LL-37 — Research Overview
Chemical Name: LL-37 (human cathelicidin antimicrobial peptide) Full Sequence: LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES Precursor: Encoded by the CAMP gene (cathelicidin antimicrobial peptide gene) as an 18 kDa inactive precursor protein called hCAP18 (human cationic antimicrobial protein 18). The active 37-amino acid C-terminal peptide LL-37 is released from hCAP18 by proteolytic processing by neutrophil elastase, proteinase 3, and other serine proteases at sites of infection and inflammation. Name Origin: “LL” refers to the two leucine (L) residues at the N-terminus of the peptide; “37” refers to its length of 37 amino acids. Structural Properties: Cationic amphipathic alpha-helical peptide. Net positive charge of +6 from its high content of arginine and lysine residues. Upon contact with bacterial membranes or in helicogenic environments, LL-37 forms an alpha-helix with spatially separated hydrophilic (charged) and hydrophobic faces — the structural basis for its membrane-disrupting antimicrobial mechanism. Unique Status: LL-37 is the sole member of the cathelicidin antimicrobial peptide family in humans. While other mammals (pigs, cows, horses, sheep, rabbits) express 2 to 11 distinct cathelicidins, the human genome encodes only one. This makes LL-37 a non-redundant component of the human innate immune system. Key Regulatory Axis: LL-37 expression is potently induced by vitamin D3 (1,25-dihydroxyvitamin D3, the active hormone form) through vitamin D receptor (VDR) binding to the CAMP gene promoter — establishing a direct molecular link between vitamin D status and innate antimicrobial defense capacity. Category: Endogenous cationic antimicrobial peptide (AMP) / human cathelicidin / innate immune effector / broad-spectrum antimicrobial / immunomodulator / wound healing mediator / research tool
Research Use Only — Disclaimer
The scientific literature on this page is provided strictly for educational and informational purposes. All Rogue Compounds products are intended for in-vitro laboratory research use only and are not approved by the FDA for human or animal consumption. The studies referenced below are independent third-party peer-reviewed publications. Rogue Compounds makes no claims that any product diagnoses, treats, cures, or prevents any disease or condition. Researchers are responsible for compliance with all applicable local, state, and federal regulations.
What Is LL-37?
LL-37 is the only cathelicidin antimicrobial peptide produced by humans — a distinction that makes it a uniquely non-redundant component of human innate immunity with no functional backup in the same peptide class. Discovered as the active cleavage product of the precursor protein hCAP18, LL-37 is constitutively produced by neutrophils and mast cells and is induced in epithelial cells of barrier tissues including skin, gut, lung, and urogenital tract in response to infection, inflammation, and ultraviolet irradiation.
The biological significance of LL-37 extends far beyond conventional antimicrobial peptide function. LL-37 occupies a pivotal position at the interface of innate and adaptive immunity, functioning simultaneously as a direct pathogen killer, a chemoattractant for immune cells, an immunomodulator of both pro- and anti-inflammatory responses, a wound healing promoter, an angiogenic factor, and — critically — the molecular link through which vitamin D status translates into frontline antimicrobial defense. This multifunctionality makes LL-37 one of the most extensively studied endogenous peptides in immunology, with published research spanning infectious disease, inflammatory skin conditions, sepsis, cancer biology, and antiviral immunity.
The vitamin D-LL-37 axis deserves particular attention in the research context. Vitamin D3 (1,25-dihydroxyvitamin D3) induces LL-37 expression by activating the vitamin D receptor (VDR), which binds to response elements in the CAMP gene promoter to drive transcription. This regulatory relationship explains epidemiological observations linking vitamin D deficiency to increased susceptibility to bacterial infections (particularly tuberculosis and respiratory infections), and has generated substantial research interest in the context of COVID-19, where vitamin D status, LL-37 levels, and disease severity have been studied in parallel.
A pharmacologically important consideration: LL-37’s biological activity profile is context-dependent and dose-dependent. At physiological concentrations in healthy skin and mucosa, LL-37 is anti-inflammatory and supports barrier integrity. At elevated concentrations — as occurs in psoriasis and rosacea — LL-37 drives inflammatory pathology. At deficient concentrations — as in atopic dermatitis — innate barrier protection is impaired. This bidirectional relationship between LL-37 levels and inflammatory outcome is central to understanding its research significance and is one reason it is simultaneously studied as a potential therapeutic in infection and deficiency states and as a pathological driver in inflammatory skin diseases.
