{"id":71392,"date":"2026-05-20T08:54:38","date_gmt":"2026-05-20T08:54:38","guid":{"rendered":"https:\/\/medsbase.com\/ll-37\/"},"modified":"2026-05-21T07:14:09","modified_gmt":"2026-05-21T07:14:09","slug":"ll-37","status":"publish","type":"product","link":"https:\/\/medsbase.com\/nl\/ll-37\/","title":{"rendered":"LL-37 (Cathelicidin Antimicrobial Peptide)"},"content":{"rendered":"<p><!-- medsbase-tldr-answer --><\/p>\n<div style=\"background: #fff8e1; border-left: 4px solid #f5a623; padding: 18px 22px; margin: 18px 0; border-radius: 4px;\">\n<h3 style=\"margin: 0 0 8px 0; font-size: 16px; color: #1a4a6b;\">Quick Answer \u2014 What is LL-37?<\/h3>\n<p style=\"margin: 0;\"><strong>LL-37<\/strong> (also called Cathelicidin Antimicrobial Peptide, CAP-18, or FALL-39) is a 37-amino-acid amphipathic \u03b1-helical host-defense peptide \u2014 the only human cathelicidin. It is released by proteinase-3 cleavage from the inactive proform (hCAP-18) and combines direct broad-spectrum antimicrobial activity (against bacteria, fungi, enveloped viruses, and biofilms) with potent immunomodulatory effects: LPS neutralisation, chemotaxis of neutrophils\/monocytes\/T-cells, anti-biofilm action, and pro-angiogenic wound-healing signalling. LL-37 is studied across antimicrobial-resistance research, wound-healing, atherosclerosis, psoriasis pathogenesis, and oncology. Supplied in 5 mg lyophilized vials for laboratory research use only.<\/p>\n<\/div>\n<div class=\"medsbase-trust-strip\" style=\"background: #f4f8fb; border: 1px solid #d8e3eb; padding: 12px 16px; margin: 16px 0; border-radius: 4px; font-size: 14px;\"><strong>Wat u krijgt bij MedsBase:<\/strong> Onderzoekskwaliteit lyofiliseerde peptiden \u00b7 HPLC \u226599% zuiverheid (COA op aanvraag) \u00b7 Discrete temperatuurstabiele verpakking \u00b7 Wereldwijde peptidekoerier \u00b7 1.400+ geverifieerd <a href=\"https:\/\/medsbase.com\/nl\/reviews\/\">klantbeoordelingen<\/a><\/div>\n<p class=\"medsbase-reship-line\" style=\"font-size: 14px; color: #444; margin: 8px 0 18px;\">\ud83d\udce6 Elke bestelling is gedekt door onze <a href=\"https:\/\/medsbase.com\/nl\/medsbase-re-shipment-assurance-policy\/\"><strong>Reshipment Assurance Policy<\/strong><\/a> \u2014 als uw pakket niet binnen 20 werkdagen arriveert, sturen wij het opnieuw.<\/p>\n<table class=\"medsbase-spec-table\" style=\"width: 100%; border-collapse: collapse; margin: 18px 0; font-size: 14px;\">\n<thead>\n<tr style=\"background: #2c7cb0; color: #fff;\">\n<th style=\"padding: 8px 12px; text-align: left; width: 30%;\">Specificatie<\/th>\n<th style=\"padding: 8px 12px; text-align: left;\">Detail<\/th>\n<\/tr>\n<\/thead>\n<tbody>\n<tr style=\"background: #f9f9f9;\">\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0; width: 30%;\"><strong>CAS-nummer<\/strong><\/td>\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0;\">154947-66-7 (LL-37 free base)<\/td>\n<\/tr>\n<tr style=\"background: #fff;\">\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0; width: 30%;\"><strong>Type<\/strong><\/td>\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0;\">37-amino-acid amphipathic \u03b1-helical cationic antimicrobial host-defense peptide; the only human cathelicidin (CAMP gene product); active C-terminal peptide released by proteinase-3 cleavage of the inactive proform hCAP-18; also called CAP-18 (C-terminal Cathelicidin Antimicrobial Peptide of 18 kDa proform) and FALL-39 (when including the N-terminal F residue from earlier sequencing)<\/td>\n<\/tr>\n<tr style=\"background: #f9f9f9;\">\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0; width: 30%;\"><strong>Molecuulformule<\/strong><\/td>\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0;\">C<sub>205<\/sub>H<sub>340<\/sub>N<sub>60<\/sub>O<sub>53<\/sub><\/td>\n<\/tr>\n<tr