KPV Peptide – Anti-Inflammatory Signaling & Intestinal Research

Lys–Pro–Val Tripeptide for NF-κB, PepT1 Transport, Epithelial Cell Biology & Experimental Inflammation Research

KPV is a naturally occurring peptide sequence composed of three amino acids: lysine (K), proline (P) and valine (V).

It corresponds to the C-terminal tripeptide of alpha-melanocyte-stimulating hormone (α-MSH), a 13-amino-acid hormone derived from the proopiomelanocortin (POMC) precursor.

KPV has attracted scientific attention because laboratory studies have demonstrated effects on inflammatory signaling in selected cellular and animal models.

One of its most important research findings involves the intestinal peptide transporter PepT1 (SLC15A1), which can facilitate KPV uptake into intestinal epithelial cells.

Experimental studies have also investigated KPV-associated changes in NF-κB activation, MAP kinase signaling and pro-inflammatory cytokine expression.

These findings make KPV relevant to research involving:

• Inflammatory signaling

• NF-κB-associated pathways

• Intestinal epithelial biology

• PepT1-mediated peptide transport

• Experimental colitis

• Gastrointestinal inflammation

• Immune cell responses

• Cytokine-associated signaling

• Epithelial barrier biology

• Skin inflammation models

• Peptide structure–activity relationships

• α-MSH-derived peptide research

Although preclinical findings are scientifically interesting, KPV has not been established as a safe or effective treatment for inflammatory bowel disease, skin disorders, autoimmune conditions or other human diseases.

ICAME Pharmacy KPV is intended strictly for laboratory research and development purposes. Not for human or veterinary use.

What Is KPV?

KPV is a short tripeptide consisting of three naturally occurring L-amino acids.

Its name comes directly from the one-letter amino acid abbreviations:

K — Lysine

P — Proline

V — Valine

KPV represents residues 11–13 of α-MSH.

The parent hormone α-MSH participates in melanocortin signaling and has been investigated for roles in pigmentation, energy regulation and inflammation.

Scientists identified the C-terminal KPV region as an important sequence in certain anti-inflammatory experimental responses.

This finding generated interest in whether a much shorter peptide could retain selected biological properties associated with the parent hormone.

However, KPV is not pharmacologically identical to full-length α-MSH.

Its receptor interactions, transport characteristics and biological responses may differ substantially.

KPV Molecular Structure

KPV is a linear tripeptide.

The commonly referenced unmodified free-acid form has the sequence:

H-Lys-Pro-Val-OH

Molecular Characteristics

Compound Name: KPV

Full Name: Lysyl-Prolyl-Valine

Alternative Names: Lys–Pro–Val / α-MSH(11–13) / MSH(11–13)

Classification: Tripeptide / α-MSH-Derived Peptide Fragment

Amino Acid Length: 3 Residues

One-Letter Sequence: KPV

Three-Letter Sequence: Lys–Pro–Val

Molecular Formula: C₁₆H₃₀N₄O₄

Molecular Weight: Approximately 342.43 g/mol

CAS Number: 67727-97-3

PubChem CID: 125672

Parent Hormone: Alpha-Melanocyte-Stimulating Hormone

Associated Transporter: PepT1 / SLC15A1

Principal Research Pathways: NF-κB / MAPK-Associated Inflammatory Signaling

Primary Research Fields: Intestinal Biology / Inflammation / Epithelial Signaling

These characteristics refer to the unmodified free-acid tripeptide.

Amidated, acetylated, D-amino-acid-containing or other chemically modified variants may have different molecular properties and should not be treated as identical compounds.

KPV Amino Acid Sequence

The sequence of KPV is:

Lys–Pro–Val

Or, using the single-letter amino acid code:

K–P–V

Each amino acid contributes different structural characteristics.

Lysine (K)

Lysine contains a positively charged side chain under typical physiological conditions.

It can participate in electrostatic interactions with surrounding molecules.

Proline (P)

Proline has a cyclic side chain that constrains peptide backbone geometry.

This structural feature influences the conformational properties of short peptides.

Valine (V)

Valine contains a branched hydrophobic side chain.

It contributes to the peptide's overall physicochemical characteristics.

Why Is the Sequence Important?

The short length of KPV makes it useful for investigating the biological activity of specific regions within larger peptide hormones.

It also provides a model for studying how tripeptide transporters interact with biologically active peptide sequences.

