Royal Peptides products are offered exclusively for laboratory research, analytical, and scientific applications. Not for human or veterinary use.
01Research Product Information
Royal Peptides supplies compounds intended for controlled laboratory research and analytical applications.
- For research and analytical use only
- Not intended for human consumption or administration
- Not intended for veterinary use
- Not represented as a drug, medicine, or therapeutic product
- Laboratory researchers are responsible for appropriate protocols and controls
02Lyophilized Product Format
Where applicable, Royal Peptides research materials are supplied in lyophilized form.
Lyophilization is a freeze-drying process used to remove moisture from material under controlled conditions.
- Material appearance may differ between compounds and production lots
- Lyophilized material may appear as a cake, film, or fragmented material
- The quantity of visible material may appear small relative to vial size
- Visual appearance alone does not establish identity or purity
03Storage & Laboratory Handling
Storage requirements may vary by compound, formulation, and production lot. Refer to the product label and available product-specific documentation.
- Protect research materials from excessive heat
- Limit unnecessary exposure to direct light and moisture
- Keep containers securely closed when stored
- Follow product-specific temperature requirements when provided
- Use appropriate laboratory contamination-control procedures
04Packaging & Quality Documentation
Packaging components may vary slightly between production lots. This can include vial closures, cap styles, label positioning, and external packaging.
- Check the product label and lot identifier before laboratory use
- Inspect the vial and closure for visible shipping damage
- Packaging design may differ between batches
- Lot-specific analytical documentation may be available in our COA library
LL-37 Kit
LL-37 – LL-37 Peptide 5mg — Cathelicidin Research Dossier
LL-37 ships from U.S. stock at Royal Peptides – Cathelicidin Antimicrobial Kit, with a lot-matched COA. LL-37 is the only human cathelicidin and a key part of innate immune defence, which is why it appears in antimicrobial and wound-model research next to kpv peptide.
LL-37 peptide is a naturally occurring 37-amino-acid human cathelicidin-derived peptide
extensively investigated in innate immunity, antimicrobial activity,
Not for human or veterinary use, administration, ingestion, injection, compounding, diagnostic, therapeutic, clinical, or personal use.

Buy LL-37 Online
Pick your strength with the selector at the top of this page and add LL-37 to your cart. Prices are per vial or per kit as shown, and every order ships with lot documentation.
Need larger quantities of LL-37? Kits and wholesale boxes lower the unit price; see our bulk research peptides options.
What Is LL-37 Peptide?
antimicrobial peptide. It is generated through proteolytic processing
of the human cathelicidin precursor protein hCAP18, which is encoded by the CAMP gene.
The name LL-37 refers to two defining structural characteristics:
(LL) and consists of 37 amino-acid residues.
LL-37 has attracted substantial research interest because its
biological activity extends beyond direct interactions with
microorganisms. Experimental studies have examined its involvement
chemotaxis, membrane biology and tissue-response pathways.
LL-37 Amino-Acid Sequence and Structure
LL-37 is a cationic peptide containing 37 amino-acid residues.
Its positive charge and amphipathic characteristics are important
areas of research because they influence interactions between the
peptide and biological membranes.
In membrane-associated environments, LL-37 can adopt an alpha-helical conformation. Researchers have
investigated how this structural behavior contributes to
peptide-membrane interactions and other biological functions.
LL-37, hCAP18 and the CAMP Gene
LL-37 does not initially exist as an isolated 37-residue peptide
inside human cells. It originates from the larger precursor protein human cationic antimicrobial protein 18 (hCAP18).
processing releases the C-terminal LL-37 sequence from the precursor,
producing the mature peptide studied extensively in innate-immunity
research.
Encodes the human cathelicidin antimicrobial peptide precursor. hCAP18
Precursor protein from which mature LL-37 can be released. LL-37
37-residue mature peptide investigated across innate immune and
antimicrobial research.
LL-37 Antimicrobial Peptide Research
LL-37 is widely classified as an antimicrobial peptide (AMP). A major area of
laboratory research involves its interaction with microbial
membranes.
Because LL-37 is both cationic and amphipathic, investigators have
examined how electrostatic and hydrophobic interactions influence
its association with lipid membranes.
Experimental studies have evaluated LL-37 against numerous
microorganisms under controlled laboratory conditions, including
models involving Gram-positive bacteria, Gram-negative
bacteria and fungal organisms.
Antimicrobial activity observed in laboratory experiments does not
mean LL-37 is an approved antimicrobial drug or treatment for an
infection.
LL-37 and Biofilm Research
of antimicrobial-peptide investigation.
Biofilms are structured microbial communities in which cells exist
within a self-produced extracellular matrix. Their biology differs
considerably from freely suspended microbial cells, making biofilms
an important model for studying microbial organization, signaling
and environmental persistence.
Researchers have examined LL-37 in experimental biofilm systems to
investigate effects on processes such as surface attachment, microbial communication, biofilm
development and membrane-associated activity.
These studies help researchers better understand the broader role
antimicrobial peptides may play in host-microbe interactions.
LL-37 and Innate Immunity Research
LL-37 is an important research target in innate immunity, the collection of rapid biological
defense mechanisms that respond to environmental and microbial
signals.
Human cells associated with barrier tissues and immune responses can
express cathelicidin-related molecules. This has led researchers to
investigate LL-37 not simply as an antimicrobial peptide, but as a
signaling molecule operating at the intersection of host defense, inflammation and cellular communication.
