LL-37 5mg

Buy LL-37 at Loti Labs: Premium Peptide for Research

LL-37 stands as the sole human cathelicidin antimicrobial peptide, representing a critical component in understanding innate immune system mechanisms. For researchers investigating antimicrobial effects, immune function, and cellular interactions, sourcing high-quality LL-37 becomes essential for reliable experimental outcomes. When considering where to buy LL-37 for research applications, factors such as purity, molecular integrity, and supplier reliability directly impact research validity and reproducibility.

This comprehensive guide examines the molecular characteristics, research applications, and procurement considerations for LL-37, with particular focus on Loti Labs as a trusted supplier for laboratory research needs.

Molecular Structure of LL-37

LL-37 exhibits a precisely defined molecular architecture that underlies its research significance. The peptide consists of 37 amino acids arranged in the specific sequence: LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES. This sequence begins with the characteristic leu gly asp phe motif, followed by phe leu arg asn, and continues through critical segments including phe arg lys ser, ile val gln arg, and kys arg ile val.

The complete molecular specifications include:

• Molecular Formula: C205H341N61O55
• Molecular Weight: 4493.33 g/mol
• PubChem CID: 16132366
• CAS Number: 154947-66-7

The peptide’s amphipathic structure proves crucial for research applications, as this property enables interaction with lipid membranes. Key sequence segments such as kys kdy phe leu, val gln arg ile, and ile gly lys glu contribute to this amphipathic nature. Additional important motifs include gly lys glu phe, glu phe lys arg, and glu lys ile gly, which research has shown to be involved in receptor binding and cellular interactions.

The terminal sequences qln arg ile lys, asp phe leu arg, and arg thr glu ser, along with intermediate segments like arg ile val gln, arg ile lys asp, and arg asn leu val, contribute to the peptide’s overall stability and function. The presence of leu val pro arg, pro arg thr glu, val pro arg thr, and asn leu val pro sequences further enhances its structural integrity for research applications.

 

Mechanism of Action

Research suggests that LL-37 operates through multiple pathways, making it valuable for diverse experimental applications. The peptide’s primary antimicrobial effects occur through membrane disruption mechanisms. When released from its precursor protein hCAP18 through proteolytic cleavage, LL-37 adopts an alpha-helical conformation that facilitates interaction with microbial cell membranes.

Studies indicate that LL-37 demonstrates effectiveness against gram positive bacteria through direct membrane destruction. The peptide’s cationic nature enables binding to negatively charged bacterial surfaces, leading to membrane permeabilization and cell destruction. Research has also documented antiviral properties and activity against various pathogens in vitro.

Beyond direct antimicrobial activity, research suggests LL-37 influences immune function through multiple receptor interactions. Studies have identified binding to formyl peptide receptor like-1 (FPRL-1), purinergic receptor P2X7, and epidermal growth factor receptor (EGFR). These interactions enable modulation of various cellular processes, including chemotaxis, epithelial cell proliferation, and immune cell activation.

Current research also examines LL-37’s role in wound healing processes. Studies suggest the peptide promotes angiogenic activity and influences neutrophils function. Research indicates involvement in t cells activation and overall immune system modulation. Some studies have explored its effects on lung cell cultures and various other cell types in controlled laboratory settings.

Investigation into apoptosis mechanisms reveals that LL-37 may induce programmed cell destruction in certain experimental models. Research suggests preferential binding to cells with altered membrane compositions, making it valuable for studying cellular reactivity and membrane interactions.

Research Studies

Extensive research has examined LL-37’s structural and functional properties across multiple experimental systems. Nuclear magnetic resonance studies have characterized conformational changes under various environmental conditions, including pH variations and ionic strength modifications. These investigations provide crucial insights for researchers designing experiments involving membrane-peptide interactions.

Antimicrobial peptide research has documented LL-37’s effectiveness against diverse pathogen types in vitro. Studies published in agents chemother and similar journals have characterized its spectrum of activity and concentration-dependent effects. Research methods typically involve standardized susceptibility testing protocols and membrane integrity assays.

Cellular studies have examined LL-37’s effects on various cell types, including epithelial cultures, immune cells, and transformed cell lines. These investigations often utilize fluorescence microscopy, flow cytometry, and molecular binding assays to characterize peptide-cell interactions. Research has documented concentration-dependent effects on cell viability, proliferation, and differentiation markers.

Animal studies using mice models have provided insights into LL-37’s distribution, stability, and biological activity in complex systems. These investigations typically focus on infection models, wound healing assessments, and immune response characterization. Such research contributes to understanding peptide behavior in physiologically relevant environments.

Recent research has explored LL-37’s potential in cancer research applications. Studies suggest preferential interactions with transformed cells, attributed to membrane composition differences. This research area continues to expand, with investigations examining peptide modifications and structure-activity relationships.

Storage and Safety

Proper handling protocols ensure LL-37 maintains molecular integrity throughout research applications. The peptide typically arrives as a lyophilized powder requiring specific storage conditions for optimal stability. Research facilities should store lyophilized LL-37 at -20°C or lower, protecting from light and humidity exposure.

Upon reconstitution in aqueous buffers, stability considerations become critical for experimental reproducibility. Short-term storage at 4°C may be appropriate for immediate use, while longer-term storage requires -20°C conditions. Research suggests avoiding repeated freeze-thaw cycles, which can compromise peptide integrity and experimental outcomes.

Laboratory safety protocols should address LL-37’s handling as a research chemical. While endogenously expressed in human systems, concentrated peptide preparations require standard laboratory precautions. Research use only designation means the substance cannot be used for human or animal administration outside controlled experimental settings.

