LL-37 5mg Research Peptide Canada

High‑Purity Antimicrobial Peptide for Innate Immunity & Cellular Signaling Research (Canada)

LL‑37 is a synthetic research peptide derived from the human cathelicidin antimicrobial peptide family, widely studied in laboratory settings for its role in innate immune responses, host‑defense mechanisms, and cell‑signaling pathways. It is commonly referenced in experimental models involving peptide–membrane interactions, inflammatory signaling pathways, and microbial response systems.

Supplied by BlueNexLabs, LL‑37 is provided as a high‑purity, lyophilized research peptide with COA‑verified analytical consistency and audit‑safe Research‑Use‑Only (RUO) labeling, supporting advanced experimental workflows across Canadian research laboratories.

LL‑37 is frequently utilized in controlled laboratory environments to explore peptide‑mediated signaling and host‑defense mechanisms.

In research settings, LL‑37 is commonly referenced in studies examining:

• Innate immune response signaling pathways
• Antimicrobial peptide interactions with membranes
• Cellular signaling modulation and pathway activation
• Inflammatory response models and signaling cascades
• Host–pathogen interaction frameworks

Its broad signaling profile supports multi-system analysis in controlled experimental designs.

LL‑37 is a synthetic analog of a naturally occurring human antimicrobial peptide, designed for laboratory studies involving:

• Innate immune system signaling
• Peptide–cell membrane interactions
• Cellular communication and signaling pathways

Its structure enables researchers to investigate peptide function within complex biological systems under controlled conditions.

In research contexts, LL‑37 supports studies involving:

• Signal transduction and pathway activation
• Peptide‑mediated cellular responses
• Interaction between peptides and microbial structures
• Regulatory signaling within immune‑associated pathways

🔵 Innate Immune Signaling

• Referenced in studies involving host‑defense peptide activity
• Used in models examining immune‑associated signaling pathways
• Supports investigation of intracellular signaling cascades

🟠 Peptide–Membrane Interaction Studies

• Applied in research examining peptide binding to lipid membranes
• Supports structural and functional interaction modeling
• Used in membrane‑permeability and signaling studies

🟣 Inflammatory Signaling Models

• Examined in studies involving pathway‑level signaling responses
• Supports analysis of signaling modulation mechanisms
• Used in comparative inflammatory pathway models

🔗 Host–Pathogen Interaction Research

• Enables investigation of peptide responses in microbial systems
• Supports modeling of interaction dynamics
• Used in studies of peptide‑mediated signaling behavior

Type: Synthetic antimicrobial peptide

Form: Lyophilized powder

Purity: ≥99%

Identity Verification: Mass Spectrometry (MS)

Purity Analysis: HPLC / UPLC

Structural & Biochemical Notes

• Derived from human cathelicidin peptide sequence
• Demonstrates consistent analytical performance in laboratory workflows
• Suitable for signaling and membrane interaction studies
• Sensitive to degradation depending on storage and handling conditions

LL‑37 is widely referenced in laboratory research involving:

• Innate immune signaling pathway analysis
• Peptide‑membrane interaction studies
• Host–pathogen interaction modeling
• Inflammatory signaling pathway research
• Structure–function analysis of antimicrobial peptides

Its versatility supports a wide range of controlled experimental applications in regulated research environments.

• Store lyophilized LL-37 at –20 °C, protected from light and moisture
• Reconstituted solutions: 2–8 °C, short-term laboratory use only
• Avoid repeated freeze–thaw cycles; use sterile technique

Batch Certificates of Analysis are listed in the certificates library when published. Match vial size and lot notes before assigning a lot to an assay.

Research-use only. Not for human or veterinary use. No medical, cosmetic, or performance claims are made or implied.