What is LL-37 (5mg)?
LL-37 is a premier cathelicidin-derived antimicrobial peptide (AMP) that has captured the attention of the global scientific community. Consisting of a 37-amino acid sequence, LL-37 is the only known functional peptide from the cathelicidin family found in humans. It plays a monumental role in innate immunity, tissue regeneration, and inflammatory modulation.
Our LL-37 (5mg) lyophilized powder is synthesized to the highest industry standards, boasting a purity level of >98%. This ensures that your laboratory evaluations yield precise, reproducible, and verifiable results every time. Whether you are investigating its potent antimicrobial mechanisms or its intricate role in wound healing pathways, our LL-37 peptide delivers the uncompromising quality your research demands.
Key Biochemical Mechanisms & Applications
1. Advanced Antimicrobial and Antibacterial Efficacy
LL-37 is widely celebrated for its broad-spectrum antimicrobial properties. Unlike traditional agents, LL-37 interacts directly with the lipid bilayers of microbial cell membranes.
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Membrane Disruption: It utilizes an electrostatic attraction to bind to bacterial membranes, causing permeabilization and subsequent lysis.
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Biofilm Eradication: Research indicates that LL-37 can inhibit the formation of, and actively disrupt, existing microbial biofilms, making it a critical subject in the fight against antibiotic-resistant strains.
2. Accelerated Wound Healing and Tissue Repair
In vivo and in vitro studies suggest that LL-37 acts as a potent chemoattractant. It recruits essential immune cells, such as neutrophils and T-lymphocytes, to the site of cellular injury. Furthermore, it stimulates angiogenesis (the formation of new blood vessels) and promotes epithelial cell proliferation, marking it as a revolutionary compound in regenerative medicine research.
3. Immunomodulation and Inflammatory Response
Beyond directly neutralizing pathogens, LL-37 serves as a sophisticated immunomodulator. It balances the host immune response by interacting with formyl peptide receptor-like 1 (FPRL1) and purinergic receptors. This dual-action capability allows it to either upregulate or downregulate inflammatory cytokines depending on the cellular microenvironment, offering rich avenues for autoimmune and chronic inflammation research.
Why Choose Our LL-37 5mg Peptide?
When conducting high-stakes biochemical analysis, the integrity of your compounds cannot be compromised. Our LL-37 is engineered for researchers who refuse to settle for subpar data.
Uncompromising Quality Assurance
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Ultra-High Purity: Every batch is verified via HPLC (High-Performance Liquid Chromatography) and Mass Spectrometry to guarantee a purity profile exceeding 98%.
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Maximum Stability: Lyophilized and sealed in a sterile, temperature-controlled environment to ensure long-term stability and resistance to degradation.
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Precise Dosing: Each vial contains exactly 5mg of active LL-37 peptide, allowing for effortless reconstitution and accurate dilution calculations.
Reconstitution and Storage Guidelines
Note: This product is intended strictly for laboratory research and in vitro evaluation. It is not for human consumption or therapeutic use.
Reconstitution Protocols
To preserve the structural integrity of the LL-37 alpha-helical conformation, it is recommended to reconstitute the lyophilized powder using sterile bacteriostatic water or a mild buffer solution. Gently swirl the vial—do not shake vigorously—until the lyophilizate is fully dissolved.
Storage Best Practices
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Lyophilized Powder: Store at -20°C for up to 24 months.
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Reconstituted Solution: Store at 2°C to 8°C for immediate use (up to 7 days), or aliquot and freeze at -80°C to avoid repeated freeze-thaw cycles.
Product Specifications
| Attribute | Specification |
| Peptide Name | LL-37 |
| Alternative Names | Cathelicidin, CAMP, CAP-18 |
| Molecular Formula | $C_{205}H_{340}N_{60}O_{53}$ |
| Molecular Weight | 4493.3 g/mol |
| Sequence | LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES |
| Purity | >98% (HPLC verified) |
| Format | Lyophilized White Powder |












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