LL-37 (human cathelicidin antimicrobial peptide / hCAP-18 C-terminal fragment) is an amphipathic 37-amino-acid host defense peptide engineered to target microbial membranes and modulate innate immune pathways. Adopting an α-helical conformation, LL-37 neutralizes bacterial lipopolysaccharide (LPS) endotoxins, binds Formyl Peptide Receptor-Like 1 (FPRL-1 / FPR2), and triggers P2X7 receptor signaling to direct cell migration, angiogenesis, and tissue repair cascades.
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| Quantity | Discounted Price |
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| 3 - 5 | $44.65 |
| 6 - 8 | $43.71 |
| 9 + | $42.30 |
LL-37 (antimicrobial peptide) is the primary active cleavage fragment of human cathelicidin antimicrobial protein 18 (hCAP-18). Comprising 37 amino acids beginning with two N-terminal leucine residues (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), LL-37 serves as an essential endogenous host defense peptide operating across central innate immunomodulatory and tissue repair systems.
Characterized by a net positive charge (+6 at physiological pH) and an amphipathic α-helical tertiary structure, LL-37 directly binds negatively charged bacterial lipopolysaccharides (LPS), neutralizing endotoxin-induced toll-like receptor 4 (TLR4) inflammatory cascades. Concurrently, LL-37 agonizes Formyl Peptide Receptor-Like 1 (FPRL-1 / FPR2) and P2X7 purinergic receptors, driving endothelial cell tubulogenesis, keratinocyte re-epithelialization, and regulated leukocyte recruitment.
Batch-verified for high analytical purity at Modern Aminos, LL-37 is offered in a pre-measured 5MG lyophilized dry powder format in a 2R glass vial. Researchers evaluating host defense kinetics, endotoxin binding capacity, and extracellular matrix remodeling utilize LL-37 alongside complementary tissue-repair reference standards available on the site, such as KPV, BPC-157, TB-500, and GHK-Cu.
| Compound Name | LL-37 (Human Cathelicidin Fragment) |
|---|---|
| Quantity / Formats Offered | 5MG Lyophilized Dry Powder in 2R Glass Vial |
| Peptide Sequence | 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 |
| Synonyms / Alt Names | LL-37, Cathelicidin, hCAP-18 (104-140), FALL-39 active peptide fragment |
| CAS Number | 154780-71-9 |
| Chemical Formula | C205H340N60O53 |
| Molecular Weight | 4493.33 g/mol |
| IUPAC Name | Human cathelicidin C-terminal 37-amino-acid peptide fragment |
| InChIKey | Protected Peptide Sequence Matrix |
| SMILES Code | Protected Peptide Sequence Matrix |
The biochemical pathways and cellular targets of LL-37 in laboratory research include:
When evaluating research efficacy and published scientific literature for LL-37:
To evaluate host defense mechanisms, immunomodulatory pathways, and tissue repair kinetics, researchers compare LL-37 against alternative reference standards available at Modern Aminos:
In cellular inflammation and host defense research, structural targeting determines pathway activation:
| Compound / Reference | Chemical Structure & Class | Core Mechanism of Action | Research Focus & Profile |
|---|---|---|---|
| LL-37 | 37-Amino-Acid Amphipathic Cathelicidin Peptide | Binds LPS endotoxins, disrupts microbial membranes via pore formation, and agonizes FPR2/P2X7 receptors | Focuses on host defense, LPS neutralization, cell migration, re-epithelialization, and microvascular angiogenesis |
| KPV | α-MSH C-Terminal Tripeptide (Lys-Pro-Val) | Inhibits NF-κB nuclear translocation to downregulate pro-inflammatory cytokines (TNF-α, IL-6) | Focuses on targeted mucosal barrier anti-inflammation, gut epithelial cell stabilization, and acute cytokine dampening |
| BPC-157 | Synthetic 15-Amino-Acid Gastric Cytoprotective Peptide | Upregulates VEGFR2 expression, activates FAK/Paxillin pathways, and modulates NO synthesis | Focuses on cytoprotective tissue repair, tendon/ligament fibroblast migration, and gut mucosal healing |
| GHK-Cu | Copper-Chelated Tripeptide (Gly-His-Lys) | Upregulates collagen, elastin, and extracellular matrix (ECM) gene networks while stimulating SOD1 antioxidant activity | Focuses on tissue remodeling, extracellular matrix synthesis, angiogenesis, and anti-inflammatory signaling |
Yes, Modern Aminos is a highly trusted vendor for high-purity research chemicals and reference peptides. Every batch of LL-37 undergoes strict third-party analytical testing (including HPLC and Mass Spectrometry) to verify minimum 98%+ chemical purity, exact 37-amino-acid sequence fidelity, correct molecular weight (4493.33 g/mol), and complete absence of heavy metals or synthesis impurities.
LL-37 is the sole human cathelicidin antimicrobial peptide. It is derived from the enzymatic cleavage of the pro-protein hCAP-18 and consists of 37 amino acids starting with two leucine residues.
LL-37 adopts an amphipathic α-helical structure that interacts electrostatically with negatively charged microbial phospholipid membranes. It inserts into the lipid bilayer to form toroidal pores, disrupting membrane potential and causing cell lysis.
LL-37 directly binds bacterial LPS endotoxins, sequestering them from TLR4 receptor complexes. This inhibits downstream NF-κB signaling and suppresses the release of pro-inflammatory cytokines such as TNF-α, IL-1β, and IL-6.
LL-37 acts as an agonist for Formyl Peptide Receptor-Like 1 (FPRL-1 / FPR2) and purinergic P2X7 receptors, stimulating MAPK/ERK cascades that regulate cell migration, re-epithelialization, and microvascular tubulogenesis.
LL-37 combines direct microbial membrane perturbation with FPR2-mediated chemotaxis and LPS neutralization. KPV focuses primarily on NF-κB anti-inflammatory signaling.
Modern Aminos utilizes High-Performance Liquid Chromatography (HPLC) to confirm active chemical purity exceeding 98% and Mass Spectrometry (MS) to verify exact molecular weight (4493.33 g/mol) and 37-amino-acid sequence identity prior to batch release.
Lyophilized LL-37 5MG glass vials should be stored tightly sealed in a cool, dry environment (15°C to 25°C) or refrigerated for long-term preservation. Protect from direct heat, light exposure, and atmospheric moisture to maintain solid-state peptide stability.
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