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These products are for laboratory research only and not intended for medical use. They are not FDA-approved to diagnose, treat, cure, or prevent any disease. By purchasing, you certify they will be used solely for research and not for human or animal consumption.
LL-37 is a 37-amino-acid cationic peptide and the only known human member of the cathelicidin family of antimicrobial peptides. It corresponds to the C-terminal segment of the precursor protein hCAP-18, which is cleaved extracellularly to release the mature peptide. LL-37 is studied in laboratory models involving innate immune defense, membrane interactions, inflammatory signaling, biofilm dynamics, and cellular recruitment.
This research peptide is verified for identity, composition consistency, and 99%+ purity through analytical quality-control testing. Certificate of Analysis documentation is available for LL-37 (5 mg).
Products from Elite Miami Peptides do not include usage instructions, as they are strictly for in vitro research and prohibited by law for human or animal use. Misuse or unlawful application will result in permanent denial of service.
Each vial contains exactly what’s indicated on the label. For instance, a 10mg vial contains precisely 10mg of lyophilized peptide. Researchers may divide it into smaller research portions—such as four 2.5mg aliquots—but the total content remains the same.
Yes. All peptides are supplied in lyophilized powder form and do not come reconstituted. Any extra materials required for research, such as solvents or diluents, must be obtained separately.
When stored as a dry powder, peptides remain stable for up to 2 years.
Once reconstituted, the solution should be kept refrigerated and is typically stable for up to 2 months under proper storage conditions.
LL-37 is an amphipathic, alpha-helical host-defense peptide studied for its ability to interact with microbial membranes and influence immune signaling pathways. Experimental research examines its involvement in membrane disruption, cytokine regulation, immune-cell recruitment, macrophage activation, biofilm behavior, and tissue-repair signaling. Its combined antimicrobial and immunomodulatory properties make it a widely used research compound for investigating innate immunity and host-defense mechanisms.
LL-37 is a naturally occurring peptide produced by the human immune system. Researchers use it to study how immune cells respond to microorganisms, how inflammation is regulated, how bacterial biofilms behave, and how tissue-repair signals are activated. LL-37 supplied for research is intended exclusively for laboratory and in-vitro investigation and is not approved for human or animal use.
⚠️ Disclaimer: this product is not approved for medical use and is not intended to diagnose, treat, or prevent any disease. All information provided is for educational and research purposes only, and this product must never be used in humans or animals.
LL-37 was identified during the 1990s as the active peptide released from human cationic antimicrobial protein 18, also known as hCAP-18. An earlier form was described as FALL-39 before researchers characterized the shorter, mature 37-amino-acid sequence now known as LL-37. Subsequent structural studies established its amphipathic alpha-helical configuration and membrane-interacting properties. It has since become a reference human antimicrobial peptide in research involving innate immunity, inflammation, and host-defense signaling.
Classification: Human cathelicidin-derived cationic antimicrobial peptide Molecular Formula: C₂₀₅H₃₄₀N₆₀O₅₃ Molecular Weight: 4493.3 g/mol Sequence Length: 37 amino acids Sequence: LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES Three-Letter 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 CAS Number: 154947-66-7 PubChem ID: CID 16198951 Structural Characteristic: Amphipathic alpha-helical conformation
LL-37 has been examined in immunology, microbiology, and cellular research models for its interaction with microbial membranes and host-signaling pathways. Studies have investigated direct membrane disruption, cytokine regulation, immune-cell recruitment through formyl peptide receptor-associated signaling, activity in bacterial biofilm models, macrophage activation, and cellular signal transduction. These findings support its continued use as a laboratory tool for studying innate immune responses and host-defense mechanisms.
In simple terms, researchers study LL-37 to understand how a naturally occurring immune peptide interacts with microorganisms and communicates with immune cells. Laboratory experiments examine how it affects microbial membranes, inflammation-related signals, bacterial biofilms, macrophage activity, and tissue-repair pathways. These studies are conducted to better map immune-system processes, not to establish directions for human or veterinary use.
Dürr, U. H. N., Sudheendra, U. S., & Ramamoorthy, A. (2006). LL-37, the only human member of the cathelicidin family of antimicrobial peptides. Biochimica et Biophysica Acta – Biomembranes, 1758(9), 1408–1425. Oren, Z., Lerman, J. C., Gudmundsson, G. H., Agerberth, B., & Shai, Y. (1999). Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes. Biochemical Journal, 341(3), 501–513.
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These products are for laboratory research only and not intended for medical use. They are not FDA-approved to diagnose, treat, cure, or prevent any disease. By purchasing, you certify they will be used solely for research and not for human or animal consumption.
All compounds from Elite Miami Peptides are intended strictly for laboratory research purposes.
They are not for human use, consumption, or therapeutic applications.
Products are supplied exclusively to qualified professionals working in compliance with all applicable laws and regulations.