style=\"background: #fff;\">\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0; width: 30%;\"><strong>Moleculair gewicht<\/strong><\/td>\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0;\">~4,493.3 Da<\/td>\n<\/tr>\n<tr style=\"background: #f9f9f9;\">\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0; width: 30%;\"><strong>Sequentie<\/strong><\/td>\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0;\">H-Leu-Leu-Gly-Asp-Phe-Phe-Arg-Lys-Ser-Lys-Glu-Lys-Ile-Gly-Lys-Glu-Phe-Lys-Arg-Ile-Val-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg-Asn-Leu-Val-Pro-Arg-Thr-Glu-Ser-OH (LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES) \u2014 linear 37-residue cationic peptide; +6 net charge at neutral pH; folds into an amphipathic \u03b1-helix in lipid\/membrane environments. Free N- and C-termini; no disulfide bridge, no acylation, no PEGylation.<\/td>\n<\/tr>\n<tr style=\"background: #fff;\">\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0; width: 30%;\"><strong>Form<\/strong><\/td>\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0;\">Lyofiliseerd poeder (wit tot off-white)<\/td>\n<\/tr>\n<tr style=\"background: #f9f9f9;\">\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0; width: 30%;\"><strong>Zuiverheid<\/strong><\/td>\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0;\">\u226599% (HPLC geverifieerd, COA op aanvraag)<\/td>\n<\/tr>\n<tr style=\"background: #fff;\">\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0; width: 30%;\"><strong>Opslag<\/strong><\/td>\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0;\">Lyophilized: 2\u20138 \u00b0C (refrigerator) for short-term working stock; \u221220 \u00b0C for long-term storage of unopened vials. Reconstituted: 2\u20138 \u00b0C, use within ~14\u201328 days. Protect from light. Avoid repeated freeze\u2013thaw cycles. Cationic AMPs can adsorb to plastic surfaces \u2014 low-binding tubes (siliconised or Protein LoBind) are recommended for stock storage and dilution.<\/td>\n<\/tr>\n<tr style=\"background: #f9f9f9;\">\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0; width: 30%;\"><strong>Oplosbaarheid<\/strong><\/td>\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0;\">Highly soluble in bacteriostatic water, sterile water, or dilute (0.01\u20130.1%) acetic acid. Reconstitute at acidic to neutral pH; avoid high-salt or strongly basic buffers for stock solutions. The amphipathic \u03b1-helix can aggregate at high concentration \u2014 prepare working dilutions immediately before use.<\/td>\n<\/tr>\n<tr style=\"background: #fff;\">\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0; width: 30%;\"><strong>Onderzoeksgebruik<\/strong><\/td>\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0;\">Alleen voor laboratoriumonderzoek. Niet voor humaan of veterinair diagnostisch of therapeutisch gebruik.<\/td>\n<\/tr>\n<\/tbody>\n<\/table>\n<p><!-- \/medsbase-tldr-answer --><\/p>\n<h2>What Is LL-37?<\/h2>\n<p><strong>LL-37<\/strong> is the active C-terminal 37-amino-acid peptide released by proteolytic cleavage of human cathelicidin antimicrobial peptide hCAP-18 \u2014 the only cathelicidin gene product in humans, encoded by the <em>CAMP<\/em> gene on chromosome 3. The peptide takes its name from its first two residues (Leu-Leu) and its length (37 residues). It belongs to the cathelicidin family of innate-immunity host-defense peptides found across most vertebrate lineages and represents the central effector molecule in the human cathelicidin arm of innate immunity, alongside the defensin family.