KPV and Alpha-Melanocyte-Stimulating Hormone (α-MSH)

Alpha-MSH is a peptide hormone produced through processing of the POMC precursor.

It contains 13 amino acid residues.

The final three residues of its sequence are:

Lys–Pro–Val

These residues form the KPV sequence.

α-MSH Research

Full-length α-MSH participates in melanocortin receptor signaling.

Its biological activities have been investigated in:

Pigmentation

Energy homeostasis

Neuroendocrine signaling

Inflammatory responses

Immune regulation

Cellular stress responses

KPV Research

KPV has been investigated primarily for selected anti-inflammatory responses.

Because KPV lacks much of the parent hormone's receptor-binding sequence, its biological effects should not automatically be attributed to classical melanocortin receptor activation.

Research suggests that peptide transport and intracellular signaling are particularly important in some KPV experimental systems.

Discovery and Scientific Development of KPV

Interest in KPV emerged from research into the biological activity of α-MSH and its peptide fragments.

Scientists investigated whether shorter sequences derived from α-MSH could retain selected anti-inflammatory properties.

Studies of the C-terminal tripeptide identified activity in experimental inflammatory systems.

Subsequent research examined the molecular mechanisms involved.

An influential study published in Gastroenterology in 2008 investigated KPV uptake through the PepT1 transporter and its effects on intestinal inflammation.

The researchers examined human intestinal epithelial cell lines, immune cells and mouse models of experimental colitis.

Their findings provided evidence connecting KPV transport to inflammatory signaling responses.

However, these studies did not establish clinical efficacy in humans.

How Does KPV Work?

KPV does not have one universally established mechanism of action across all tissues.

Its best-characterized experimental mechanisms involve cellular uptake through peptide transporters and changes in inflammatory signaling pathways.

Simplified Research Mechanism

KPV (Lys–Pro–Val)

↓

PepT1-Mediated Cellular Uptake in Responsive Models

↓

Intracellular Signaling Responses

↓

Reduced NF-κB and MAPK Activation in Selected Experimental Systems

↓

Changes in Pro-Inflammatory Cytokine Expression

↓

Reduced Inflammatory Markers in Experimental Models

This pathway summarizes observations from specific studies.

It does not establish that KPV suppresses inflammation in every tissue or clinical condition.

The precise intracellular molecular targets remain incompletely characterized.

KPV and PepT1 (SLC15A1)

One of the most important areas of KPV research involves PepT1, also known as the proton-coupled oligopeptide transporter 1.

PepT1 is encoded by the SLC15A1 gene.

It transports many dipeptides and tripeptides across cellular membranes.

Where Is PepT1 Found?

PepT1 is normally expressed prominently in the small intestine.

Its expression can also change in inflammatory conditions.

Research has demonstrated PepT1 expression in selected intestinal epithelial and immune cell models.

KPV Transport Research

A 2008 study examined whether PepT1 could mediate KPV uptake.

Researchers used human intestinal epithelial cell lines and immune cells to investigate peptide transport.

The findings supported PepT1-associated uptake of KPV.

Why Is This Important?

Cellular transport influences whether a peptide can reach intracellular signaling systems.

However, transporter-mediated uptake in laboratory models does not establish clinically effective absorption, tissue distribution or systemic bioavailability in humans.

KPV and NF-κB Signaling

Nuclear factor kappa B (NF-κB) is a family of transcription factors involved in immune and inflammatory responses.

NF-κB regulates genes associated with:

Inflammatory cytokines

Immune signaling

Cell survival

Stress responses

Cellular proliferation

Inflammation-associated enzymes

KPV has been investigated in models involving NF-κB activation.

Experimental Findings

In selected cell culture systems, KPV exposure was associated with reduced NF-κB activation following inflammatory stimulation.

These changes were accompanied by alterations in inflammatory mediator expression.

Scientific Interpretation

Reduced NF-κB activity is an experimental molecular finding.

It does not automatically establish a beneficial clinical outcome.

NF-κB also participates in normal immune defense and cellular survival.

Its suppression can have context-dependent consequences.

KPV and MAP Kinase Signaling

Mitogen-activated protein kinase (MAPK) pathways participate in numerous cellular responses.

These include inflammation, growth, differentiation and stress signaling.

Major MAPK-related pathways include:

ERK1/2

JNK

p38 MAPK

KPV has been investigated in experimental systems involving inflammatory MAPK signaling.

Some studies have reported reductions in MAPK-associated activation following inflammatory stimulation.

