PX1 Research provides fast shipping on high-purity LL-37 peptide for qualified laboratory research applications. Orders placed Monday through Friday before 3 PM PST dispatch same-day from our dual fulfillment centers in California and Arizona to prevent project downtime.
PX1 Research provides fast shipping on high-purity LL-37 peptide for qualified laboratory research applications. Orders placed Monday through Friday before 3 PM PST dispatch same-day from our dual fulfillment centers in California and Arizona to prevent project downtime.
Fast shipping for LL-37 is critical for maintaining research timelines and preserving reagent integrity in laboratory settings. PX1 Research dispatches high-purity, lyophilized LL-37 (human cathelicidin) same-day for orders placed by 3 PM PST, Monday through Friday. Shipped directly from strategic facilities in California and Arizona, every lot arrives rapidly with complete analytical documentation.
When managing active experimental series in cellular biology, microbiology, or immunology, unexpected reagent depletion can interrupt ongoing assays. By maintaining robust domestic stock and direct regional dispatch, PX1 Research eliminates long lead times associated with overseas suppliers or third-party drop-shippers. Qualified investigators can order LL-37 for laboratory research with full confidence in rapid transit and verified lot consistency.
LL-37 is the sole human representative of the cathelicidin family of host-defense peptides. Composed of 37 amino acid residues (sequence: LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES), it features a overall net positive charge (+6 at physiological pH) and adopts an amphipathic alpha-helical secondary structure upon interaction with lipid membranes.
In nature, LL-37 is cleaved from the C-terminus of the human cationic antimicrobial protein 18 (hCAP18) precursor protein by extracellular proteases such as proteinase 3. Researchers studying innate immune mechanisms evaluate LL-37 due to its dual functional capacity: direct disruption of lipid bilayers and selective interaction with host cell surface receptors, such as Formyl Peptide Receptor 2 (FPR2/ALX). To explore broader peptide classifications, review our research library hub covering host-defense and structural peptide architectures.
In vitro models demonstrate that LL-37 executes antimicrobial mechanism-of-action studies through electrostatic attraction to negatively charged microbial membrane components, such as lipopolysaccharides (LPS) in Gram-negative bacteria and teichoic acids in Gram-positive bacteria. Following initial surface binding, the amphipathic alpha-helix inserts into the lipid bilayer, leading to membrane destabilization, pore formation, and loss of transmembrane potential.
Beyond direct membrane disruption, preclinical assays show that LL-37 binds free LPS, effectively neutralizing endotoxin-induced signaling cascades in macrophage culture assays. This dual action makes LL-37 a focal compound in studies evaluating host-pathogen interactions, inflammatory signaling pathways, and membrane dynamics across various research peptides evaluated in preclinical settings.
Biofilm formation presents a significant challenge in microbiological and bio-materials research. In vitro studies indicate that LL-37 inhibits bacterial biofilm formation and destabilizes established mature biofilms produced by pathogens such as Pseudomonas aeruginosa and Staphylococcus aureus. The mechanism involves downregulating genes associated with flagellar assembly and quorum sensing, thereby preventing bacterial attachment and matrix development.
In preclinical wound-environment models, researchers examine how LL-37 influences cell migration, angiogenesis, and tissue remodeling signals. In vitro culture assays demonstrate that LL-37 stimulates keratinocyte and endothelial cell migration via transactivation of the epidermal growth factor receptor (EGFR) and activation of the FPR2/ALX pathway. Further detailed documentation on cathelicidin mechanisms is cataloged in our dedicated cathelicidin LL-37 research guide.
Within preclinical investigation, LL-37 is frequently evaluated alongside other regulatory and host-defense compounds to compare membrane interaction kinetics, receptor binding affinities, and cellular signaling responses. Understanding the operational differences between these molecules allows investigators to select the precise peptide profile required for their experimental models.
For instance, while LL-37 relies primarily on amphipathic helical pore formation and FPR2 receptor signaling, compounds like Thymosin Beta-4 act primarily through actin-sequestering mechanisms to promote cell migration and tissue architecture. Similarly, BPC-157 is investigated for cytoprotective growth factor signaling in gastrointestinal and musculoskeletal tissue models, whereas peptides like Melittin exhibit aggressive, non-selective membrane-lytic behavior compared to the regulated host-defense signaling observed with cathelicidins.
Assay reproducibility depends entirely on peptide purity and structural integrity. PX1 Research subjects every lot of LL-37 to comprehensive third-party testing in ISO 17025 accredited analytical laboratories. Our quality standards ensure that research compounds meet strict chemical specifications prior to distribution.
