LL37 (5mg)
$120.00
Description
A single-component research material supplied for controlled research environments. LL-37 is a synthetic cathelicidin-derived peptide used in research exploring innate immunity, antimicrobial pathways, and wound-healing models in controlled systems.
Composition
• LL-37
• Appearance: Lyophilized powder in a sealed research vial
Research Focus (non-clinical)
• Characterization of LL-37 in antimicrobial activity assays
• Studies on immune modulation and inflammatory pathway signaling
• Evaluation in cell culture and tissue models related to epithelial repair
• Stability and solubility profiling under laboratory storage conditions
For qualified research professionals and institutional laboratories. Not for human use.
Documentation & Quality Assurance
Each lot is sourced through our verified global supply chain with emphasis on traceability and quality control.These documents are reviewed internally and displayed as they become available. Independent third-party testing is also performed on select lots to confirm identity, purity, and alignment with our internal specifications.
Important Notice
This product is intended for laboratory research use only. It is not intended for human or veterinary use, and must not be used for diagnostic, therapeutic, or clinical purposes.
This material is not a drug, medical device, or dietary supplement, and has not been evaluated by the U.S. Food and Drug Administration.
Quality & Manufacturing
All materials are sourced from carefully vetted domestic and international manufacturing partners who follow quality systems consistent with ISO and cGMP principles. Each supplier is reviewed for reliability, documentation integrity, and transparency in testing.
We require a verified purity of 99% or higher and perform independent third-party spot testing to confirm that select lots meet our internal standards for identity, purity, and composition. Where available, endotoxin testing results are included on Certificates of Analysis to verify laboratory purity; their inclusion is for research quality assessment only and does not imply suitability for human or veterinary use.
All research materials are sealed for integrity and packaged for stability during storage and transport from manufacturing through final delivery.
Additional information
| Weight | 0.0625 lbs |
|---|
Certificate of Analysis
Every batch undergoes independent third-party laboratory analysis to verify identity, potency, and safety. Testing includes quantitative assay verification, heavy metals screening, and comprehensive microbial analysis.
View Certificate of AnalysisStorage Instructions
All products from Apex Health Performance are manufactured using a lyophilization (freeze-drying) process. This method is designed to maintain product integrity and allows vials to remain stable during shipping for approximately 3–4 months.
Once a vial is reconstituted with bacteriostatic water, it should be stored in the refrigerator to help maintain stability. Under these conditions, reconstituted material is generally considered stable for up to 30 days.
Lyophilization is a dehydration technique in which compounds are frozen and then exposed to low pressure. This causes the water in the vial to sublimate directly from solid to gas, leaving behind a stable, crystalline white structure. This powder can be kept at room temperature until reconstitution.
Upon receipt, products should be stored away from heat and light. For short-term use, refrigeration at approximately 4°C (39°F) is suitable. For long-term storage (several months to years), vials may be placed in a freezer at approximately -80°C (-112°F). Freezing is the preferred method for preserving product stability over extended periods.
⚠️ Important Notice:
These products are intended for research use only. Not for human consumption.
Related products
Research Use Only
The following peer-reviewed publications reference compounds for laboratory and in vitro research purposes only. Not for human or animal use. Not intended to diagnose, treat, cure, or prevent any disease or condition.
Published Scientific Research
Peer-reviewed laboratory studies investigating metabolic research peptides
A sonosensitive diphenylalanine-based broad-spectrum antimicrobial peptide.
The antimicrobial effect of antimicrobial peptides is typically slow; they can be rapidly biodegraded and often have non-selective toxicity and elaborate sequences. Here we report a short peptide that is activated by ultrasound, that shows high broad-spectrum antibacterial efficiency (>99%) against clinically isolated methicillin-resistant bacteria (specifically, Staphylococcus aureus, Escherichia coli, Staphylococcus epidermidis, Enterobacter cancerogenus and Pseudomonas aeruginosa) with 15 m
View Full Study on PubMedAntimicrobial peptide CRAMP/LL-37 mediates ferroptosis resistance in cardiomyocytes by inhibiting cathepsin L.