However, these responses may vary depending on cell type, inflammatory stimulus and experimental conditions.

KPV should not be described as a universally selective MAPK inhibitor.

KPV and Cytokine Research

Cytokines are signaling proteins that coordinate immune and inflammatory responses.

Inflammatory cell models often measure cytokine production to evaluate cellular responses.

KPV-related research has examined markers including:

TNF-α

IL-1β

IL-6

Other inflammation-associated mediators

Changes in these markers can provide evidence of altered inflammatory signaling.

However, cytokine responses are complex.

A reduction in one inflammatory marker does not establish broad immune benefits or clinical effectiveness.

KPV and Intestinal Inflammation Research

Gastrointestinal research represents one of the most extensively investigated areas of KPV biology.

The intestinal epithelium forms an important interface between the external environment and internal tissues.

It participates in nutrient transport, immune signaling and barrier regulation.

KPV has been investigated in experimental systems involving intestinal inflammation.

Principal Research Areas

Intestinal epithelial cells

PepT1-mediated transport

NF-κB signaling

Inflammatory cytokines

Experimental colitis

Epithelial stress responses

Gastrointestinal immune regulation

The strongest evidence in this field remains preclinical.

KPV and Experimental Colitis

Colitis is inflammation of the colon.

Researchers commonly use animal models to investigate inflammatory mechanisms.

Two experimental systems frequently used in KPV research are:

DSS-Induced Colitis

Dextran sulfate sodium can produce intestinal injury and inflammation in laboratory animals.

TNBS-Induced Colitis

Trinitrobenzene sulfonic acid is used to induce inflammatory responses in experimental models.

Preclinical Findings

In a published study, KPV reduced selected inflammatory markers and histological signs of inflammation in mouse colitis models.

The researchers also investigated PepT1-associated transport.

Important Limitation

Mouse colitis models do not fully reproduce human inflammatory bowel disease.

Positive animal findings cannot establish clinical efficacy for ulcerative colitis or Crohn's disease.

KPV and Inflammatory Bowel Disease Research

Inflammatory bowel disease (IBD) includes conditions such as ulcerative colitis and Crohn's disease.

These disorders involve complex interactions between genetics, immune signaling, intestinal epithelial cells and environmental factors.

KPV has been investigated because its experimental activity intersects with pathways relevant to intestinal inflammation.

Research topics include:

PepT1 expression

Intestinal epithelial signaling

NF-κB activation

Cytokine expression

Experimental mucosal inflammation

Immune cell responses

However, KPV is not an established treatment for IBD.

No adequate human clinical evidence demonstrates that KPV induces remission, prevents relapse or replaces approved IBD therapies.

KPV and Intestinal Epithelial Cells

Intestinal epithelial cells perform multiple functions.

They contribute to nutrient absorption, barrier maintenance and immune communication.

KPV has been investigated in human intestinal epithelial cell lines, including Caco-2-derived and HT29-derived models.

Research endpoints include:

PepT1 transport activity

Inflammatory gene expression

NF-κB signaling

MAPK-associated responses

Cytokine production

Cellular stress

Cell line results are useful for understanding mechanisms but cannot fully predict responses in living humans.

KPV and Intestinal Barrier Research

The intestinal barrier consists of epithelial cells, tight junctions, mucus and immune-associated structures.

Barrier dysfunction is relevant to several gastrointestinal disorders.

KPV-related research intersects with epithelial inflammatory signaling.

Potential research endpoints include:

Tight junction-associated proteins

Epithelial permeability

Inflammatory mediator expression

Cell viability

Barrier-associated signaling

Cellular stress responses

However, evidence that KPV directly restores intestinal barrier function in humans is lacking.

Claims that it clinically repairs a “leaky gut” are not established.

KPV and Immune Cell Research

KPV has been investigated in selected immune cell systems.

These studies are relevant because immune cells contribute to inflammatory signaling.

Experimental research has included:

T-cell-associated models

Inflammatory stimulation

NF-κB activity

Cytokine expression

Peptide transporter biology

Cellular responses to inflammatory signals

KPV's effects may differ between immune cell types.

It should not be described as a proven systemic immunomodulatory treatment.

KPV and Skin Inflammation Research

Skin biology involves interactions among keratinocytes, fibroblasts, immune cells and extracellular matrix components.

Inflammatory signaling is relevant to numerous dermatological processes.

