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LL-37 Kit

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For laboratory and research purposes only.Not intended for human consumption, diagnostic use, therapeutic use, or administration to humans or animals.
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Human Cathelicidin Research Peptide • Research Use Only

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,

Research Use Only

Not for human or veterinary use, administration, ingestion, injection, compounding, diagnostic, therapeutic, clinical, or personal use.

LL-37

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5mg Kit(50mg)$390≈ $39 per vial
10mg Kit (100mg)$560≈ $56 per vial

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.

01

What Is LL-37 Peptide?

LL-37 is the principal human cathelicidin

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:

the mature peptide begins with two leucine residues

(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

in innate immune signaling, inflammatory responses,

chemotaxis, membrane biology and tissue-response pathways.

02

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.

LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES

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.

03

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).

hCAP18 is encoded by the CAMP gene. Enzymatic

processing releases the C-terminal LL-37 sequence from the precursor,

producing the mature peptide studied extensively in innate-immunity

research.

CAMP Gene

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.

04

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.

Research Context

Antimicrobial activity observed in laboratory experiments does not

mean LL-37 is an approved antimicrobial drug or treatment for an

infection.

05

LL-37 and Biofilm Research

LL-37 biofilm research is another important area

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.

06

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.

Host-Defense Research

LL-37 is studied as part of the endogenous peptide systems

associated with early innate immune responses.

Immune-Cell Signaling

Experimental research has examined interactions between LL-37

and signaling pathways involved in immune-cell recruitment and

cellular communication.

07

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

08

Host Defense

LL-37 and Inflammation Research

The relationship between LL-37 and inflammatory

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.

09

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.

10

LL-37 Research Areas

Antimicrobial Research

Laboratory investigation of LL-37 interactions with microbial

membranes and antimicrobial peptide mechanisms.

Biofilm Biology

Research involving microbial attachment, biofilm development

and peptide interactions with structured microbial communities.

Innate Immune Signaling

Investigation of LL-37 within endogenous host-defense and

immune-cell signaling systems.

Inflammatory Biology

Experimental analysis of context-dependent interactions between

LL-37 and inflammatory signaling pathways.

Membrane Research

Investigation of how the cationic and amphipathic structure of

LL-37 influences interactions with lipid membranes.

Cellular Response Research

Studies involving epithelial cells, fibroblasts, endothelial

cells and other cellular models associated with tissue responses.

11

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

12

Lyophilized Research Material

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.

13

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.

Quality Documentation

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.

Related Research

Researchers Also Order

Compounds often studied alongside LL-37:

Buying Questions

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.

Research Use Only

LL-37 for Laboratory Research

LL-37 is supplied for laboratory research use only. Not for human or veterinary use.