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Product | LL-37 5MG

LL-37 5MG

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.

€42.00

What is LL-37 Peptide?

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.

Chemical and Molecular Data

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

What are the Mechanisms of Action?

The biochemical pathways and cellular targets of LL-37 in laboratory research include:

  • LPS Binding & Endotoxin Neutralization: The cationic lysine and arginine residues of LL-37 electrostatically bind the anionic lipid A region of bacterial lipopolysaccharides (LPS). This prevents LPS interaction with LBP (LPS-binding protein) and CD14/TLR4 complexes, suppressing pro-inflammatory NF-κB activation and cytokine output (TNF-α, IL-1β, IL-6).
  • FPR2 / FPRL-1 & P2X7 Receptor Agonism: LL-37 binds Formyl Peptide Receptor-Like 1 (FPRL-1 / FPR2), triggering intracellular calcium mobilization and MAPK/ERK signaling. This drives directional chemotaxis of monocytes, neutrophils, and endothelial cells, accelerating microvascular angiogenesis and tissue repair.
  • Direct Antimicrobial Membrane Perturbation: In microbial cell models, LL-37 adopts an amphipathic α-helical conformation upon encountering lipid bilayers. It aligns parallel to the cell membrane before inserting vertically to form toroidal pores, disrupting transmembrane electrochemical gradients and osmotic equilibrium.

What do Preclinical & Academic Studies Show for LL-37?

When evaluating research efficacy and published scientific literature for LL-37:

  • Host Defense Kinetics & Antimicrobial Action (PubMed): Landmark bioenergetic studies cataloged on PubMed (PMID: 11017138) confirm that LL-37 neutralizes Gram-negative and Gram-positive bacterial membranes while regulating host immune responses without inducing non-specific cell lysis.
  • Wound Healing & Angiogenic Remodeling (PMC): Comprehensive biomedical reviews archived in PMC (PMC3836653) document LL-37’s capacity to accelerate re-epithelialization, promote endothelial tubulogenesis via FPR2, and modulate extracellular matrix synthesis in cell culture models.
  • Chemical Profiling & Identification (PubChem): Official structural characterization maintained on PubChem verifies the molecular mass (4493.33 g/mol), 37-amino-acid sequence identity, and HPLC mass spectrometry profile of CAS 154780-71-9.

How does LL-37 compare to other compounds?

To evaluate host defense mechanisms, immunomodulatory pathways, and tissue repair kinetics, researchers compare LL-37 against alternative reference standards available at Modern Aminos:

LL-37 vs. KPV (α-MSH Tripeptide) in Inflammatory Signaling

In cellular inflammation and host defense research, structural targeting determines pathway activation:

  • LL-37: Dual-action antimicrobial and immunomodulatory 37-amino-acid peptide. Directly neutralizes LPS endotoxins, forms membrane pores in pathogens, and stimulates FPR2/P2X7 receptors to drive cellular migration and angiogenesis.
  • KPV (α-MSH C-Terminal Tripeptide): Targeted tripeptide (Lys-Pro-Val). Operates primarily by blocking NF-κB nuclear translocation to dampen acute mucosal and epithelial cytokine cascades without direct pore-forming membrane activity.
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

Frequently Asked Questions (FAQs)

1. Is Modern Aminos a reliable place to buy LL-37?

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.

2. What is LL-37 peptide and how is it derived?

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.

3. How does LL-37 exert its direct antimicrobial membrane effects?

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.

4. How does LL-37 interact with Lipopolysaccharides (LPS)?

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.

5. What specific receptor pathways does LL-37 target in host cells?

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.

6. How does LL-37 compare to KPV in cellular research models?

LL-37 combines direct microbial membrane perturbation with FPR2-mediated chemotaxis and LPS neutralization. KPV focuses primarily on NF-κB anti-inflammatory signaling.

7. How does Modern Aminos verify the chemical purity and mass identity of LL-37?

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.

8. What are the recommended storage parameters for lyophilized LL-37 2R glass vials?

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.

DISCLAIMER: All compounds and research materials provided by Modern Aminos are strictly for laboratory and research use only. They are not approved for human consumption by the Food and Drug Administration (FDA). No products are approved for oral, sublingual, nor in vivo use. These products should not be used for any form of in vivo experimentation or for any other non-laboratory purpose. Any violation or indication of human or animal use will result in immediate removal from being able to purchase products in the future. By purchasing these products, you acknowledge that they will be used exclusively within a controlled and qualified research environment.

Why Choose Modern Aminos?

Modern Aminos is the best place to buy peptides online. We are a trusted Research Chemicals vendor with formulations that meet industry standards and comply with quality regulations in Europe, USA, and Canada to ensure product safety and efficiency.

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DISCLAIMERS

The products available for purchase from Modern Aminos are intended solely for research and laboratory use. These compounds are not designed for human consumption or the diagnosis, treatment, cure, or prevention of any disease or condition.

All customers are presumed to be research professionals who understand that any compounds purchased from Modern Aminos will be handled in accordance with safety protocols mandated by their respective regulatory agencies.

Modern Aminos does not endorse the use of these products in a non-clinical setting or any other non-laboratory-based operations. By purchasing any of these compounds, you acknowledge that you will use them for legitimate research purposes only.

Modern Aminos shall not be held liable for injuries or damages resulting from the handling or use of our products. If you do not agree with these conditions, we advise  you not to proceed with the purchase of any research compounds from our company.

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