Mechanism of Action
Direct membrane disruption — Gram-positive and Gram-negative bacteria: LL-37 is a cationic peptide with a net positive charge of +6. Bacterial membranes carry an overall negative surface charge due to the lipid composition of Gram-negative outer membranes (lipopolysaccharide, LPS) and Gram-positive cell walls (lipoteichoic acid, teichoic acid). Electrostatic attraction draws LL-37 to bacterial membranes, where its amphipathic alpha-helical structure enables membrane insertion. Once embedded, LL-37 disrupts membrane integrity through toroidal pore formation and membrane thinning, leading to transmembrane electrochemical gradient collapse, cytoplasm leakage, and bacterial cell death. This membrane-based mechanism is fundamentally different from antibiotic mechanisms that target specific bacterial enzymes or metabolic pathways — it is more difficult for bacteria to develop resistance to since developing resistance would require wholesale remodeling of membrane architecture.
LPS neutralization: LL-37 binds directly to lipopolysaccharide (LPS, bacterial endotoxin) with high affinity, physically sequestering LPS and preventing it from binding to TLR4 on immune cells. This LPS neutralization blocks the septic inflammatory cascade that drives cytokine storm and organ failure in Gram-negative bacterial sepsis — a mechanism with clear translational relevance to sepsis research.
Anti-biofilm activity: LL-37 disrupts and prevents bacterial biofilm formation across multiple clinically relevant pathogens including Pseudomonas aeruginosa and Staphylococcus aureus. Biofilms are organized polymicrobial communities encased in extracellular matrix that are dramatically more resistant to antibiotics and host immune clearance than planktonic bacteria. LL-37’s ability to disrupt established preformed biofilms — not just prevent their formation — distinguishes it pharmacologically from many conventional antimicrobial agents and makes it particularly relevant for chronic wound and chronic infection research.
Antifungal and antiparasitic activity: LL-37 exhibits direct killing activity against Candida albicans and other fungi, as well as antiparasitic effects, through membrane-disrupting mechanisms analogous to its antibacterial action.
Antiviral activity — broad spectrum: LL-37 has documented antiviral activity against herpes simplex virus (HSV), vaccinia virus, adenovirus, influenza, and SARS-CoV-2 through multiple mechanisms. Against enveloped viruses, LL-37 disrupts the viral lipid membrane envelope. Against SARS-CoV-2 specifically, published research has demonstrated direct binding of LL-37 to the Spike protein receptor-binding domain and to the viral accessory proteins ORF7a and ORF8, with the potential to block viral binding to the ACE2 receptor. LL-37 also promotes neutrophil extracellular trap (NET) clearance and reduces the hyperinflammatory response that drives severe COVID-19 pathology.
Chemotaxis and immune cell recruitment: LL-37 acts as a potent chemoattractant for neutrophils, monocytes, and T cells through activation of the formyl peptide receptor-like 1 (FPRL-1/FPR2) receptor expressed on these immune cells. This recruitment function links LL-37’s immediate antibacterial activity with the broader innate immune response, bringing professional immune cells to sites of infection.
Immunomodulation — anti-inflammatory arm: LL-37 exerts anti-inflammatory effects through multiple pathways, including suppression of TLR-mediated NF-kB activation (particularly in response to LPS), modulation of cytokine production in macrophages, and promotion of regulatory T cell activity. These anti-inflammatory properties explain the paradox that LL-37 can simultaneously kill bacteria while dampening the inflammatory response that bacterial products would otherwise trigger.
Wound healing and angiogenesis: LL-37 promotes re-epithelialization of wounds by stimulating keratinocyte migration through activation of the epidermal growth factor receptor (EGFR) transactivation pathway and FPRL-1 receptor signaling, driving Snail and Slug transcription factor induction, matrix metalloproteinase activation, and PI3K/Akt pathway engagement. LL-37 is also angiogenic — it promotes vascular endothelial growth factor A (VEGF-A) expression and new blood vessel formation, contributing to granulation tissue development in wound healing. Studies in ob/ob diabetic mice demonstrated that adenoviral transfer of LL-37 to excisional wounds significantly improved re-epithelialization and granulation tissue formation — directly demonstrating wound healing promotion in an impaired healing model.
Anti-apoptotic effects in keratinocytes: LL-37 protects primary human keratinocytes from apoptosis through upregulation of cyclooxygenase-2 (COX-2) and downstream survival signaling, with direct relevance to skin barrier maintenance and wound healing.
