LL-37 Peptide | Antimicrobial Research
RESEARCH PEPTIDE

LL-37 Peptide | Antimicrobial Research

Synthetic Cathelicidin Antimicrobial Peptide — Research Peptide
$49.00
LL-37 is the mature 37-residue human cathelicidin peptide supplied as a lyophilized laboratory reference material for membrane-interaction and host-defense peptide research. Research use only. Not for human or veterinary use.
✓ Scientific Identity Established
⏳ Laboratory Testing In Progress
⏳ Batch Documentation Pending
✓ Research Use Only
✓ U.S. Fulfillment
In Laboratory Testing
Lot Verification Variant-specific documentation
Traceable Lots VBL lot identification
Primary Literature Peer-reviewed sources
Research Use Only Laboratory research materials

Scientific Specifications

Reference characteristics for laboratory research materials.

CAS Number
154947-66-7
Purity
≥98%
Molecular Formula
C205H340N60O53
Molecular Weight
4493.3
Appearance
White lyophilized powder
Storage
-20°C
Research Classification
Research Use Only (RUO). Not for human or veterinary use.

SCIENTIFIC OVERVIEW

Scientific background and research classification for this laboratory reference material.

LL-37 is the mature form of the only human cathelicidin host-defense (antimicrobial) peptide, a 37-residue L-peptide (LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES) released by processing of the hCAP18 precursor. CAS 154947-66-7; molecular formula C205H340N60O53. It is cysteine-free, unmodified, with a free N-terminus and free C-terminal acid, and is supplied as a lyophilized peptide reference material for laboratory research use only.

As a research material, LL-37 is studied as a prototypical cationic amphipathic antimicrobial peptide and innate-immune effector. It is a plain, unmodified peptide entity distinct from truncated analogs (for example KR-12) that are sometimes studied alongside it.

Primary Research Category
Immune Regulation
Material Type
Lyophilized Peptide
Intended Use
Laboratory Research
Research Categories
Innate Immunity Immune Regulation Inflammation

Mechanism of Action

Molecular interaction profile describing how this research material engages receptor systems and influences downstream biological signaling pathways.

LL-37's principal antimicrobial activity is attributed to direct interaction with and disruption of microbial membranes by the cationic amphipathic peptide, rather than to a defined receptor. Structural studies describe its helical, membrane-associated conformation (Wang, 2008). LL-37 also has reported immunomodulatory activity involving host receptors (for example formyl peptide receptor 2), but these receptors and the membrane-disruption mechanism are not represented in the governed molecular-target or pathway vocabularies; accordingly those governed fields are left empty by design and no near-match target or pathway is asserted.

Primary Organ Systems
  • Immune System
  • Integumentary System

Research Documentation

Laboratory documentation is presented when available for the selected product specification and current lot.

In Laboratory Testing
Laboratory Documentation In Progress

Laboratory documentation for the current lot is being completed.

Scientific References
Peer-Reviewed Literature

Explore published literature, clinical investigations, and foundational scientific research.

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Laboratory Resources
Technical Guidance

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Related Research
Companion Materials

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Research Center

Scientific literature, laboratory resources, and related materials curated to support research involving this research material.

Scientific References
Peer-Reviewed Literature

Explore curated publications from peer-reviewed journals including clinical investigations, mechanistic studies, and foundational scientific literature.

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Scientific Dossier
Deeper Technical Treatment

Comprehensive scientific documentation including literature review, mechanism, pharmacology, and study data for this research material.

Laboratory Resources
Technical Guidance

Storage guidance, handling information, analytical standards, research policies, and laboratory support documentation.

Research Library

Curated peer-reviewed literature selected to provide scientific context for this research material.

Mechanistic Study•Proceedings of the National Academy of Sciences of the United States of America• 1995

FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis

Foundational identification of FALL-39 (the precursor designation for the peptide later named LL-37) as a cysteine-free putative human peptide antibiotic expressed in bone marrow and testis.
Velora Research Insight
Discovery/identification of the human cathelicidin peptide. Boman/Gudmundsson/Agerberth originating lineage (Karolinska). Foundational molecular identification.
PubMed →DOI →
Mechanistic Study•European Journal of Biochemistry• 1996

The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes

Characterization of the human FALL39 gene and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes — the origin of the LL-37 designation and its biosynthetic processing.
Velora Research Insight
Establishes the LL-37 name and precursor processing. Same Gudmundsson/Agerberth originating lineage as VSE-PUB-000108 (investigator concentration disclosed; not an additional independent lineage).
PubMed →DOI →
Structural Biology•Journal of Biological Chemistry• 2008

Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles

Determination of the three-dimensional structures of LL-37 and its minimal active fragment KR-12 in lipid micelles, characterizing the membrane-associated amphipathic helix underlying LL-37's activity.
Velora Research Insight
Independent structural-biology evidence (Wang, UNMC) for the membrane-associated conformation — the basis for representing the mechanism as membrane interaction rather than a governed receptor target. Fully independent of the originating lineage.
PubMed →DOI →
Review Article•Cellular Immunology• 2012

A comprehensive summary of LL-37, the factotum human cathelicidin peptide

Comprehensive independent review synthesizing LL-37's antimicrobial and immunomodulatory biology across many studies — the 'factotum' human cathelicidin.
Velora Research Insight
Fully independent evidence synthesis (Schoofs group, KU Leuven) situating LL-37's multifunctional biology; carried as evidence-scoped context, not a product efficacy claim.
PubMed →DOI →