However, its specific role and mechanism in ferroptosis are unclear. Finally, the regulatory mechanism of CRAMP in ferroptosis was verified in vivo by mouse myocardial infarction model.
View Full Study on PubMedMilk-derived extracellular vesicles functionalized with anti-tumour necrosis factor-α nanobody and anti-microbial peptide alleviate ulcerative colitis in mice.
In mice with chronic UC, simultaneously introducing VHH and an antimicrobial peptide LL37 into EV (EV), then administering orally improved intestinal barrier, inflammation and microbiota balance, resulted in relief of UC-induced depression and anxiety. Collectively, we demonstrated that oral delivery of EV effectively alleviated UC in mice and TAT efficiently loaded biologics into EV to confer protection from degradation in the gastrointestinal tract.
View Full Study on PubMedCathelicidin peptide LL-37: A multifunctional peptide involved in heart disease.
In recent years, LL-37 has been found to have a variety of biological functions, including its role in the regulation of atherosclerosis, thrombosis, inflammatory responses, and cardiac hypertrophy.
View Full Study on PubMedLL-37: Structures, Antimicrobial Activity, and Influence on Amyloid-Related Diseases.
Antimicrobial peptides (AMPs), as well as host defense peptides (HDPs), constitute the first line of defense as part of the innate immune system. Humans are known to express antimicrobial precursor proteins, which are further processed to generate AMPs, including several types of α/β defensins, histatins, and cathelicidin-derived AMPs like LL37. The broad-spectrum activity of AMPs is crucial to defend against infections caused by pathogenic bacteria, viruses, fungi, and parasites. The emergenc
View Full Study on PubMedThe LL-37 domain: A clue to cathelicidin immunomodulatory response?
Other cathelicidins also share structural and functional characteristics with the LL-37 domain, suggesting that these fragments may be responsible for interaction between these peptides and receptors in humans.
View Full Study on PubMedResearch Use Only
The following peer-reviewed publications reference compounds for laboratory and in vitro research purposes only. Not for human or animal use. Not intended to diagnose, treat, cure, or prevent any disease or condition.
Published Scientific Research
Peer-reviewed laboratory studies investigating metabolic research peptides
A sonosensitive diphenylalanine-based broad-spectrum antimicrobial peptide.
The antimicrobial effect of antimicrobial peptides is typically slow; they can be rapidly biodegraded and often have non-selective toxicity and elaborate sequences. Here we report a short peptide that is activated by ultrasound, that shows high broad-spectrum antibacterial efficiency (>99%) against clinically isolated methicillin-resistant bacteria (specifically, Staphylococcus aureus, Escherichia coli, Staphylococcus epidermidis, Enterobacter cancerogenus and Pseudomonas aeruginosa) with 15 m
View Full Study on PubMedAntimicrobial peptide CRAMP/LL-37 mediates ferroptosis resistance in cardiomyocytes by inhibiting cathepsin L.
However, its specific role and mechanism in ferroptosis are unclear. Finally, the regulatory mechanism of CRAMP in ferroptosis was verified in vivo by mouse myocardial infarction model.
View Full Study on PubMedMilk-derived extracellular vesicles functionalized with anti-tumour necrosis factor-α nanobody and anti-microbial peptide alleviate ulcerative colitis in mice.
In mice with chronic UC, simultaneously introducing VHH and an antimicrobial peptide LL37 into EV (EV), then administering orally improved intestinal barrier, inflammation and microbiota balance, resulted in relief of UC-induced depression and anxiety. Collectively, we demonstrated that oral delivery of EV effectively alleviated UC in mice and TAT efficiently loaded biologics into EV to confer protection from degradation in the gastrointestinal tract.
View Full Study on PubMedCathelicidin peptide LL-37: A multifunctional peptide involved in heart disease.
In recent years, LL-37 has been found to have a variety of biological functions, including its role in the regulation of atherosclerosis, thrombosis, inflammatory responses, and cardiac hypertrophy.