Because KPV is derived from α-MSH, researchers have investigated its effects in inflammation-associated systems that may be relevant to skin biology.

Research Topics

Keratinocyte signaling

Inflammatory mediators

Epithelial cell responses

NF-κB-associated pathways

Immune cell interactions

Cellular stress

However, findings from intestinal models should not automatically be transferred to skin tissue.

KPV has not been established as a clinical treatment for eczema, psoriasis, acne or rosacea.

KPV and Keratinocyte Research

Keratinocytes are the predominant cells in the epidermis.

They participate in skin barrier formation and inflammatory responses.

KPV may be relevant to experimental studies involving epithelial inflammation.

Potential endpoints include:

Keratinocyte viability

Inflammatory signaling

Cytokine expression

Barrier-associated proteins

Cellular stress responses

Immune-associated signaling

The evidence base for KPV in skin-specific models is less extensive than its better-characterized intestinal research.

Clinical benefits remain unproven.

KPV and Wound Healing Research

Wound healing is a complex biological process involving inflammation, cell migration, extracellular matrix formation and tissue remodeling.

Because KPV has been investigated in inflammatory signaling models, it has attracted interest in wound-related research.

Potential research topics include:

Inflammatory mediator regulation

Epithelial cell responses

Cellular migration

Tissue stress

Immune-associated signaling

However, KPV has not been clinically established to accelerate wound closure or improve healing outcomes in humans.

Anti-inflammatory activity alone does not establish wound-healing efficacy.

KPV and Oxidative Stress Research

Oxidative stress involves the production and regulation of reactive oxygen species.

Inflammatory signaling and oxidative stress often influence one another.

KPV-related experimental research may investigate:

Inflammatory stress responses

Reactive oxygen species-associated pathways

NF-κB signaling

Cell viability

Epithelial stress

Immune-associated cellular responses

However, KPV has not been established as a clinically effective antioxidant treatment.

KPV and Macrophage Research

Macrophages are immune cells involved in inflammatory responses, tissue maintenance and pathogen defense.

Their activity is influenced by numerous signaling pathways.

KPV-related research has investigated peptide transporter expression and inflammatory responses in immune-associated models.

Potential research endpoints include:

Inflammatory cytokines

NF-κB activation

Peptide transporter expression

Cellular stress

Immune signaling

Inflammation-associated gene expression

The effects of KPV on macrophage behavior remain dependent on the experimental model.

KPV and the Melanocortin System

The melanocortin system includes several receptors, commonly designated MC1R through MC5R.

These receptors participate in different physiological processes.

Full-length α-MSH activates melanocortin receptors.

KPV is a much shorter fragment.

Important Distinction

KPV should not automatically be classified as a full melanocortin receptor agonist.

Its reported anti-inflammatory activity in certain models is associated with mechanisms that can differ from the classical receptor interactions of full-length α-MSH.

The specific molecular targets underlying all KPV responses have not been completely established.

KPV and Peptide Transport Research

KPV is especially relevant to peptide transporter research because of its short length.

Transporters such as PepT1 recognize a range of dipeptides and tripeptides.

Research may examine:

Transporter substrate recognition

Cellular peptide uptake

Transport kinetics

Competition with other peptide substrates

Transporter expression

Intracellular signaling after uptake

However, the transport behavior of KPV can vary across tissues and experimental conditions.

Its human pharmacokinetic properties remain insufficiently characterized.

KPV and Cellular Uptake

Cellular uptake is important for understanding how a compound interacts with intracellular pathways.

KPV has been investigated using transporter-associated uptake experiments.

These studies support the role of PepT1 in certain cellular systems.

However, uptake into a cultured cell does not establish:

Effective systemic exposure

Tissue-specific delivery

Clinical bioavailability

Human therapeutic activity

Long-term safety

These properties require separate investigation.

KPV and Peptide Structure–Activity Relationships

Structure–activity relationship research examines how molecular structure influences biological activity.

KPV is useful because it represents a short fragment of a larger peptide hormone.

Researchers can compare:

KPV

Full-length α-MSH

Modified KPV analogues

D-Amino-Acid Variants

Terminally Modified Peptides

Other Melanocortin-Derived Fragments

These comparisons can help identify which structural features influence experimental signaling responses.

However, chemically modified analogues are distinct molecular entities.

Their results should not automatically be attributed to unmodified KPV.

KPV vs. Alpha-MSH

KPV and α-MSH share a related amino acid sequence but differ substantially in molecular size and pharmacology.

