Cellular Repair & Recovery
LL-37
Cathelicidin antimicrobial peptide
LL-37 (Cathelicidin antimicrobial peptide)
Research context
LL-37 is the active C-terminal fragment released from human cathelicidin hCAP-18. Research examines membrane permeabilisation in bacterial models, formyl peptide receptor engagement, and chemotactic activity in immune cell preparations.
Common assays: Minimum inhibitory concentration · Membrane permeabilisation · FPRL1 receptor binding · Chemotaxis
Specification
| Designation | Cathelicidin antimicrobial peptide |
|---|---|
| Full name | LL-37 (Cathelicidin antimicrobial peptide) |
| 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 |
| Molecular formula | C205H340N60O53 |
| Molecular weight | 4493.26 g/mol |
| Formats | 10 mL Vial |
| Solubility | Sterile water; low-binding tubes recommended |
| Storage | Lyophilised: −20 °C, desiccated. Reconstituted: 2–8 °C. |
Published literature
Selected peer-reviewed references describing research involving this compound. Listed for reference only; inclusion is not a claim about any outcome.
- Dürr UH, Sudheendra US, Ramamoorthy A.LL-37, the only human member of the cathelicidin family of antimicrobial peptidesBiochimica et Biophysica Acta · 2006 Find on PubMed ↗
Common questions
Why are low-binding tubes recommended for LL-37?
It is a highly cationic amphipathic peptide that adsorbs readily to standard plastic and glass surfaces, producing real concentration losses in dilute solutions.
What is LL-37 derived from?
The C-terminus of hCAP-18, the only cathelicidin identified in humans. Proteolytic cleavage releases the active 37-residue peptide.
Same pathway
Related compounds
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TB-500
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A synthetic fragment corresponding to the actin-binding domain of thymosin beta-4.
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Peptide blend
A prepared blend of the two most extensively studied compounds in the repair signalling literature.