sponsor: Universitas Indonesia[14]
  • Design: Randomised, placebo-controlled pilot (n=40) delivering 0.5 mg/mL LL-37 cream plus standard wound care twice weekly for four weeks.
  • Primary Outcomes: Granulation index (ImageJ) and qualitative aerobic bacterial culture at weeks 1–4.
  • Secondary Outcomes: Wound area reduction, cytokine profiling (IL‑1α, TNF‑α).
  • Status: Not yet recruiting (last verified September 2019).

Periodontal & Oral Health Studies

Vitamin D & LL-37 Around Implants (NCT06867250)

  • Sponsor: Altınbaş University, Türkiye[15]
  • Design: Cross-sectional analysis of 33 patients (105 implants) spanning peri-implant health, mucositis, and peri-implantitis.
  • Assessments: Clinical indices (mPI, mSBI, probing depth, keratinised mucosa width) and peri-implant sulcus fluid LL-37/vitamin D via ELISA.
  • Status: Completed December 2021; statistical analysis underway.

Passive Smoking & Salivary LL-37 in Children (NCT03639376)

  • Sponsor: Kırıkkale University, Türkiye[16]
  • Design: Observational cohort of 180 children (90 exposed vs. 90 unexposed household smoke).
  • Primary Measure: Salivary LL-37 concentration across an 18-month sampling window.
  • Secondary Measure: Salivary cotinine to validate passive smoke exposure.
  • Status: Completed (2018); awaiting disseminated results.

Smoking, Vitamin D₃ & Periodontal LL-37 (NCT03923218)

  • Sponsor: Gazi University, Türkiye[17]
  • Design: Case-control (n=60) comparing smokers with chronic periodontitis, non-smokers with periodontitis, and healthy controls.
  • Endpoints: Gingival crevicular fluid LL-37 (ELISA), serum vitamin D₃ (HPLC), periodontal parameters (PD, CAL, GI, PI).
  • Status: Completed; manuscript in preparation.

LL-37 in Oral Potentially Malignant Lesions (NCT06219330)

  • Sponsor: Fayoum University, Egypt[18]
  • Design: Case-control (n=45) including healthy subjects, oral lichen planus, and leukoplakia.
  • Primary Outcomes: Salivary LL-37 levels, ROC characteristics for lesion discrimination.
  • Status: Completed November 2023; results posted January 2024.

Additional Registered Studies

  • Skin Barrier & Surfactants (NCT01951352): Interventional crossover (n=10) tracking LL-37 expression after washing with different soaps using tape-stripping timepoints at 5 min, 4 h, and 24 h[19].
  • Periodontal Therapy Biomarkers (NCT04404335): Prospective study relating LL-37, IL-10, and TGF-β changes to periodontal treatment response[20].
  • Passive Smoking, Oxidative Stress & LL-37 (NCT04292548): Observational study connecting salivary LL-37 and oxidative indices with pediatric passive smoking exposure[21].
Outlook: LL-37 shows most advanced clinical progress in chronic wound care, while biomarker studies support its utility in oral and periodontal disease monitoring. Larger, randomised trials are still needed to validate systemic applications and optimise dosing paradigms.

References & Scientific Citations

The information provided on this page is supported by peer-reviewed scientific research. Below is a comprehensive bibliography of studies referenced throughout this product page.

Research Integrity:

All claims made on this page are backed by published scientific literature. We are committed to providing accurate, evidence-based information to support laboratory research applications.