The biological activity of α-MSH cannot automatically be assigned to KPV.

KPV vs. GHK-Cu

KPV and GHK-Cu are both short peptides, but they have different structures and research applications.

KPV is a tripeptide associated with inflammatory and epithelial signaling research.

GHK-Cu is a copper-binding tripeptide complex investigated in extracellular matrix and skin-related biology.

The two compounds should not be treated as interchangeable.

KPV vs. BPC-157

BPC-157 is a synthetic 15-amino-acid peptide.

KPV contains only three amino acids.

BPC-157 has been investigated primarily in preclinical tissue injury and gastrointestinal models.

KPV has been investigated in inflammatory signaling and PepT1-associated intestinal research.

Findings from one compound cannot establish the biological activity of the other.

KPV vs. TB-500

TB-500 is a commercial designation associated with thymosin beta-4-related peptides.

Thymosin beta-4 research includes actin regulation, cellular migration and tissue biology.

KPV research focuses more directly on inflammatory and epithelial signaling.

The two compounds have different molecular structures and research histories.

The exact identity of TB-500 must be verified because commercial preparations may contain different thymosin beta-4-related sequences.

KPV vs. KLOW Peptide Blend

KPV is one of the four components commonly included in the commercial research blend known as KLOW.

KLOW typically contains:

GHK-Cu

BPC-157

TB-500

KPV

Main Difference

KPV is a single defined tripeptide.

KLOW is a multi-component formulation.

The inclusion of KPV in KLOW is generally associated with interest in inflammatory and epithelial signaling research.

However, there is no established evidence that adding KPV produces a synergistic effect with the other three peptides.

KPV vs. KLOW Comparison

Research on KPV alone does not establish the safety or efficacy of KLOW.

KPV and GLOW Peptide Blend

GLOW is another commercial research blend commonly containing GHK-Cu, BPC-157 and TB-500.

KPV is not generally part of the commonly advertised three-component GLOW formulation.

The addition of KPV is one of the defining differences between GLOW and KLOW.

However, commercial formulations vary, and exact product composition should always be verified.

KPV Human Clinical Evidence

The available KPV evidence is predominantly preclinical.

Published studies have investigated KPV in:

Human-derived cell lines

Immune cell models

Mouse colitis models

Peptide transport experiments

Inflammatory signaling assays

These studies provide mechanistic information.

However, they do not establish clinical efficacy.

A 2026 FDA scientific review reported that it had not identified clinical studies or human exposure data for KPV administered by any route.

Clinical Evidence Limitations

KPV has not been clinically established to:

• Treat ulcerative colitis.

• Treat Crohn's disease.

• Prevent inflammatory bowel disease relapse.

• Improve human intestinal barrier function.

• Treat eczema or psoriasis.

• Treat autoimmune disease.

• Accelerate wound healing.

• Improve systemic inflammatory disorders.

• Prevent age-related disease.

• Extend human lifespan.

The absence of adequate human evidence is a major limitation.

KPV Safety Considerations

KPV is biologically active in certain experimental systems.

Its safety profile in humans remains insufficiently characterized.

Important scientific concerns include:

Unknown Human Pharmacokinetics

Human absorption, distribution, metabolism and clearance have not been adequately established.

Unknown Long-Term Safety

Long-term systemic exposure has not been sufficiently studied.

Immune Signaling Effects

Changes in inflammatory pathways may have different consequences depending on the biological context.

Formulation Differences

Free-acid KPV, amidated analogues, acetate salts and other derivatives may have different analytical characteristics.

Product Impurities

Research-grade materials may contain synthesis-related impurities or degradation products.

Immunogenicity and Aggregation

Although KPV is a small peptide, the safety of specific preparations cannot be assumed without appropriate testing.

Lack of Clinical Evidence

Preclinical anti-inflammatory effects do not establish a safe or effective human treatment.

KPV and Regulatory Status

KPV is not an established FDA-approved human therapeutic drug.

In 2026, the FDA evaluated KPV in the context of pharmaceutical compounding and highlighted the absence of identified human clinical studies or exposure data.

The agency also noted that potential human safety risks remain unknown.

Regulatory discussion of a substance does not constitute approval of a finished drug product.

The regulatory status of research peptides and compounded substances may change.

Any commercial claims should be reviewed against current rules in the relevant jurisdiction.

