LL37

Researchers investigate peptide interaction and signaling using LL-37 in experimental settings. Laboratory teams explore experimental immune-related research models in controlled environments. Immune-related research models examine how peptides function in cellular defense systems. Scientists conduct laboratory-based peptide stability studies under various conditions. Research groups examine how peptides maintain structure and function in experimental frameworks. These studies occur exclusively in research settings without clinical applications.

LL-37 is investigated in research environments for peptide interaction analysis. Scientists have studied this compound within controlled laboratory models using standardized protocols. The formulation is explored for experimental peptide interaction research in academic facilities. Researchers evaluate the peptide under controlled conditions without outcome claims.

Store LL-37 in cool, dry, light-protected conditions between 2-8°C. Light-protected conditions mean storage away from direct sunlight and intense artificial lighting. This product is intended for laboratory handling only by qualified research personnel. Qualified personnel have received appropriate training in peptide handling and storage procedures. Avoid moisture exposure as water content can affect peptide stability and quality. Avoid heat exposure above recommended temperature ranges to maintain structural integrity. Structural integrity refers to peptides maintaining their proper molecular configuration. Reconstituted solutions should follow established laboratory guidelines specific to peptide research protocols.

Each LL-37 batch undergoes comprehensive purity verification procedures through analytical testing. Analytical testing uses scientific instruments to measure peptide composition and quality. Our processes ensure batch-to-batch consistency across all research supply orders. Internal quality assurance standards follow research-grade supply positioning for peptide compounds. Research-grade supply means products meet specifications required for scientific laboratory use. Testing protocols verify peptide purity and structural characteristics using validated methods. Every unit meets our specifications before receiving distribution approval. Laboratory certificates accompany each order for institutional tracking and compliance documentation.

• CAS: 597562-32-8
• Chemical Formula: C₂₀₅H₃₄₀N₆₀O₅₃
• Molecular Weight: 4493.3 g/mol
• Peptide Sequence: Leu-Leu-Gln-Asp-Phe-Phe-Arg-Asn-Lys-Ser-Lys-Lys-Ile-Gln-Gly-Glu-Lys-Leu-Lys-Lys-Asp-Arg-Ile-Arg-Asn-Thr-Ala-Ile-Arg-Asn-Leu-Ile-Gly-Arg-Ile-Ala-Leu
• Synonyms: Cathelicidin, ropocamptide, Bac4, Cathelicidin antimicrobial peptide 18
• Shelf life: 24 months from the manufacturing date.

LL-37 is a short synthetic peptide consisting of 37 amino acids in sequence. This peptide is derived from a larger naturally occurring protein found in research models. Immune-related peptides are studied in research to understand molecular defense mechanisms. Molecular defense mechanisms describe how cells respond to external molecular challenges. The general role of peptides in laboratory research models includes serving as molecular tools. Molecular tools help scientists investigate cellular processes in controlled experimental settings. Researchers examine how this peptide interacts with various molecules and cellular components. Laboratory research investigates peptide stability, structure, and interaction patterns in controlled systems.

LL-37 provides a synthetic research peptide formulation developed for scientific applications. Synthetic peptides are manufactured compounds created through chemical synthesis processes. Each batch undergoes high-purity testing to ensure compound consistency across orders. The formulation is designed for controlled laboratory environments conducting peptide interaction research. Peptide interaction research examines how peptides behave with other molecules in systems. Secure packaging with discreet shipment protects the peptide during transit to research facilities.

LL-37 is a 37-amino acid cationic antimicrobial peptide derived from the C-terminal region of human cathelicidin precursor protein hCAP-18. It is the only cathelicidin in the human genome and is studied in research models for its roles in innate immune defence, microbial membrane disruption, wound-associated cellular signalling, and immunomodulatory receptor interactions.

In controlled research systems, LL-37 exerts antimicrobial activity by inserting into and disrupting bacterial membranes. Its amphipathic alpha-helical structure facilitates interaction with negatively charged bacterial lipopolysaccharide and phosphatidylglycerol, leading to membrane permeabilisation. This mechanism has been characterised using fluorescent dye leakage assays, electron microscopy, and minimum inhibitory concentration studies in vitro.

Beyond direct membrane disruption, LL-37 has been investigated in research models for interactions with formyl peptide receptor 2 (FPR2/ALX), P2X7 purinergic receptors, and epidermal growth factor receptor (EGFR), with downstream effects on inflammatory signalling, cellular migration, and growth factor pathway activation studied in cell-based systems.

LL-37 is typically reconstituted in sterile water or phosphate-buffered saline. Due to its cationic character, it may interact with negatively charged surfaces including certain plastics and glass; use of low-binding tubes is recommended. Stock solutions should be aliquoted and stored at -80°C to minimise degradation from repeated freeze-thaw cycling.

No. LL-37 as supplied by Elivena is a research-grade compound for use in controlled laboratory settings only. It is not approved for human administration, therapeutic use, or clinical application outside formally registered clinical programmes.