<\/p>\n<p>Inactive hCAP-18 proform is produced in neutrophil granules, in epithelial surfaces (skin keratinocytes, respiratory and gut epithelium), and in lower amounts by macrophages, NK cells, mast cells, B-cells, and \u03b3\u03b4 T-cells. Activation occurs by proteinase-3 cleavage (in neutrophils) or by kallikrein-5\/kallikrein-7 (in skin), liberating the bioactive 37-mer that adopts a strongly amphipathic \u03b1-helical conformation in membrane-mimetic environments. The peptide carries a +6 net positive charge at neutral pH, with cationic lysine and arginine residues concentrated on one face of the helix and hydrophobic leucine, phenylalanine, isoleucine, and valine residues on the opposing face \u2014 the canonical &#8220;amphipathic \u03b1-helix&#8221; architecture that enables selective interaction with negatively-charged microbial membranes.<\/p>\n<p>LL-37 combines two distinct host-defense modalities in a single peptide. Its <strong>direct antimicrobial activity<\/strong> spans Gram-positive bacteria (including methicillin-resistant <em>S. aureus<\/em>, MRSA), Gram-negative bacteria (including <em>E. coli<\/em>, <em>K. pneumoniae<\/em>, <em>P. aeruginosa<\/em>), enveloped viruses (HSV-1, influenza, RSV), fungi (<em>Candida<\/em>), and microbial biofilms. Its <strong>immunomodulatory activity<\/strong> includes binding and neutralisation of bacterial lipopolysaccharide (LPS) and lipoteichoic acid, chemotaxis of neutrophils \/ monocytes \/ T-cells \/ mast cells via formyl peptide receptor like-1 (FPRL1\/FPR2), modulation of TLR signalling, suppression of LPS-induced cytokine storms, induction of angiogenesis through FPRL1 signalling on endothelial cells, and stimulation of keratinocyte migration in wound repair. Dysregulation of LL-37 is implicated in the pathogenesis of psoriasis (where excess LL-37 complexes with self-DNA to activate plasmacytoid dendritic cells), atherosclerosis, and certain cancers. LL-37 is <strong>niet goedgekeurd<\/strong> by the FDA, EMA, MHRA, or any other major regulator for human therapeutic use. The research-grade LL-37 sold here is supplied <strong>uitsluitend voor laboratoriumonderzoek<\/strong> and is not intended for human or veterinary administration.<\/p>\n<h2>Mechanism of Action \u2014 Membrane Disruption + Immunomodulation<\/h2>\n<p>LL-37 acts through three principal mechanisms documented in published research:<\/p>\n<ul>\n<li><strong>Selective microbial membrane disruption via amphipathic \u03b1-helix insertion<\/strong> \u2014 In bulk aqueous solution LL-37 is largely unstructured, but on contact with a negatively-charged microbial membrane (rich in phosphatidylglycerol, cardiolipin, lipoteichoic acid, or LPS) it folds rapidly into an amphipathic \u03b1-helix. The cationic face engages with the anionic membrane surface; the hydrophobic face inserts into the lipid bilayer. At threshold peptide-to-lipid ratios, this drives formation of toroidal pores or &#8220;carpet&#8221;-style membrane disintegration, depolarising the microbial cell and disrupting essential transmembrane gradients. Mammalian cell membranes are protected by their zwitterionic outer leaflet (phosphatidylcholine, sphingomyelin) and the presence of cholesterol \u2014 providing a degree of microbial selectivity that distinguishes AMPs from broadly cytotoxic detergents.<\/li>\n<li><strong>LPS neutralisation and TLR4 pathway modulation<\/strong> \u2014 LL-37 binds directly to bacterial lipopolysaccharide (LPS) with high affinity, sequestering it from the TLR4 \/ MD-2 \/ CD14 receptor complex. This blocks LPS-driven NF-\u03baB activation, reduces downstream TNF-\u03b1 \/ IL-6 \/ IL-1\u03b2 release, and protects host tissue from sepsis-like cytokine storms during severe Gram-negative infections. The same property makes LL-37 a research tool for dissecting LPS-driven signalling.