KPV and Research Product Quality

The chemical identity of a KPV preparation should be confirmed analytically.

Important specifications include:

Amino acid sequence

Stereochemistry

Terminal chemical groups

Molecular identity

Peptide purity

Peptide content

Counterion composition

Impurity profile

Stability

Batch-specific analytical documentation

Why Terminal Chemistry Matters

The unmodified free-acid KPV tripeptide has the structure:

H-Lys-Pro-Val-OH

Other variants may contain different terminal groups.

These modifications can change molecular weight, charge, stability and biological behavior.

Consequently, the exact molecular form should be specified rather than relying only on the name KPV.

KPV Analytical Testing

Research-grade KPV may be characterized using appropriate analytical techniques.

High-Performance Liquid Chromatography (HPLC)

HPLC can help evaluate peptide purity and detect certain impurities.

Liquid Chromatography–Mass Spectrometry (LC-MS)

LC-MS can support molecular identity confirmation and impurity characterization.

Mass Spectrometry

Mass analysis can verify whether the detected molecular species is consistent with the expected peptide.

Peptide Content Analysis

Content analysis helps distinguish the quantity of the target peptide from total lyophilized material.

Stability Studies

Stability testing can identify degradation under defined conditions.

Certificate of Analysis

A batch-specific COA should identify the material, testing methods and analytical results.

A purity percentage alone does not establish pharmaceutical quality or suitability for human use.

Scientific Evidence and Research Limitations

Established Scientific Findings

• KPV is a three-amino-acid peptide.

• Its sequence is Lys–Pro–Val.

• It corresponds to the C-terminal region of α-MSH.

• The unmodified free-acid form has a molecular weight of approximately 342.43 g/mol.

• KPV has been investigated in inflammatory cell models.

• PepT1-mediated uptake has been demonstrated in selected experimental systems.

• Reduced NF-κB and MAPK activation has been reported in certain models.

• Reduced inflammatory markers have been observed in mouse colitis experiments.

• KPV is included in some multi-peptide research blends, including KLOW.

Important Limitations

• Human therapeutic efficacy is not established.

• Human pharmacokinetics are insufficiently characterized.

• Long-term human safety is unknown.

• Results from mouse colitis models cannot establish efficacy for human IBD.

• Reduced inflammatory markers do not establish broad clinical benefits.

• KPV is not pharmacologically identical to full-length α-MSH.

• Modified KPV analogues may differ from the unmodified peptide.

• Evidence involving KPV alone does not establish the effects of KLOW.

• Product identity and purity must be confirmed for each research batch.

Potential KPV Research Applications

KPV may be relevant to appropriately controlled laboratory investigations involving:

• Alpha-MSH fragment biology

• Tripeptide structure–activity relationships

• PepT1 / SLC15A1 transport

• Intestinal epithelial cell biology

• NF-κB-associated signaling

• MAPK-associated inflammatory pathways

• Cytokine expression

• Immune cell responses

• Experimental colitis

• DSS-induced intestinal inflammation

• TNBS-induced intestinal inflammation

• Gastrointestinal epithelial research

• Inflammatory bowel disease mechanisms

• Intestinal barrier-associated biology

• Keratinocyte research

• Skin inflammatory signaling

• Cellular stress responses

• Peptide transporter pharmacology

• Peptide stability

• Peptide analytical characterization

• Comparative melanocortin-derived peptide research

• Multi-peptide formulation studies

These are research applications, not established clinical benefits.

KPV Research Overview

Compound Name: KPV

Full Name: Lysyl-Prolyl-Valine

Alternative Names: Lys–Pro–Val / α-MSH(11–13)

Classification: Tripeptide

Peptide Length: 3 Amino Acids

Sequence: H-Lys-Pro-Val-OH

Molecular Formula: C₁₆H₃₀N₄O₄

Molecular Weight: Approximately 342.43 g/mol

CAS Number: 67727-97-3

PubChem CID: 125672

Parent Hormone: Alpha-Melanocyte-Stimulating Hormone

Associated Transporter: PepT1 / SLC15A1

Principal Research Pathways: NF-κB / MAPK

Primary Research Fields: Inflammation / Intestinal Biology / Peptide Transport

Established Human Clinical Efficacy: None

Human Long-Term Safety: Not Established

Intended Product Use: Laboratory Research Only

Product Information

Product Name: KPV

Alternative Name: Lys–Pro–Val

Brand: ICAME Pharmacy

Product Category: Research Peptide

Research Classification: α-MSH-Derived Tripeptide

Research Areas: NF-κB / PepT1 / Inflammatory Signaling / Intestinal Epithelial Biology

Intended Use: Laboratory Research & Development Only

The identity and specifications of the supplied research material should be confirmed through batch-specific manufacturer documentation.