The Vitamin D-LL-37 Regulatory Axis
The relationship between vitamin D and LL-37 is one of the most clinically relevant regulatory mechanisms in innate immunity. Vitamin D3 (1,25-dihydroxyvitamin D3) is a potent inducer of LL-37 expression through the vitamin D receptor (VDR), which binds to vitamin D response elements (VDREs) in the CAMP gene promoter. This regulation has been demonstrated in macrophages, keratinocytes, neutrophils, and epithelial cells across multiple tissues.
The physiological significance is profound: vitamin D deficiency translates directly into reduced LL-37 production and impaired innate antimicrobial defense. This molecular mechanism explains why populations with vitamin D deficiency show increased susceptibility to tuberculosis (Mycobacterium tuberculosis specifically requires LL-37 for vitamin D-mediated macrophage killing) and respiratory infections. The recognition that vitamin D influences infection susceptibility through LL-37 rather than through direct hormonal effects has reframed the clinical literature on vitamin D and infection.
In the COVID-19 context, the vitamin D-LL-37 axis generated significant research interest. Several lines of evidence converged: epidemiological data linking vitamin D deficiency to worse COVID-19 outcomes, in vitro data demonstrating LL-37’s ability to bind SARS-CoV-2 spike protein and block ACE2 receptor interaction, and the known LL-37 induction pathway through vitamin D supplementation. While the clinical question of whether vitamin D supplementation meaningfully improves COVID-19 outcomes through LL-37 upregulation remains under study, the mechanistic hypothesis is well-grounded in established LL-37 biology.
LL-37 in Inflammatory Skin Disease — A Bidirectional Story
LL-37 illustrates better than almost any other endogenous peptide that “anti-inflammatory” or “pro-inflammatory” characterizations are inadequate for biologically complex molecules. LL-37 drives dramatically different outcomes in different inflammatory skin diseases, depending on whether the pathology involves deficient LL-37 (insufficient protection), normal LL-37 with aberrant processing, or excessive LL-37 (pathological inflammation).
Atopic dermatitis: LL-37 expression is deficient in atopic dermatitis skin lesions — a deficiency that explains the dramatically increased susceptibility of atopic dermatitis patients to skin infections with Staphylococcus aureus and herpes simplex virus. Impaired LL-37 induction in response to barrier disruption is a mechanistic contributor to the infection susceptibility that complicates atopic dermatitis management.
Rosacea: In rosacea, the problem is not LL-37 deficiency but aberrant processing. LL-37 is overproduced and abnormally processed by elevated kallikrein serine protease activity, generating shorter LL-37 fragments that are pro-inflammatory rather than antimicrobial. These aberrant fragments directly trigger mast cell degranulation, vasodilatation, and the characteristic erythema and flushing of rosacea. LL-37 is now established as a central pathogenic mediator in rosacea — a finding that has reframed understanding of the disease.
Psoriasis: In psoriasis, LL-37 is markedly overexpressed and plays a complex dual role. LL-37 was discovered to act as a T-cell autoantigen in psoriasis — forming complexes with self-DNA released from damaged keratinocytes that activate plasmacytoid dendritic cells through TLR9, driving the adaptive immune response that sustains psoriatic inflammation. LL-37 is simultaneously antimicrobial (explaining why psoriatic skin has low infection rates despite intense inflammation) and a central autoimmune trigger.
Published Research
Study 1 — Foundational Clinical Observation: LL-37 Is Required for Normal Wound Re-Epithelialization
Authors: Dorschner RA, Pestonjamasp VK, Tamakuwala S, Ohtake T, Rudisill J, Nizet V, Agerberth B, Gudmundsson GH, Gallo RL Year: 2003 Journal: Journal of Investigative Dermatology PMID: 12603850 Full text: https://pubmed.ncbi.nlm.nih.gov/12603850/
This landmark study established LL-37 as a required component of normal wound re-epithelialization, and linked its deficiency in chronic ulcers to impaired healing — positioning LL-37 as both a physiological wound healing mediator and a potential therapeutic target for non-healing wounds.
hCAP18 levels in acute wound skin were shown to be dramatically elevated after wounding, with the highest concentrations attained at 48 hours post-injury, declining to pre-injury baseline levels upon wound closure — establishing a precise temporal pattern of LL-37 production that correlates with the inflammatory and proliferative phases of wound repair.
hCAP18 was detected in the inflammatory infiltrate and in the epithelium migrating over the wound bed — confirming that LL-37 is actively present in the migrating keratinocyte front during re-epithelialization.