<\/li>\n<li><strong>Immunomodulation via FPRL1 (formyl peptide receptor-like 1) and downstream signalling<\/strong> \u2014 LL-37 acts as a chemoattractant for neutrophils, monocytes, and T-cells through binding to FPRL1 (FPR2), a G-protein-coupled receptor expressed broadly on innate-immunity effector cells. The same receptor on endothelial cells mediates LL-37&#8217;s pro-angiogenic effect \u2014 stimulating endothelial-cell proliferation, migration, and tube formation. Keratinocyte migration during wound re-epithelialisation is also FPRL1-dependent. The peptide additionally engages purinergic P2X7 receptors on macrophages, contributing to inflammasome modulation.<\/li>\n<\/ul>\n<p>A distinctive feature of LL-37 biology is the <strong>&#8220;sword vs shield&#8221; balance<\/strong>: at low concentrations the peptide is dominantly immunomodulatory and tissue-protective, while at high local concentrations the direct membrane-disruptive activity dominates. This concentration-dependent functional switching is one reason why LL-37 has therapeutic-research interest across both antimicrobial and wound-healing indications, and why detailed dose-response characterisation is critical in any in-vitro or in-vivo protocol.<\/p>\n<h2>Gepubliceerde onderzoeksapplicaties<\/h2>\n<p>LL-37 is used in laboratory research contexts that investigate:<\/p>\n<ul>\n<li><strong>Antimicrobial-resistance research<\/strong> \u2014 broad-spectrum minimum-inhibitory-concentration (MIC) panels against MRSA, ESBL-producing Enterobacteriaceae, carbapenem-resistant strains, and biofilm-associated pathogens; AMP-development pipeline benchmarking<\/li>\n<li><strong>Biofilm research<\/strong> \u2014 biofilm-prevention assays, established-biofilm disruption assays against <em>P. aeruginosa<\/em>, <em>S. aureus<\/em>, en <em>K. pneumoniae<\/em> \u2014 important in cystic-fibrosis and chronic-wound research contexts<\/li>\n<li><strong>LPS \/ sepsis research<\/strong> \u2014 LPS-neutralisation assays, TLR4 signalling dissection, septic-shock cytokine-storm models<\/li>\n<li><strong>Wound-healing and skin research<\/strong> \u2014 keratinocyte migration assays, dermal-fibroblast and endothelial wound-closure models; one of the primary research peptides in cutaneous wound-healing research<\/li>\n<li><strong>Psoriasis pathogenesis research<\/strong> \u2014 LL-37 \/ self-DNA \/ plasmacytoid-dendritic-cell axis dissection (LL-37 is overexpressed in psoriatic skin and complexes with self-DNA to break tolerance via TLR9 in pDCs)<\/li>\n<li><strong>Atherosclerosis research<\/strong> \u2014 LL-37 in plaque macrophages, oxidised LDL interaction, vascular-inflammation models<\/li>\n<li><strong>Oncology research<\/strong> \u2014 paradoxical pro- and anti-tumour effects depending on tumour type (LL-37 is pro-proliferative in some cancers via FPRL1, anti-tumour in others through direct membrane disruption of tumour cells)<\/li>\n<li><strong>Innate-immunity mechanistic research<\/strong> \u2014 FPRL1 signalling, P2X7 modulation, neutrophil extracellular trap (NET) biology, vitamin-D-mediated CAMP induction<\/li>\n<\/ul>\n<p>For broader context on innate-immunity and host-defense peptide research, see <a href=\"https:\/\/medsbase.com\/nl\/kpv-lysine-proline-valine\/\">KPV<\/a> (\u03b1-MSH-derived anti-inflammatory tripeptide), <a href=\"https:\/\/medsbase.com\/nl\/bpc-157\/\">BPC-157<\/a> (multi-pathway tissue-repair pentadecapeptide), and <a href=\"https:\/\/medsbase.com\/nl\/tb-500\/\">TB-500<\/a> (Thymosin Beta-4 fragment, broad tissue repair). Browse the full <a href=\"https:\/\/medsbase.com\/nl\/peptides\/\">onderzoekspeptiden catalogus<\/a> voor gerelateerde verbindingen.