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LL-37

LL-37

Base Peptides are intended for licensed medical professionals and experienced researchers. Reconstitution required. Dosing and use instructions are not provided.

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$50.00
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LL-37 — Human Cathelicidin Antimicrobial Peptide (37 aa)

LL-37 is the active, 37-amino-acid fragment released from the human cathelicidin precursor hCAP-18. Researchers use LL-37 to study innate immune defense, epithelial repair, and host–pathogen interactions in vitro and in vivo.

Identifiers
  • CAS: 154947-66-7
  • PubChem CID: 16198951
  • Formula / MW: C205H340N60O53 · ≈ 4493 Da
  • Sequence (human): LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES
  • Origin: C-terminal peptide generated from hCAP-18 (CAMP gene) by proteolytic processing
How It Works (Plain English)
  • Amphipathic helix: LL-37 forms a curved α-helix that can interact with and disrupt microbial membranes, a classic innate-defense mechanism.
  • Immunomodulation: Beyond direct microbe effects, LL-37 can tune pattern-recognition pathways and inflammatory signaling in host cells.
  • Tissue context: It’s studied in epithelial models (skin, airway) for roles in wound repair and barrier defense.
Why Researchers Use It
  • To map host–pathogen interactions and membrane-active peptide biology.
  • To examine immune signaling (chemotaxis, cytokine modulation) in epithelial and myeloid cells.
  • To explore repair and angiogenic markers in wound-healing models.

Key Studies — What Was Tested, What Changed, Why It Matters

Host defense & membrane interaction
  • What was tested: Structure and membrane binding of LL-37 in model membranes and micelles.
  • What changed: A helix–bend–helix topology spanning residues ~2–31 promotes amphipathic surface binding and membrane disruption. )
  • Why it matters: Explains how LL-37 combines direct antimicrobial activity with signaling at host membranes.
Immunomodulation in epithelial/myeloid cells
  • What was tested: TLR-linked pathways and cytokine readouts after LL-37 exposure.
  • What changed: Context-dependent tuning of inflammatory responses (e.g., TLR2/4) and chemotaxis.
  • Why it matters: Positions LL-37 as more than an antimicrobial—it's a host-response coordinator.
Wound repair / angiogenesis context
  • What was tested: Epithelial wound models and corneal/skin systems.
  • What changed: Signals consistent with barrier repair, epithelial migration, and pro-angiogenic activity. [oai_citation:12‡Anaspec]
  • Why it matters: Supports use of LL-37 in epithelial defense and healing research designs.

Potential Research Applications

Innate Immunity

  • Host–pathogen interaction assays
  • TLR signaling & chemotaxis panels

Barrier & Wound Models

  • Epithelial migration and re-epithelialization
  • Angiogenic and matrix-remodeling markers

Peptide Mechanism

  • Helix formation, membrane binding, and peptide–lipid interactions
  • Salt/form comparisons (e.g., trifluoroacetate vs acetate)

Synergistic Peptides (for Study Design)

BPC-157

  • Why pair: Often used in epithelial repair models; complements LL-37’s barrier-defense role.
  • Angle: Co-culture migration + cytokine endpoints.

TB-500 (Thymosin-β4 fragment)

  • Why pair: Cell motility/cytoskeleton focus useful alongside antimicrobial/immune signaling.
  • Angle: Matrix and angiogenic markers with wound-closure assays.

Tα1 (Thymosin-α1)

  • Why pair: Innate→adaptive immune coordination; contrast with LL-37’s epithelial/innate emphasis.
  • Angle: Th1/Th2 cytokine profiling with epithelial barrier metrics.

Design Notes

  • Report salt form (e.g., TFA vs acetate) and vehicle; these can affect cell responses.
  • Include dose–response and time-course sampling—LL-37’s effects are context-dependent.
  • Use standardized serum/media to reduce cytokine baseline noise.

Known Concerns (Context)

  • Concentration effects: At higher μM ranges, LL-37 can be cytotoxic to mammalian cells in some models—plan viability controls.
  • Assay variability: Outcomes depend on ionic strength, serum, and lipid composition; document conditions carefully.
  • General: Research use only; not for human consumption or therapeutic use.

Specifications & Handling

  • Form: Lyophilized powder (lot-coded)
  • Purity: ≥ 99% (HPLC/MS verified)
  • Storage: ≤ −20 °C; protect from light/moisture
  • In solution: Aliquot promptly; avoid repeat freeze–thaw
  • Additives: None unless specified per lot
  • Packaging: Tamper-evident; research-only labeling

Regulatory & Use Notice

Sold for laboratory research use only. Not for human consumption, medical, or veterinary use. No human-use instructions are provided. Buyer is responsible for safe handling and regulatory compliance.

LL-37 Peptide Research | Human Cathelicidin (hCAP-18 Derived) | Innate Immunity, Epithelial Repair & Host–Pathogen Studies

Keywords: LL-37 peptide, cathelicidin, hCAP-18, CAMP gene, antimicrobial peptide, epithelial wound healing, TLR signaling, Base Peptides.

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Instructions are NOT provided before or after purchase.

Peptide molecules are unfinished and require reconstitution from a skilled and licensed professional to activate the compound into liquid form. Instructions are not provided for reconstitution, dosing, or adminstration. All products are strictly intended for research purposes and laboratory experimentation. Handling should be by skilled licensed and credentialed professionals only. Non experimental use is strictly prohibited.
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