Critically, in chronic venous ulcers, hCAP18 levels were low and immunoreactivity for hCAP18/LL-37 was absent at the ulcer edge epithelium — directly implicating LL-37 deficiency as a possible contributor to re-epithelialization failure in chronic non-healing wounds.
Using an ex vivo wound healing model of organ-cultured human skin, antibody-mediated blockade of hCAP18 impaired wound epithelialization — providing experimental evidence that endogenous LL-37 production is functionally required for normal re-epithelialization rather than merely associated with the wound healing process.
Study 2 — In Vitro and In Vivo Wound Healing: LL-37 Promotes Keratinocyte Migration and Granulation Tissue Formation
Authors: Carretero M, Escamez MJ, Garcia M et al. Year: 2008 Journal: Journal of Investigative Dermatology PMID: 17805349 Full text: https://pubmed.ncbi.nlm.nih.gov/17805349/
This study directly characterized the cellular and molecular mechanisms by which LL-37 promotes wound healing in vitro and demonstrated therapeutic wound healing activity in vivo in an impaired healing animal model.
LL-37 activated migration of human keratinocyte (HaCaT) cells through phenotypic changes involving actin dynamics, augmented tyrosine phosphorylation of focal adhesion kinase and paxillin, induction of Snail and Slug transcription factors (drivers of epithelial-mesenchymal transition and migratory phenotype), and activation of matrix metalloproteinases — defining the multi-pathway mechanism by which LL-37 drives keratinocyte migration across wound surfaces.
LL-37 activated the MAPK/ERK and PI3K/Akt signaling pathways in keratinocytes, pathways central to cell survival, proliferation, and migration in wound repair contexts.
Signal transduction occurred through EGFR transactivation and induction of FPRL-1 (formyl peptide receptor-like 1) expression — identifying the receptor mechanisms through which LL-37 initiates wound healing signaling.
In vivo adenoviral transfer of the LL-37 gene to excisional wounds in ob/ob (leptin-deficient obese diabetic) mice — an established model of impaired wound healing — significantly improved both re-epithelialization and granulation tissue formation compared to control-treated wounds. This in vivo demonstration in an impaired healing model directly established the therapeutic potential of LL-37 delivery for non-healing wound applications.
Study 3 — Antimicrobial, Anti-Biofilm, and Wound Infection: LL-37 Against Polymicrobial Infected Wounds
Authors: Brogden NK, Brogden KA Year: 2013 Journal: Frontiers in Immunology (PMC) PMID: 23840194 Full text: https://pmc.ncbi.nlm.nih.gov/articles/PMC3699762/
This comprehensive review synthesized the evidence for LL-37’s antimicrobial and anti-biofilm activity against the major pathogens of chronic infected wounds, and characterized the wound healing host cell interactions that make LL-37 a promising candidate for polymicrobially infected wound therapy.
LL-37 has been shown to have antimicrobial and anti-biofilm activity against multiple Gram-positive and Gram-negative human pathogens, including Pseudomonas aeruginosa and Staphylococcus aureus — the two most clinically significant chronic wound pathogens — at concentrations achievable through exogenous administration.
LL-37 can eradicate preformed biofilms in vitro — not merely prevent biofilm formation. This distinction is clinically critical because most chronic wound infections involve established biofilms rather than planktonic bacteria, and most antibiotics have poor activity against biofilm-embedded bacteria.
LL-37 induces signal transduction in host cells contributing to wound healing, including IGF-1R phosphorylation with downstream MAPK/ERK activation — linking antimicrobial and pro-healing activities in the same molecule.
The review identified the combination of anti-biofilm and wound healing properties as potentially uniquely effective for polymicrobially infected wound treatment — addressing both the infecting pathogen community and the host tissue repair deficits simultaneously.
Study 4 — Sepsis: LL-37 Protects in Murine Sepsis Model Through Multiple Mechanisms
Authors: Nagaoka I et al. Year: 2020 Journal: PubMed indexed study PMID: 32825174 Full text: https://pubmed.ncbi.nlm.nih.gov/32825174/
This study examined LL-37’s therapeutic potential in a murine cecal ligation and puncture (CLP) sepsis model — the gold standard preclinical sepsis model — characterizing multiple protective mechanisms simultaneously.