<\/p>\n<h2>Beschikbare sterktes en concentraties<\/h2>\n<p>MedsBase stocks LL-37 in 5 mg lyophilized vials. Available in 10-vial or 20-vial pack formats with full reconstitution guidance:<\/p>\n<table style=\"width: 100%; border-collapse: collapse; margin: 16px 0;\">\n<thead>\n<tr style=\"background: #2c7cb0; color: #fff;\">\n<th style=\"padding: 10px; border: 1px solid #ddd; text-align: left;\">Vulsterkte<\/th>\n<th style=\"padding: 10px; border: 1px solid #ddd; text-align: left;\">Typisch Onderzoeksgebruik<\/th>\n<th style=\"padding: 10px; border: 1px solid #ddd; text-align: left;\">Verpakkingsgroottes<\/th>\n<\/tr>\n<\/thead>\n<tbody>\n<tr>\n<td style=\"padding: 10px; border: 1px solid #ddd;\"><strong>5 mg<\/strong><\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">Standard research strength \u2014 multi-week MIC panels, biofilm assays, wound-healing experiments, LPS-neutralisation assays, immunomodulation dose-response work<\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">10 of 20 flesjes<\/td>\n<\/tr>\n<\/tbody>\n<\/table>\n<p>LL-37 is supplied as the unmodified linear 37-mer free-acid form (no acylation, no PEGylation, no disulfide bridge). The peptide is sensitive to plastic adsorption \u2014 researchers should use low-binding tubes for stock storage and dilution. Working concentrations in published assays range from ~0.5 \u00b5g\/mL in chemotaxis assays up to ~50 \u00b5g\/mL in direct-killing antimicrobial assays.<\/p>\n<h2>How It Compares \u2014 LL-37 vs KPV<\/h2>\n<p>LL-37 and <a href=\"https:\/\/medsbase.com\/nl\/kpv-lysine-proline-valine\/\">KPV<\/a> are both used in innate-immunity research but operate at completely different scales and target different machinery. LL-37 is a full 37-residue host-defense peptide combining direct antimicrobial membrane disruption with FPRL1-mediated immunomodulation. KPV (Lysine-Proline-Valine) is a 3-residue C-terminal fragment of \u03b1-melanocyte-stimulating hormone (\u03b1-MSH) that acts as a focused anti-inflammatory and modest antimicrobial peptide through melanocortin-receptor pathway modulation.<\/p>\n<table style=\"width: 100%; border-collapse: collapse; margin: 16px 0;\">\n<thead>\n<tr style=\"background: #2c7cb0; color: #fff;\">\n<th style=\"padding: 10px; border: 1px solid #ddd; text-align: left;\">Criterium<\/th>\n<th style=\"padding: 10px; border: 1px solid #ddd; text-align: left;\">LL-37<\/th>\n<th style=\"padding: 10px; border: 1px solid #ddd; text-align: left;\">KPV<\/th>\n<\/tr>\n<\/thead>\n<tbody>\n<tr>\n<td style=\"padding: 10px; border: 1px solid #ddd;\"><strong>Origin<\/strong><\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">C-terminus of human cathelicidin hCAP-18 (CAMP gene)<\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">C-terminus of \u03b1-melanocyte-stimulating hormone (\u03b1-MSH)<\/td>\n<\/tr>\n<tr style=\"background: #f9f9f9;\">\n<td style=\"padding: 10px; border: 1px solid #ddd;\"><strong>Lengte<\/strong><\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">37 amino acids<\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">3 amino acids<\/td>\n<\/tr>\n<tr>\n<td style=\"padding: 10px; border: 1px solid #ddd;\"><strong>Primary mechanism<\/strong><\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">Amphipathic \u03b1-helical membrane disruption + FPRL1 immunomodulation<\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">Melanocortin-pathway-modulated anti-inflammatory signalling (NF-\u03baB suppression)<\/td>\n<\/tr>\n<tr style=\"background: #f9f9f9;\">\n<td style=\"padding: 10px; border: 1px solid #ddd;\"><strong>Antimicrobial spectrum<\/strong><\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">Broad \u2014 Gram+, Gram\u2212, enveloped viruses, fungi, biofilms<\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">Narrow \u2014 primarily Gram+; weaker than LL-37 by orders of magnitude<\/td>\n<\/tr>\n<tr>\n<td style=\"padding: 10px; border: 1px solid #ddd;\"><strong>Ontstekingsremmend<\/strong><\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">Strong (LPS neutralisation, cytokine modulation)<\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">Strong (canonical anti-inflammatory research tripeptide)<\/td>\n<\/tr>\n<tr style=\"background: #f9f9f9;\">\n<td style=\"padding: 10px; border: 1px solid #ddd;\"><strong>Net charge<\/strong><\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">+6 (highly cationic)<\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">+1<\/td>\n<\/tr>\n<tr>\n<td style=\"padding: 10px; border: 1px solid #ddd;\"><strong>Structure in membrane<\/strong><\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">Amphipathic \u03b1-helix<\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">No defined secondary structure (short linear motif)<\/td>\n<\/tr>\n<tr style=\"background: #f9f9f9;\">\n<td style=\"padding: 10px; border: 1px solid #ddd;\"><strong>Best-studied indication<\/strong><\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">Antimicrobial resistance, wound healing, psoriasis<\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">IBD\/colitis models, gut inflammation, atopic dermatitis<\/td>\n<\/tr>\n<\/tbody>\n<\/table>\n<p>For research focused on broad-spectrum antimicrobial activity, biofilm disruption, or membrane-pore mechanisms, LL-37 is the canonical reference peptide. For research focused on melanocortin-pathway anti-inflammatory signalling at the cellular level, <a href=\"https:\/\/medsbase.com\/nl\/kpv-lysine-proline-valine\/\">KPV<\/a> is the more selective tool. See also <a href=\"https:\/\/medsbase.com\/nl\/bpc-157\/\">BPC-157<\/a> for tissue-repair-focused anti-inflammatory research and <a href=\"https:\/\/medsbase.com\/nl\/tb-500\/\">TB-500<\/a> for broad tissue-repair benchmarking.<\/p>\n<div style=\"background: #f4f8fb; border-left: 4px solid #2c7cb0; padding: 14px 18px; margin: 18px 0;\"><strong class=\"mb-bac-water-callout\">\ud83d\udca7 Need BAC water?<\/strong> Reconstituting any lyophilized vial requires sterile bacteriostatic water. Pair this product with our <a href=\"\/nl\/bac-water\/\"><strong>BAC Water (Bacteriostatisch Water)<\/strong><\/a> \u2014 30 mL multi-dose vial, 0.9% benzyl-alcohol-preserved, USP-grade.<\/div>\n<h2>Opslag en Reconstituering<\/h2>\n<p><strong>Voor reconstituering:<\/strong> store lyophilized vials refrigerated at 2\u20138 \u00b0C in original packaging for short-term working stock. For long-term storage, freeze unopened vials at \u221220 \u00b0C. Lyophilized LL-37 is stable under refrigeration for up to 24 months and at \u221220 \u00b0C for up to 36 months. Avoid freeze-thaw cycles of the lyophilized powder. Like all cationic AMPs, LL-37 is prone to <strong>plastic adsorption<\/strong> \u2014 even small losses to standard polypropylene tubes can confound dose-response data. Use low-binding tubes (siliconised glass, Protein LoBind, or polypropylene pre-coated with bovine serum albumin) for stock storage and serial dilutions in low-protein assay buffers.<\/p>\n<p><strong>Reconstitueringsprocedure:<\/strong> inject bacteriostatic water down the side wall of the vial (not directly onto the lyophilized cake). For a 5 mg vial, 1.0 mL of bacteriostatic water yields a 5 mg\/mL working concentration; 2.0 mL yields a 2.5 mg\/mL working stock. Swirl gently \u2014 do not vortex aggressively, as foaming entrains air and can disrupt helix folding. Allow the powder to dissolve fully (typically 1\u20132 minutes) before withdrawing. For applications sensitive to bacteriostatic agents (cell-culture experiments), reconstitute in sterile water or 0.01% acetic acid. Once reconstituted, store the vial at 2\u20138 \u00b0C and use within 14\u201328 days. Protect from light. Discard if cloudiness, particulates, or colour change appears.<\/p>\n<h2>Veelgestelde vragen<\/h2>\n<h3>Is LL-37 the same as cathelicidin?