LL-37 is a healing & repair research compound currently in stock directly from a verified Chinese manufacturer. Every batch is HPLC-verified and shipped with a Certificate of Analysis (COA). Sourcing is direct — no intermediaries. Minimum order value is $600 USD. International shipping available.
LL-37 is the only known human cathelicidin antimicrobial peptide, derived from the C-terminal cleavage of the precursor protein hCAP18 (human cationic antimicrobial protein 18). The 37-amino acid sequence — LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES — begins with two leucine residues (LL) and terminates at residue 37, giving rise to its designation. As an amphipathic α-helical peptide, LL-37 adopts a helical conformation in the presence of anionic membranes, which is central to its membrane-disruption activity against bacteria and its interaction with mammalian cell surface receptors.
Research interest in LL-37 spans multiple fields. In innate immunity, it functions as both a direct antimicrobial agent and an immunomodulator — activating dendritic cells, macrophages, and mast cells, inducing cytokine production, and modulating Toll-like receptor (TLR) signaling. In wound healing research, LL-37 has been studied for its ability to promote re-epithelialization and angiogenesis via formyl peptide receptor 2 (FPR2/ALX) and EGFR transactivation. More recently, research has examined LL-37 in the context of cancer biology — where it exhibits context-dependent roles, acting as a tumor suppressor in some cancers and a growth promoter in others.
PeptidesFromChina.co supplies LL-37 as a lyophilized powder at 99%+ purity, verified by HPLC and Mass Spectrometry. Certificate of Analysis accompanies every batch. All products are for laboratory research use only and are not for human consumption.
| Chemical Class | Human cathelicidin antimicrobial peptide (AMP) |
|---|---|
| Synonyms | Cathelicidin LL-37, hCAP18 C-terminal peptide, FALL-39 |
| Sequence | LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES |
| Amino Acids | 37 |
| Molecular Formula | C₂₀₅H₃₄₀N₆₀O₅₃ |
| Molecular Weight | 4493.3 Da |
| CAS Number | 154947-66-7 |
| Research Areas | Innate immunity, antimicrobial pharmacology, wound healing, immunomodulation, TLR signaling, cancer biology |
| Form | Lyophilized powder |
| Storage | −20°C long-term; 2-8°C aqueous (use within 1 week) |
| Name | Strength | Pack Size | Purity | Availability | Price (USD) |
|---|---|---|---|---|---|
| LL-37 | 5 mg | 10 vials | ≥98% | In Stock | $113.00 |
Testing method: HPLC / LC-MS. Every batch is tested before shipment. Purity ≥99% confirmed per batch.
Certificate of Analysis (COA) is included with every order. Documentation covers purity, molecular weight, and batch identification.
LL-37 exhibits broad-spectrum antimicrobial activity against Gram-positive and Gram-negative bacteria, fungi, and some enveloped viruses. Its amphipathic helical structure enables membrane insertion and disruption of bacterial lipid bilayers — a mechanism studied as a basis for resistance-proof antimicrobial design. Minimum inhibitory concentration (MIC) studies, membrane permeabilization assays, and resistance evolution experiments using LL-37 as a reference AMP are core applications in antimicrobial peptide research.
LL-37 acts on multiple innate immune cell types via receptor-mediated signaling: FPR2/ALX on neutrophils and macrophages, P2X7 on dendritic cells, and FPRL1 on monocytes. Research has examined LL-37's role in TLR4 and TLR9 signaling modulation — both potentiating and suppressing TLR-mediated inflammation depending on context and concentration. These immunomodulatory properties make LL-37 a tool for studying the boundary between direct antimicrobial action and immune cell signaling in innate defense research.
Research has documented LL-37's ability to promote wound closure in ex vivo and rodent wound healing models via EGFR transactivation and FPR2-mediated cell migration signaling. Studies have examined re-epithelialization rates, keratinocyte proliferation, and angiogenic marker expression following LL-37 application to wound models. This wound-healing activity — separate from its antimicrobial properties — has generated research interest in LL-37 as a dual-function peptide for tissue repair biology.
LL-37 is the only human cathelicidin — making it the primary innate antimicrobial peptide of human skin and mucosal surfaces. Unlike most AMPs, it also has extensive immunomodulatory activity via multiple receptors (FPR2, P2X7, FPRL1), wound-healing properties via EGFR transactivation, and complex roles in cancer biology. This multifunctionality makes it a versatile but complex research tool.
LL-37 has been reported to suppress tumor growth in some cancers (e.g., colon) while promoting proliferation and metastasis in others (e.g., ovarian, lung). The context dependence appears to involve receptor expression patterns, tumor microenvironment composition, and local peptide concentration. This complexity is a primary reason LL-37 is studied as a cancer biology tool rather than a straightforward therapeutic candidate.
LL-37 is synthesized to 99%+ purity, verified by HPLC and Mass Spectrometry. Certificate of Analysis from the manufacturing facility is included with every batch.
Lyophilized LL-37 should be stored at −20°C, protected from moisture and light. Aqueous solutions should be kept at 2-8°C and used within 1 week. LL-37 tends to self-aggregate in solution, particularly at physiological salt concentrations — low-salt buffers are recommended for reconstitution.
For laboratory research use only. Not for human or veterinary use. PeptidesFromChina.co is a B2B wholesale supplier operating under strict research-use-only terms. All products are sold exclusively for in vitro and preclinical research purposes.