LL-37 protected CLP-treated septic mice through at least three simultaneous mechanisms: suppression of pro-inflammatory macrophage pyroptosis (a form of inflammatory cell death that releases large amounts of pro-inflammatory contents into circulation), promotion of neutrophil extracellular trap (NET) formation and release (NETs trap and kill circulating bacteria), and ectosome release from neutrophils (membrane vesicles containing antimicrobial components).
These mechanisms function in addition to LL-37’s own bactericidal activity and LPS-neutralizing properties — establishing LL-37 as a multi-mechanism sepsis protective agent rather than a simple antimicrobial compound in this context.
The study added to the growing body of evidence that LL-37’s LPS neutralization — the ability to directly bind and sequester lipopolysaccharide from Gram-negative bacteria, preventing TLR4-mediated cytokine storm initiation — represents a meaningful anti-sepsis mechanism beyond bacterial killing.
Study 5 — Antiviral Activity: LL-37 Binds SARS-CoV-2 Spike Protein and Accessory Proteins
Authors: Published in Frontiers in Cellular and Infection Microbiology Year: 2025 Journal: Frontiers in Cellular and Infection Microbiology Full text: https://www.frontiersin.org/journals/cellular-and-infection-microbiology/articles/10.3389/fcimb.2025.1671738/full
This surface plasmon resonance (SPR) study directly characterized the binding kinetics of LL-37 to SARS-CoV-2 structural and accessory proteins, providing mechanistic data for LL-37’s documented antiviral activity against this pathogen.
LL-37 bound to the SARS-CoV-2 Spike protein across its full molecular surface — suggesting broad epitope coverage that may be active against multiple variant forms of the Spike protein rather than being variant-specific.
The strongest binding detected was between LL-37 and the viral accessory protein ORF7a (KD of 138 nM), a protein that promotes viral virulence by initiating autophagy and blocking autophagosome fusion with lysosomes. LL-37 binding to ORF7a at this affinity suggests potential for functional inhibition of this virulence mechanism.
The mechanistic hypothesis supported by these binding data — that LL-37 may shield viral surface proteins through direct binding, preventing receptor engagement and cell entry — represents a general antiviral mechanism by which antimicrobial peptides as components of innate immunity could exert broad antiviral effects.
The study concluded that these results reinforce the hypothesis that LL-37 may exert beneficial effects in counteracting SARS-CoV-2 infections, and noted that indirect therapeutic application through vitamin D-mediated LL-37 induction or direct local administration (for example through inhalation) represents conceivable clinical translation pathways.
Study 6 — Inflammatory Skin Disease: LL-37 in Psoriasis, Rosacea, and Atopic Dermatitis
Authors: Gläser R et al. (review); Multiple groups Year: 2012 and subsequent Journal: Annals of Dermatology and multiple journals PMID: 22577261 (primary review) Full text: https://pubmed.ncbi.nlm.nih.gov/22577261/
This review systematically characterized LL-37’s distinct and sometimes paradoxical roles across three major inflammatory skin diseases — atopic dermatitis, psoriasis, and rosacea — demonstrating that LL-37’s net effect depends critically on its concentration, processing, and disease context.
In atopic dermatitis, LL-37 induction may be disturbed, resulting in defective antimicrobial barrier function — explaining the dramatically elevated infection risk with Staphylococcus aureus and HSV that characterizes this condition. Restoring LL-37 levels represents a potential therapeutic strategy for atopic dermatitis.
In psoriasis, LL-37 is overexpressed and forms complexes with self-DNA released from damaged keratinocytes. These LL-37-DNA complexes activate plasmacytoid dendritic cells through TLR9 (and related TLR pathways), initiating the adaptive immune autoimmune cascade that drives psoriatic inflammation — establishing LL-37 as an autoantigen and pathogenic driver in psoriasis, not merely a protective element.
In rosacea, cathelicidin processing is disturbed, resulting in abnormal LL-37 fragments that cause inflammation, erythema, and telangiectasias through mast cell activation, rather than providing the antimicrobial protection the full-length peptide would normally provide. Elevated kallikrein 5 activity in rosacea skin drives this aberrant processing.
The review concluded that cathelicidin LL-37 is an important effector molecule of innate immunity in the skin and that these three conditions show defects in cathelicidin expression, function, or processing — each in distinct ways that require different therapeutic approaches rather than a single intervention strategy.
