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LL-37 5MG
SKU NP-LL37-5MG
$90.00
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LL-37
|
Human Cathelicidin Antimicrobial Peptide
Receptor Target
FPR2 / FPRL1
Peptide Class
Cathelicidin
Research Pathway
Antimicrobial / Immunomodulatory
LL-37 is the sole human cathelicidin, representing the C-terminal 37-residue fragment cleaved from the precursor protein hCAP-18 (human cationic antimicrobial protein 18). The "LL" designation reflects the two N-terminal leucine residues of the mature peptide. LL-37 adopts an amphipathic α-helical conformation in membrane-mimicking environments, carrying a net charge of approximately +6 at physiological pH. It is a widely studied multifunctional research peptide with proposed roles in innate immune defence, immunomodulation, and tissue repair signalling, acting primarily through the formyl peptide receptor 2 (FPR2/FPRL1).
Molecular Profile
| Property | Detail |
|---|---|
| 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 |
| Single-Letter Code | LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES |
| Residue Count | 37 AA; linear; free N- and C-termini |
| Molecular Formula | C₂₀₅H₃₄₀N₆₀O₅₃ |
| Molecular Weight | ~4493 Da |
| CAS Number | 154947-66-7 |
| Also Known As | hCAP-18 C-terminal peptide; CRAMP (murine homologue) |
| Net Charge (pH 7) | ~+6 (cationic; 9 basic residues, 3 acidic) |
| Secondary Structure | Amphipathic α-helix (residues 2–31 in membrane-mimicking conditions) |
| Precursor Protein | hCAP-18 (CAMP gene product); cleaved by kallikrein serine proteases |
| Format | Lyophilized Powder — 5 mg/vial |
| Purity | ≥98% (HPLC) |
Research Targets & Proposed Mechanisms
FPR2 / FPRL1
Primary GPCR target; Gαi-coupled formyl peptide receptor 2. Studied in chemotaxis, neutrophil activation, and pro-resolution signalling research models.
TLR Modulation
Investigated as a modulator of TLR2, TLR4, and TLR9 signalling; studied in innate immune cell models examining cytokine induction and LPS response pathways.
Membrane Disruption
Direct amphipathic helix–membrane interaction studied in antimicrobial mechanism models; proposed toroidal-pore and carpet disruption mechanisms investigated in lipid bilayer assays.
Amphipathic Helix Architecture: LL-37 adopts a random coil in aqueous solution but transitions to an amphipathic α-helix upon interaction with anionic lipid membranes or membrane-mimicking environments (e.g. SDS micelles, DPC). This structural switch is central to its proposed dual role in direct membrane interaction and receptor-mediated signalling studied across research models.
Research Context
- →First characterised from human bone marrow by Agerberth et al. (1995); identified as the only member of the cathelicidin family expressed in humans, distinguishing it from the multiple cathelicidins found in other mammals
- →Expressed by neutrophils, epithelial cells, macrophages, and NK cells; released upon infection or injury — studied as an endogenous component of first-line innate immune defence research models
- →Investigated in wound healing and tissue repair models; proposed to stimulate keratinocyte migration and proliferation via EGFR transactivation, studied in scratch-assay and epithelial barrier research systems
- →Widely used in anti-biofilm research; studied for activity against Gram-positive, Gram-negative, and fungal organisms in membrane permeabilisation and biofilm disruption assays
- →Investigated in immunomodulatory research for proposed roles in angiogenesis, apoptosis regulation, and neutrophil extracellular trap (NET) formation models
Storage & Handling
Store sealed lyophilized material under controlled laboratory conditions in accordance with validated institutional SOPs and applicable technical documentation. Protect from light and moisture.
- →Keep in original sealed vial until use in research protocols
- →LL-37's cationic character means it may adsorb to standard polypropylene surfaces in dilute solution; use low-binding tubes and add carrier protein where appropriate per institutional SOP
- →Handle in accordance with institutional biosafety and chemical handling guidelines
Literature & Resources
- →NexPept — LL-37 Research Peptide Overview: nexpept
- →Agerberth B et al. "FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis." Proc Natl Acad Sci USA, 1995 — PMID 7568028
- →Mookherjee N, Hancock REW. "Cationic host defence (antimicrobial) peptides: immunomodulatory asset?" Cell Mol Life Sci, 2007 — PMID 17558473
- →PubChem Compound — LL-37 (CID 16198951): pubchem.ncbi.nlm.nih.gov
Research Use Only. LL-37 / Human Cathelicidin (CAS 154947-66-7) is supplied exclusively for qualified laboratory and scientific research purposes. This product is not approved for human or veterinary use in Canada, is not a drug or supplement, and has not been evaluated by Health Canada, the FDA, or any regulatory authority for safety or efficacy in any application within this context. No claims are made regarding therapeutic, diagnostic, or preventive properties. Researchers are responsible for ensuring all use complies with applicable institutional, regional, and federal regulations.
All products are intended for laboratory research use only. Not for human or veterinary use.
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Every peptide product sold on our site is lab-tested before it's listed. If a product hasn't been tested, we don't sell it.
Unless otherwise noted on the product page, all NexPept research compounds are supplied as lyophilized (freeze-dried) powder for laboratory research use. Physical form and net quantity are listed individually on each product page.