View Full Study on PubMedLL-37: Structures, Antimicrobial Activity, and Influence on Amyloid-Related Diseases.
Antimicrobial peptides (AMPs), as well as host defense peptides (HDPs), constitute the first line of defense as part of the innate immune system. Humans are known to express antimicrobial precursor proteins, which are further processed to generate AMPs, including several types of α/β defensins, histatins, and cathelicidin-derived AMPs like LL37. The broad-spectrum activity of AMPs is crucial to defend against infections caused by pathogenic bacteria, viruses, fungi, and parasites. The emergenc
View Full Study on PubMedThe LL-37 domain: A clue to cathelicidin immunomodulatory response?
Other cathelicidins also share structural and functional characteristics with the LL-37 domain, suggesting that these fragments may be responsible for interaction between these peptides and receptors in humans.
View Full Study on PubMedResearch Use Only
The following peer-reviewed publications reference compounds for laboratory and in vitro research purposes only. Not for human or animal use. Not intended to diagnose, treat, cure, or prevent any disease or condition.
Published Scientific Research
Peer-reviewed laboratory studies investigating metabolic research peptides
A sonosensitive diphenylalanine-based broad-spectrum antimicrobial peptide.
The antimicrobial effect of antimicrobial peptides is typically slow; they can be rapidly biodegraded and often have non-selective toxicity and elaborate sequences. Here we report a short peptide that is activated by ultrasound, that shows high broad-spectrum antibacterial efficiency (>99%) against clinically isolated methicillin-resistant bacteria (specifically, Staphylococcus aureus, Escherichia coli, Staphylococcus epidermidis, Enterobacter cancerogenus and Pseudomonas aeruginosa) with 15 m
View Full Study on PubMed →Antimicrobial peptide CRAMP/LL-37 mediates ferroptosis resistance in cardiomyocytes by inhibiting cathepsin L.
However, its specific role and mechanism in ferroptosis are unclear. Finally, the regulatory mechanism of CRAMP in ferroptosis was verified in vivo by mouse myocardial infarction model.
View Full Study on PubMed →Milk-derived extracellular vesicles functionalized with anti-tumour necrosis factor-α nanobody and anti-microbial peptide alleviate ulcerative colitis in mice.
In mice with chronic UC, simultaneously introducing VHH and an antimicrobial peptide LL37 into EV (EV), then administering orally improved intestinal barrier, inflammation and microbiota balance, resulted in relief of UC-induced depression and anxiety. Collectively, we demonstrated that oral delivery of EV effectively alleviated UC in mice and TAT efficiently loaded biologics into EV to confer protection from degradation in the gastrointestinal tract.
View Full Study on PubMed →Cathelicidin peptide LL-37: A multifunctional peptide involved in heart disease.
In recent years, LL-37 has been found to have a variety of biological functions, including its role in the regulation of atherosclerosis, thrombosis, inflammatory responses, and cardiac hypertrophy.
View Full Study on PubMed →LL-37: Structures, Antimicrobial Activity, and Influence on Amyloid-Related Diseases.
Antimicrobial peptides (AMPs), as well as host defense peptides (HDPs), constitute the first line of defense as part of the innate immune system. Humans are known to express antimicrobial precursor proteins, which are further processed to generate AMPs, including several types of α/β defensins, histatins, and cathelicidin-derived AMPs like LL37. The broad-spectrum activity of AMPs is crucial to defend against infections caused by pathogenic bacteria, viruses, fungi, and parasites. The emergenc
View Full Study on PubMed →The LL-37 domain: A clue to cathelicidin immunomodulatory response?
Other cathelicidins also share structural and functional characteristics with the LL-37 domain, suggesting that these fragments may be responsible for interaction between these peptides and receptors in humans.
View Full Study on PubMed →Important Research Notice: These products are research chemicals intended exclusively for in vitro laboratory research by qualified professionals. Not for human or animal consumption. Not approved by the FDA for any therapeutic purpose. Sold strictly for scientific research applications only.