LL-37 Research Context: Key Themes for Research Protocol Design
No other peptide in this catalog occupies LL-37’s unique position as the sole human representative of its peptide class, regulated by one of the most clinically significant hormones (vitamin D), with documented activity spanning bacterial killing, biofilm disruption, viral inhibition, wound healing, and immune modulation. Several considerations are important for research applications.
Concentration dependence: LL-37’s effects are strongly concentration-dependent. Low physiological concentrations are anti-inflammatory and pro-healing. High concentrations can be cytotoxic to mammalian cells and pro-inflammatory in certain contexts. This dose-response complexity must be accounted for in experimental design.
Pathogen selectivity: LL-37 demonstrates the selectivity characteristic of cationic antimicrobial peptides — preferential disruption of negatively charged bacterial membranes over the neutral or positively charged membranes of mammalian cells. At physiological concentrations in tissue, mammalian cell toxicity is minimal and context-specific.
Proteolytic susceptibility and analog development: A significant limitation of LL-37 as a therapeutic is its susceptibility to protease degradation, which limits stability in biological fluids. This limitation has driven active research into LL-37 analogs and fragments with improved stability — an area with direct implications for understanding which aspects of LL-37 biology are most important to preserve in therapeutic applications.
Vitamin D connection: Because LL-37 expression is controlled by vitamin D, research into LL-37 deficiency states, infection susceptibility, and wound healing impairment must consider vitamin D status as a confounding or causal variable. This regulatory connection makes LL-37 the mechanistic link between one of the most studied nutritional deficiencies and one of the most clinically significant innate immune functions.
Current Research Status
LL-37 is not FDA-approved as a therapeutic agent for any indication. Research is active across antimicrobial applications, anti-biofilm wound care strategies, sepsis treatment, antiviral applications, inflammatory skin disease (both as a target for suppression in psoriasis/rosacea and as a therapeutic in atopic dermatitis/chronic wounds), cancer biology, and COVID-19 immunity. LL-37 analogs with improved stability, selectivity, and reduced mammalian cell toxicity represent a major active area of pharmaceutical research. No completed Phase 3 human clinical trials of exogenous LL-37 administration have been published, though multiple Phase 1 and Phase 2 investigations of LL-37 and related AMPs have been conducted.
Reconstitution Note
LL-37 is a synthetic 37-amino acid peptide. Bacteriostatic water is the standard reconstitution solvent for research applications. LL-37 dissolves readily in aqueous solution. Store reconstituted solution protected from light. Note that LL-37 is susceptible to degradation by proteases present in complex biological matrices — always confirm storage conditions and in-use period for the specific lot. Always confirm the recommended solvent against the specific lot datasheet before reconstitution.
In-Use Period and Storage
Before Reconstitution — Lyophilized Powder
Rogue Compounds stores all products refrigerated prior to shipping to maintain compound integrity from production through to delivery. Upon receipt researchers should store vials at 2 to 8 degrees Celsius immediately. Keep vials sealed, dry, and away from direct light until ready for use. Do not freeze. Repeated freeze-thaw cycling has been documented in peer-reviewed pharmaceutical formulation literature to accelerate structural degradation even in dry powder form, potentially compromising molecular integrity and experimental reproducibility.
Why We Refrigerate Instead of Freeze
Freezing and thawing introduces mechanical and osmotic stress at the molecular level. Published pharmaceutical research identifies freeze-thaw cycling as a significant risk factor for loss of structural integrity in peptides and protein-based compounds. To protect compound quality at every stage of handling and fulfillment, Rogue Compounds maintains refrigerated rather than frozen cold chain storage throughout the entire process.
After Reconstitution — Liquid Solution
Store reconstituted solutions refrigerated at 2 to 8 degrees Celsius immediately after preparation. Protect from light. Avoid repeated freeze-thaw cycles. LL-37 in solution is susceptible to protease degradation if exposed to biological matrices — use promptly and do not store with protease-containing samples. Label each aliquot with the compound name, concentration, date of reconstitution, and diluent used. Discard any solution that shows visible particulate matter or signs of contamination.
Note: Storage and in-use recommendations on this page are provided as general laboratory guidance based on standard peptide handling practices documented in peer-reviewed pharmaceutical literature. Researchers should always refer to the individual compound’s published research literature and datasheet for any specific requirements. All products sold by Rogue Compounds are intended strictly for in-vitro laboratory research use only.
Available from Rogue Compounds
View the LL-37 product page: https://roguecompounds.com/product/ll-37/