LL-37 10mg – Research Peptide

Research Area: Antimicrobial & Immunology Research

Product Description

LL-37 is a 37-amino-acid cationic antimicrobial peptide derived from the human cathelicidin precursor hCAP18. It is the only known cathelicidin-derived antimicrobial peptide identified in humans and has been extensively studied in the context of innate immune defense, microbial membrane interactions, immunomodulation, and inflammatory signaling.

LL-37 is an amphipathic peptide capable of interacting with lipid membranes and has been investigated for its broad antimicrobial activity against different classes of microorganisms. In addition to membrane-associated activity, research has examined LL-37 as a signaling molecule involved in chemotaxis, immune-cell recruitment, and modulation of inflammatory responses.

LL-37 is supplied as a lyophilized powder for qualified laboratory research. The material is intended exclusively for in vitro, analytical, and non-clinical research applications.

Product Designation Note

LL-37 is the C-terminal 37-amino-acid peptide derived from human cathelicidin antimicrobial protein (hCAP18). It should be distinguished from the full-length hCAP18 precursor and from synthetic LL-37 analogs or modified derivatives.

The product described here refers to the native LL-37 amino acid sequence: LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES.

Research Applications

LL-37 may be used as a research material in studies involving:

• Antimicrobial peptide activity
• Microbial membrane interactions
• Host-defense peptide biology
• Innate immune signaling
• Immunomodulatory mechanisms
• Chemotaxis and immune-cell recruitment
• Inflammatory signaling pathways
• Peptide–lipid and peptide–membrane interactions
• Tissue and epithelial biology
• Peptide structure and stability
• Analytical characterization and identification
• Assay development and method validation

Research Background

LL-37 is generated through proteolytic processing of the human cathelicidin precursor hCAP18. The mature peptide is expressed in association with neutrophils and epithelial tissues and has been investigated as an important component of human innate immune defense.

Research has demonstrated that LL-37 interacts with microbial membranes and can exhibit antimicrobial activity. Its amphipathic structure and cationic character are important areas of investigation in studies examining peptide–lipid interactions and membrane disruption.

Beyond direct antimicrobial activity, LL-37 has been investigated for immunomodulatory properties. Experimental studies have reported interactions with immune-cell signaling and chemotactic responses, including recruitment of neutrophils, monocytes, and T lymphocytes.

Antimicrobial & Membrane Research

A major area of LL-37 research concerns interactions between the peptide and microbial lipid membranes. Its cationic and amphipathic characteristics allow researchers to investigate peptide association with negatively charged membrane components, membrane organization, permeability, and microbial susceptibility.

LL-37 has therefore become an established experimental model for studying host-defense peptides, antimicrobial mechanisms, membrane biophysics, and potential strategies for investigating antimicrobial resistance.

Immunology & Inflammatory Signaling

LL-37 is also studied as an immunomodulatory peptide. Experimental research has investigated its effects on leukocyte migration, calcium signaling, cytokine-associated responses, and interactions between innate and adaptive immune components.

Studies have identified interactions involving formyl peptide receptor-like 1 (FPRL1), providing a mechanistic basis for investigating LL-37-mediated chemotactic and immune-cell responses.

Tissue & Cellular Research

LL-37 is expressed in several epithelial environments and has been investigated in relation to epithelial biology, cellular signaling, tissue responses, and host–microbe interactions.

These properties make LL-37 useful as a research material for studying the relationship between antimicrobial defense, inflammation, cellular communication, and tissue homeostasis under controlled experimental conditions.

Product Specifications

The molecular formula, sequence, PubChem identification, and molecular weight are consistent with the human LL-37 record in PubChem.

Storage and Handling

• Store the lyophilized material according to validated laboratory procedures and supplier specifications.
• Protect from excessive heat, moisture, and direct light.
• Keep the container sealed when not in use.
• Any reconstitution or preparation should be performed according to an appropriate validated laboratory protocol.
• Avoid unnecessary repeated freeze–thaw cycles where applicable.
• Handle using appropriate laboratory practices for synthetic peptide research materials.

Compliance Notice

FOR RESEARCH USE ONLY.

LL-37 is supplied as a research material for qualified laboratory use and is not intended for human or veterinary administration. The biological activities described above represent findings from experimental and preclinical research and should not be interpreted as established therapeutic claims.