LL-37 is studied as part of the endogenous peptide systems
associated with early innate immune responses.
Experimental research has examined interactions between LL-37
and signaling pathways involved in immune-cell recruitment and
cellular communication.
LL-37 and Immunomodulatory Signaling
One reason LL-37 remains an active research subject is that its
biological behavior appears more complex than simple direct
antimicrobial activity.
Experimental research has examined interactions involving chemotactic signaling, cytokine-associated pathways,
immune-cell recruitment and receptor-mediated cellular
communication.
These observations have contributed to LL-37 being studied as an immunomodulatory peptide as well as an antimicrobial
peptide.
Innate Immunity
Cathelicidin
CAMP
hCAP18
Chemotaxis
Cell Signaling
LL-37 and Inflammation Research
signaling is complex and context dependent.
Researchers have investigated LL-37 in models examining inflammatory
mediators, immune-cell behavior, cellular stress and interactions
between innate immune signaling pathways.
Depending on the experimental system, concentration, cellular
environment and other variables, LL-37-associated responses may
differ substantially. This makes the peptide particularly useful for
mechanistic research into the regulation of inflammatory biology.
LL-37 and Tissue-Response Research
LL-37 has also been investigated in experimental models involving epithelial biology, keratinocytes, fibroblasts, endothelial
cells and tissue-response signaling.
Laboratory studies have examined processes associated with cellular
migration, barrier biology, angiogenic signaling and communication
between immune and structural cells.
This area of research is often discussed in relation to
wound-response biology. Such research describes experimental
mechanisms and should not be interpreted as evidence that an LL-37
research product heals wounds or treats tissue injuries.
LL-37 Research Areas
Laboratory investigation of LL-37 interactions with microbial
membranes and antimicrobial peptide mechanisms.
Research involving microbial attachment, biofilm development
and peptide interactions with structured microbial communities.
Investigation of LL-37 within endogenous host-defense and
immune-cell signaling systems.
Experimental analysis of context-dependent interactions between
LL-37 and inflammatory signaling pathways.
Investigation of how the cationic and amphipathic structure of
LL-37 influences interactions with lipid membranes.
Studies involving epithelial cells, fibroblasts, endothelial
cells and other cellular models associated with tissue responses.
LL-37 5mg Research Specifications
Compound
LL-37
Product Format
5mg
Classification
Human Cathelicidin Peptide
Peptide Length
37 Amino Acids
Precursor
hCAP18
Gene
CAMP
Research Class
Antimicrobial Peptide
Form
Why Is LL-37 Studied?
LL-37 is scientifically interesting because a single endogenous
peptide participates in several interconnected areas of biological
research.
Its cationic amphipathic structure makes it valuable for membrane and antimicrobial peptide research, while
its endogenous role as a human cathelicidin makes it relevant to innate immune and host-defense biology.
At the same time, research involving inflammatory signaling,
chemotaxis, cellular migration and tissue responses demonstrates why
LL-37 is often studied as a multifunctional signaling peptide rather
than exclusively as an antimicrobial molecule.
LL-37 Peptide FAQ
What is LL-37 peptide?
LL-37 is a 37-amino-acid human cathelicidin-derived peptide studied extensively in antimicrobial, innate immunity, inflammatory signaling, biofilm and cellular-response research.
What does LL-37 stand for?
The name refers to the two leucine residues at the beginning of the mature peptide sequence, represented by LL, and its total length of 37 amino-acid residues.
Is LL-37 an antimicrobial peptide?
Yes. LL-37 is widely classified as a human antimicrobial peptide and has been extensively investigated in laboratory models involving microbial membranes and host-defense biology.
What is the LL-37 amino-acid sequence?
The 37-amino-acid LL-37 sequence is LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES.
What is hCAP18?
hCAP18 is the human cathelicidin precursor protein from which the mature LL-37 peptide is released through proteolytic processing.
What is the CAMP gene?
CAMP is the gene that encodes the human cathelicidin antimicrobial peptide precursor associated with hCAP18 and LL-37.
Why is LL-37 studied in biofilm research?
Researchers have investigated LL-37 in experimental biofilm systems to study microbial attachment, biofilm development, membrane interactions and other aspects of host-microbe biology.
Is LL-37 approved for human use?
LL-37 research material is not an approved medication. Royal Peptides supplies LL-37 5mg strictly for laboratory, analytical and research purposes.
LL-37 Lot Testing & COA
Every LL-37 lot is independently tested before release; results are listed with our coas peptides. For background reading, see published LL-37 research on PubMed.
Researchers Also Order
Compounds often studied alongside LL-37:
Buying LL-37
Where can I buy LL-37?
Order LL-37 directly from Royal Peptides. Choose a format in the Buy section, check out securely and your order ships from U.S. stock with lot documentation.
How fast do orders ship?
Orders are dispatched from U.S. inventory, usually within one business day, with tracking.
LL-37 for Laboratory Research
LL-37 is supplied for laboratory research use only. Not for human or veterinary use.
Specifications
Product information pulled directly from WooCommerce.
COA / Testing
Review available analytical documentation for the applicable product and batch in the COA library.
View COA LibraryShipping & Storage
Shipping options and delivery estimates are shown at checkout. Refer to the product label for storage requirements.