<\/h3>\n<p>LL-37 is the active C-terminal 37-amino-acid peptide released from human cathelicidin (the inactive proform hCAP-18, encoded by the CAMP gene). Cathelicidin is the family name and refers across many vertebrate species; LL-37 is the specific name of the active human cathelicidin peptide. Other names you may see in the literature \u2014 CAP-18 and FALL-39 \u2014 refer to the same molecule from different historical naming conventions.<\/p>\n<h3>How is LL-37 different from defensins?<\/h3>\n<p>LL-37 and the defensins (\u03b1- and \u03b2-defensins) are the two main families of mammalian antimicrobial peptides. Defensins are smaller, cysteine-rich, and adopt \u03b2-sheet structures stabilised by 3 disulfide bonds. LL-37 is a longer linear cationic peptide that adopts an amphipathic \u03b1-helix in membrane environments \u2014 with no disulfide bridge. Both classes share broad antimicrobial activity and immunomodulatory roles but operate through structurally distinct mechanisms.<\/p>\n<h3>What is the typical effective concentration of LL-37 in antimicrobial assays?<\/h3>\n<p>Published minimum inhibitory concentrations (MICs) for LL-37 against susceptible Gram-positive and Gram-negative pathogens generally range from 1 to 32 \u00b5g\/mL depending on strain, assay buffer ionic strength, and biofilm vs planktonic format. Higher concentrations (50\u2013100 \u00b5g\/mL) are commonly used for direct membrane-disruption studies and biofilm-eradication assays. Immunomodulatory readouts (chemotaxis, LPS neutralisation, keratinocyte migration) typically use much lower concentrations (0.5\u201310 \u00b5g\/mL). Determine dose ranges from peer-reviewed literature appropriate to your specific protocol.<\/p>\n<h3>Why does plastic adsorption matter for LL-37?<\/h3>\n<p>Cationic AMPs like LL-37 can adsorb significantly to standard polypropylene and polystyrene labware surfaces, especially in low-protein buffers. Losses of 30\u201380% to a single tube transfer have been documented in the literature for cationic peptides at low concentrations. This can produce systematic under-estimation of activity, particularly in dilution series for MIC determination. Use low-binding tubes, pre-coat tubes with BSA, or include carrier protein in dilution buffers as appropriate to the assay readout.<\/p>\n<h3>How does LL-37 distinguish microbial from mammalian membranes?<\/h3>\n<p>The selectivity arises from membrane composition. Microbial membranes (especially Gram-negative outer membranes and Gram-positive cytoplasmic membranes) are rich in negatively-charged lipids (phosphatidylglycerol, cardiolipin, LPS, lipoteichoic acid). Mammalian cytoplasmic membranes carry a zwitterionic outer leaflet (phosphatidylcholine, sphingomyelin) and a high cholesterol content that stabilises the bilayer. The cationic face of LL-37 preferentially engages the negatively-charged microbial surface; the cholesterol-stabilised mammalian membrane is much less susceptible to insertion. Selectivity is concentration-dependent \u2014 at very high local concentrations LL-37 can become cytotoxic to mammalian cells as well.<\/p>\n<h3>What is the &#8220;sword vs shield&#8221; model of LL-37 function?<\/h3>\n<p>The model describes the concentration-dependent functional switching of LL-37: at low concentrations (&lt;5 \u00b5g\/mL) the peptide is dominantly immunomodulatory and tissue-protective \u2014 chemotactic, pro-angiogenic, LPS-neutralising. At high concentrations (&gt;20 \u00b5g\/mL) the direct membrane-disruptive antimicrobial activity dominates. This dual nature underlies LL-37&#8217;s diverse roles in host defense and is one of the reasons careful dose-response characterisation is essential in any in-vitro or in-vivo research context.<\/p>\n<h3>What is the link between LL-37 and psoriasis?