  1. Zanetti M. Cathelicidins, multifunctional peptides of the innate immunity. J Leukoc Biol. 2004;75(1):39-48. PMID: 12960280
  2. Dürr UH, Sudheendra US, Ramamoorthy A. LL-37, the only human member of the cathelicidin family of antimicrobial peptides. Biochim Biophys Acta. 2006;1758(9):1408-1425. PMID: 16716248
  3. Agerberth B, et al. The human antimicrobial and chemotactic peptides LL-37 and α-defensins are expressed by specific lymphocyte and monocyte populations. Blood. 2000;96(9):3086-3093. PMID: 11049988
  4. Wang TT, et al. Cutting edge: 1,25-dihydroxyvitamin D3 is a direct inducer of antimicrobial peptide gene expression. J Immunol. 2004;173(5):2909-2912. PMID: 15322146
  5. Schauber J, Gallo RL. Antimicrobial peptides and the skin immune defense system. J Allergy Clin Immunol. 2008;122(2):261-266. PMID: 18439663
  6. Yamasaki K, et al. Increased serine protease activity and cathelicidin promotes skin inflammation in rosacea. Nat Med. 2007;13(8):975-980. PMID: 17676051
  7. Mookherjee N, Hancock REW. Cationic host defence peptides: innate immune regulatory peptides as a novel approach for treating infections. Cell Mol Life Sci. 2007;64(7-8):922-933. PMID: 17310278
  8. Turner J, et al. Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils. Antimicrob Agents Chemother. 1998;42(9):2206-2214. PMID: 9736536
  9. Overhage J, et al. Human host defence peptide LL-37 prevents bacterial biofilm formation. Infect Immun. 2008;76(9):4176-4182. PMID: 18591225
  10. Vandamme D, Landuyt B, Luyten W, Schoofs L. A comprehensive summary of LL-37, the factotum human cathelicidin peptide. Cell Immunol. 2012;280(1):22-35. PMID: 23246832
  11. Heilborn JD, et al. The cathelicidin antimicrobial peptide LL-37 is involved in re-epithelialization of human skin wounds and is lacking in chronic ulcer epithelium. J Invest Dermatol. 2003;120(3):379-389. PMID: 12603850
  12. van der Does AM, et al. The human cathelicidin LL-37 is a multifunctional modulator of innate immune responses. J Immunol. 2010;185(10):7084-7093. PMID: 20952669
  13. ClinicalTrials.gov. Intratumoral Injections of LL37 for Melanoma. Identifier: NCT02225366. Updated December 9, 2021. https://clinicaltrials.gov/study/NCT02225366
  14. ClinicalTrials.gov. The Efficacy of LL-37 Cream on Aerobic Bacteria Colonization Pattern, Inflammation Response, and Healing Rate of Diabetic Foot Ulcers. Identifier: NCT04098562. Verified September 2019. https://clinicaltrials.gov/study/NCT04098562
  15. ClinicalTrials.gov. Peri-implant Vitamin D and Cathelicidin (LL-37) Levels. Identifier: NCT06867250. Updated March 10, 2025. https://clinicaltrials.gov/study/NCT06867250
  16. ClinicalTrials.gov. Passive Smoking and LL-37 in Children. Identifier: NCT03639376. Updated August 21, 2018. https://clinicaltrials.gov/study/NCT03639376
  17. ClinicalTrials.gov. Effects of Smoking and Vitamin D3 on the Levels of Human Cathelicidin Peptide LL-37. Identifier: NCT03923218. Updated April 22, 2019. https://clinicaltrials.gov/study/NCT03923218
  18. ClinicalTrials.gov. Cathelicidin LL-37 Relation to Potentially Malignant Lesions. Identifier: NCT06219330. Updated January 23, 2024. https://clinicaltrials.gov/study/NCT06219330
  19. ClinicalTrials.gov. Effects of Surfactants on the Innate Immune System. Identifier: NCT01951352. Updated October 2, 2019. https://clinicaltrials.gov/study/NCT01951352
  20. ClinicalTrials.gov. The Role of Anti-inflammatory Cytokines and Antimicrobial Peptide LL-37 Biomarkers in the Treatment of Periodontal Disease. Identifier: NCT04404335. Updated September 30, 2022. https://clinicaltrials.gov/study/NCT04404335
  21. ClinicalTrials.gov. Salivary TAS, TOS, LL-37 and Dental Status in Passive Smoking Children. Identifier: NCT04292548. Updated March 6, 2020. https://clinicaltrials.gov/study/NCT04292548
Additional Research: For comprehensive LL-37 literature, search PubMed: LL-37 / Cathelicidin (>1,500 publications)

⚠️ Research Use Only

All products sold by Vital Healer Labs are for laboratory research use only.
Not for human consumption, medical, or veterinary use.

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