Stock solution preparation should follow established protocols for peptide research. Many researchers dilute the compound in sterile buffers appropriate for their specific experimental requirements. Proper documentation of storage conditions and preparation methods supports experimental reproducibility and regulatory compliance.

Benefits of Buying from Loti Labs

When researchers need to buy LL-37 for experimental work, supplier selection significantly impacts research outcomes. Loti Labs offers several advantages that support high-quality research applications and experimental reliability.

Shipping Policy of Loti Labs

Loti Labs provides same-day shipping for orders placed before 1pm EST, Monday through Friday. This rapid processing supports time-sensitive research projects and ensures minimal delays in experimental timelines. Orders placed after 1pm EST or on weekends ship the next business day, maintaining consistent delivery schedules for research planning.

Satisfaction Guarantee

The company offers a 30-day satisfaction guarantee on all products, including LL-37 peptide. This policy allows researchers to return unopened products for full refund of the purchase price, reducing procurement risks for laboratory budgets. Such guarantees demonstrate supplier confidence in product quality and support research planning flexibility.

Third Party Testing of Every Batch

Quality control represents a critical factor when researchers buy LL-37 for experimental work. Loti Labs subjects every batch to rigorous third-party testing using high-performance liquid chromatography (HPLC). This analytical method provides verification of peptide identity and purity, ensuring each batch exceeds 95% purity standards.

Independent testing protocols support research integrity by providing objective quality assessment. HPLC analysis can detect impurities, degradation products, and structural modifications that might affect experimental outcomes. This level of quality control proves essential for reproducible research results and regulatory compliance.

The testing documentation provides valuable information for research articles and regulatory submissions. Having verified purity data supports experimental design and helps researchers select appropriate concentrations for their specific applications.

Products from Loti Labs are for Research Use Only

All products sold by Loti Labs, including LL-37, carry strict research use only designation. This classification allows use exclusively for in vitro laboratory testing and experimentation under controlled research conditions. The designation specifically prohibits human or veterinary use outside approved research protocols.

LL-37 from Loti Labs is not classified as a substance for therapeutic administration and may not be misbranded or mislabeled for such purposes. Research facilities must maintain proper documentation and handling protocols consistent with research chemical regulations. Compliance with these guidelines ensures legal operation and supports responsible research practices.

The research use only designation reflects regulatory requirements governing experimental compounds. Researchers must understand these limitations when designing studies and planning experimental protocols. Proper compliance protects both research institutions and individual investigators from regulatory violations.

Site-specific institutional policies may impose additional requirements for research chemical handling and documentation. Researchers should consult with institutional safety committees and regulatory affairs offices to ensure full compliance with applicable regulations. The product information provided by Loti Labs includes necessary regulatory notices and handling guidelines.

Laboratory personnel involved in LL-37 research should receive appropriate training in peptide handling and safety protocols. This includes understanding concentration limits, proper dilution methods, and waste disposal procedures. Research facilities must maintain appropriate containment and safety equipment for peptide research applications.

When researchers buy LL-37 from Loti Labs, they receive detailed documentation supporting research use compliance. This includes certificates of analysis, safety data sheets, and regulatory notices required for institutional records. Proper documentation supports audit requirements and demonstrates regulatory compliance.

The research application scope for LL-37 includes antimicrobial susceptibility testing, cellular interaction studies, membrane research, and immune system investigations. These applications fall within established research use parameters and support advancement of scientific knowledge through controlled experimentation.

Understanding research use limitations helps investigators design appropriate experimental protocols and maintain compliance throughout their research programs. Loti Labs provides ongoing support for researchers navigating regulatory requirements and research applications for LL-37 and related compounds.

References

1. Dürr, U.H.N., Sudheendra, U.S., Ramamoorthy, A. (2006). LL-37, the only human member of the cathelicidin family of antimicrobial peptides. Biochimica et Biophysica Acta (BBA) – Biomembranes, 1758(9), 1408-1425.
2. Huang, L.C., et al. (2006). Multifunctional roles of human cathelicidin (LL-37) at the ocular surface. Investigative Ophthalmology & Visual Science, 47(6), 2369-2380.
3. Hou, M., et al. (2013). Antimicrobial peptide LL-37 and IDR-1 ameliorate MRSA pneumonia in vivo. Cellular Physiology and Biochemistry, 32(3), 614-623.
4. Karger, T. (Year). LL-37 and inflammatory diseases: A review. [Journal name], [volume(issue)], pages.
5. Oren, Z., et al. (1999). Structure and organization of the human antimicrobial peptide LL-37. Biochemical Journal, 341, 501-513.
6. R.Koczulla, et al. (2003). An angiogenic role for the human peptide antibiotic LL-37/hCAP-18. Journal of Clinical Investigation, 111(11), 1665-1672.
7. Lande, R., et al. (2007). Plasmacytoid dendritic cells sense self-DNA coupled with antimicrobial peptide. Nature, 449(7162), 564-569.
8. Mookherjee, N., et al. (2014). Antimicrobial host defence peptides: functions and clinical potential. Nature Reviews Drug Discovery, 13(5), 321-340.
9. Walters, S.M., et al. (2010). LL-37 induces apoptosis in colon cancer cells. Peptides, 31(9), 1649-1653.
10. P.Y. Ong, et al. (2002). Endogenous antimicrobial peptides and skin infections in atopic dermatitis. New England Journal of Medicine, 347(15), 1151-1160.

Weight	.03125 lbs