<\/h3>\n<p>LL-37 is markedly overexpressed in psoriatic skin lesions and binds avidly to self-DNA and self-RNA released from damaged keratinocytes. These LL-37 \/ self-nucleic-acid complexes activate plasmacytoid dendritic cells via TLR9 (DNA) and TLR7 (RNA), driving the IFN-\u03b1-rich autoimmune-like inflammation that characterises psoriasis. Targeting the LL-37 \/ pDC \/ TLR axis is an active area of psoriasis pharmacology research.<\/p>\n<h3>Why are some cancer studies pro-tumour while others are anti-tumour?<\/h3>\n<p>LL-37 has documented context-dependent effects on cancer. In some tumour types (ovarian, breast, lung, colorectal) elevated LL-37 expression correlates with worse outcome \u2014 likely through FPRL1-mediated pro-proliferative and pro-angiogenic signalling. In others (gastric, melanoma in some models) LL-37 has direct membrane-disruptive cytotoxic effect on tumour cells with weaker anti-tumour activity. The net effect depends on tumour type, local concentration, FPRL1 expression, and tumour-microenvironment composition.<\/p>\n<div class=\"medsbase-trust-strip\" style=\"background: #f4f8fb; border: 1px solid #d8e3eb; padding: 12px 16px; margin: 20px 0 8px; border-radius: 4px; font-size: 14px;\"><strong>Why order research peptides from MedsBase:<\/strong> Lyophilized HPLC \u226599% peptides \u00b7 COA available on request \u00b7 Discreet temperature-stable packaging \u00b7 Worldwide peptide courier \u00b7 <a href=\"https:\/\/medsbase.com\/nl\/medsbase-re-shipment-assurance-policy\/\">Reshipment Assurance<\/a> on every order \u00b7 1,400+ verified <a href=\"https:\/\/medsbase.com\/nl\/reviews\/\">klantbeoordelingen<\/a><\/div>\n<p><!-- medsbase-related-alts-v1 --><\/p>","protected":false},"excerpt":{"rendered":"<p>\u2705 Only human cathelicidin antimicrobial peptide (37 aa)<br \/>\n\u2705 Amphipathic \u03b1-helix; +6 net charge<br \/>\n\u2705 Broad-spectrum: Gram+, Gram\u2212, enveloped viruses, biofilms<br \/>\n\u2705 Immunomodulatory via FPRL1 + LPS neutralisation<br \/>\n\u2705 Studied in antimicrobial-resistance, wound healing, psoriasis, oncology<\/p>\n<p><strong>LL-37<\/strong> bevat synthetisch peptideverbinding.<\/p>","protected":false},"featured_media":71408,"comment_status":"open","ping_status":"closed","template":"","meta":[],"product_brand":[],"product_cat":[5426],"product_tag":[6465,6464,6463,5441],"class_list":{"0":"post-71392","1":"product","2":"type-product","3":"status-publish","4":"has-post-thumbnail","6":"product_cat-peptides","7":"product_tag-cap-18","8":"product_tag-cathelicidin","9":"product_tag-ll-37","10":"product_tag-peptide","12":"first","13":"instock","14":"shipping-taxable","15":"purchasable","16":"product-type-variable","17":"has-default-attributes"},"acf":[],"_links":{"self":[{"href":"https:\/\/medsbase.com\/nl\/wp-json\/wp\/v2\/product\/71392","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/medsbase.com\/nl\/wp-json\/wp\/v2\/product"}],"about":[{"href":"https:\/\/medsbase.com\/nl\/wp-json\/wp\/v2\/types\/product"}],"replies":[{"embeddable":true,"href":"https:\/\/medsbase.com\/nl\/wp-json\/wp\/v2\/comments?post=71392"}],"wp:featuredmedia":[{"embeddable":true,"href":"https:\/\/medsbase.com\/nl\/wp-json\/wp\/v2\/media\/71408"}],"wp:attachment":[{"href":"https:\/\/medsbase.com\/nl\/wp-json\/wp\/v2\/media?parent=71392"}],"wp:term":[{"taxonomy":"product_brand","embeddable":true,"href":"https:\/\/medsbase.com\/nl\/wp-json\/wp\/v2\/product_brand?post=71392"},{"taxonomy":"product_cat","embeddable":true,"href":"https:\/\/medsbase.com\/nl\/wp-json\/wp\/v2\/product_cat?post=71392"},{"taxonomy":"product_tag","embeddable":true,"href":"https:\/\/medsbase.com\/nl\/wp-json\/wp\/v2\/product_tag?post=71392"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}