Verification procedures include High-Performance Liquid Chromatography (RP-HPLC) to confirm peptide purity exceeding 98%, and Electrospray Ionization Mass Spectrometry (ESI-MS) to verify precise molecular mass (4493.3 Da). Additionally, because LL-37 is frequently utilized in cell culture and immunological assays, every lot undergoes Chromogenic LAL testing to verify endotoxin levels remain below strict threshold limits (<0.01 EU/mg). Institutions requiring continuous analytical traceability can reference sample data via our wholesale accounts portal.
Proper handling and reconstitution protocols are essential to preserve the secondary structure and solubility of LL-37 in vitro. High-purity LL-37 is supplied as a lyophilized (freeze-dried) powder under inert gas flushing to maximize shelf stability.
For initial reconstitution, laboratory protocols typically specify sterile, deionized water or low-salt aqueous buffers such as 0.01% acetic acid to prevent aggregation. Once dissolved, working solutions may be diluted into phosphate-buffered saline (PBS) or culture media immediately prior to assay execution. Stock solutions should be aliquoted into polypropylene microcentrifuge tubes to prevent hydrophobic adsorption to glass walls, and stored at -20°C or -80°C to avoid freeze-thaw degradation.
Logistical delays can compromise thermal stability and disrupt experimental schedules. PX1 Research operates dual fulfillment nodes located in California and Arizona. This geographic footprint enables rapid ground and air freight handling across North America.
All LL-37 shipments are packed in heavy-duty, temperature-resilient packaging engineered to protect lyophilized peptides from light, moisture, and extreme ambient temperature fluctuations during transit. Automated tracking provides real-time oversight from dispatch to laboratory delivery.
PX1 Research caters to academic institutions, biotechnology enterprises, and contract research organizations (CROs) requiring reliable, bulk-quantity peptide supply. We maintain consistent inventory lots to support long-term, multi-phase longitudinal studies without batch-to-batch variation.
Institutional accounts benefit from dedicated account management, bulk pricing tiers, and direct access to full batch analytical certificates (COAs). Qualified procurement departments can submit inquiries through our wholesale program to coordinate custom lot reservations and scheduled delivery arrangements.
What is the standard shipping timeframe for LL-37 from PX1 Research?
Orders placed before 3 PM PST Monday through Friday ship same-day from our California or Arizona facilities. Expedited shipping options ensure arrival within 1 to 3 business days depending on destination.
How is the purity of LL-37 verified?
Every lot of LL-37 undergoes third-party ISO 17025 laboratory testing. Purity is verified to be ≥98% using Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC), and identity is confirmed via Mass Spectrometry (MS).
What is the molecular weight and sequence of research-grade LL-37?
LL-37 has a molecular weight of approximately 4493.3 Da and consists of 37 amino acid residues with the sequence: LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES.
What solvent is recommended for reconstituting LL-37 in laboratory settings?
Lyophilized LL-37 is typically reconstituted using sterile bacteriostatic water or dilute 0.01% acetic acid to maintain solubility. Dilution into physiological buffers like PBS should occur immediately prior to experimental assays to prevent aggregation.
What are the endotoxin specifications for PX1 Research LL-37?
LL-37 lots undergo Limulus Amebocyte Lysate (LAL) testing to confirm low endotoxin levels, typically measuring under 0.01 EU/mg, making it suitable for sensitive in vitro immunological models.
How should lyophilized and reconstituted LL-37 be stored?
Lyophilized LL-37 should be stored at -20°C upon receipt. Reconstituted stock solutions should be aliquoted into low-binding polypropylene tubes and stored at -80°C to minimize degradation and avoid repeated freeze-thaw cycles.
How does LL-37 differ structurally from other antimicrobial peptides like Melittin?
While both form alpha-helices, LL-37 is a 37-residue human cathelicidin with specific host-receptor signaling properties (such as FPR2 interaction), whereas Melittin is a 26-residue bee venom peptide with aggressive, non-selective cell membrane lytic activity.
Can institutions purchase LL-37 in bulk or custom lot sizes?
Yes, PX1 Research offers bulk ordering and reserved single-lot fulfillment for academic, corporate, and institutional laboratories through our wholesale account program.
All products are sold strictly for laboratory and research use only. Not for human or veterinary use, diagnosis, treatment or consumption. Statements have not been evaluated by the FDA.