Relevant analytical information includes:

• Verified amino acid sequence

• Stereochemical identity

• Terminal functional groups

• Molecular identity

• Peptide purity

• Peptide content

• Salt form and counterions

• Impurity profile

• Analytical methodology

• Certificate of Analysis (COA)

• Batch/lot identification

• Validated storage conditions

No claims of pharmaceutical quality, sterility, injectable suitability or clinical efficacy should be made without appropriate supporting documentation and regulatory authorization.

Important Research Use Notice

FOR RESEARCH USE ONLY (RUO)

This ICAME Pharmacy product is intended exclusively for legitimate laboratory, analytical and scientific research purposes.

Not for human or veterinary use. Not for diagnostic, therapeutic, anti-inflammatory treatment, gastrointestinal treatment, dermatological treatment, performance-enhancing, anti-aging or other clinical purposes. Not for direct administration to humans or animals.

KPV is a biologically active tripeptide investigated in experimental inflammatory and intestinal models.

Its human clinical efficacy, pharmacokinetics and long-term safety have not been established.

Preclinical findings should not be interpreted as proof of therapeutic effectiveness.

Information presented on this page is intended solely for scientific and educational purposes and does not constitute medical advice, prescribing information, dosage guidance or instructions for human use.

About ICAME Pharmacy

ICAME Pharmacy provides specialized research products for professional laboratory and scientific applications.

Our portfolio focuses on compounds relevant to peptide science, inflammatory signaling, intestinal biology, molecular pharmacology and analytical research.

We emphasize accurate product identification, responsible research use, scientific transparency and clear communication of evidence limitations.

For batch-specific analytical documentation and product inquiries, please contact ICAME Pharmacy.

Frequently Asked Questions About KPV

What is KPV?

KPV is a tripeptide composed of lysine, proline and valine. It corresponds to the C-terminal three amino acids of α-MSH.

What does KPV stand for?

KPV represents the one-letter amino acid codes for lysine (K), proline (P) and valine (V).

How many amino acids does KPV contain?

KPV contains three amino acid residues.

What is the amino acid sequence of KPV?

The sequence is Lys–Pro–Val, commonly written as H-Lys-Pro-Val-OH for the unmodified free-acid form.

What is the molecular weight of KPV?

Approximately 342.43 g/mol for the unmodified free-acid tripeptide.

What is the molecular formula of KPV?

C₁₆H₃₀N₄O₄.

What is the CAS number of KPV?

67727-97-3 for the commonly referenced free-acid form.

Is KPV derived from α-MSH?

Yes. KPV corresponds to the final three amino acid residues of α-MSH.

What is the main mechanism of KPV?

KPV has been investigated for PepT1-associated cellular uptake and changes in NF-κB and MAPK inflammatory signaling in selected experimental models.

Does KPV inhibit NF-κB?

Certain cell studies have reported reduced NF-κB activation following KPV exposure. This does not establish universal inhibition or clinical effectiveness.

What is PepT1?

PepT1 is a proton-coupled peptide transporter involved in the uptake of many dipeptides and tripeptides.

Has KPV been studied in colitis?

Yes. KPV has been investigated in DSS- and TNBS-induced mouse colitis models.

Does KPV treat inflammatory bowel disease?

KPV has not been established as a safe or effective treatment for human inflammatory bowel disease.

Is KPV effective for ulcerative colitis?

No adequate human clinical evidence establishes KPV as an effective treatment for ulcerative colitis.

Does KPV help with Crohn's disease?

Clinical efficacy for Crohn's disease has not been established.

Is KPV a skin treatment?

KPV has been investigated in inflammation-related research, but it is not an established treatment for dermatological disorders.

Is KPV the same as GHK-Cu?

No. KPV is Lys–Pro–Val, while GHK-Cu is a copper complex of Gly–His–Lys.

Is KPV included in KLOW?

Yes. KPV is commonly one of the four components of the KLOW research blend.

Is KPV approved for human treatment?

KPV is not an established approved human therapeutic drug.

Is ICAME Pharmacy KPV intended for human use?

No. ICAME Pharmacy KPV is intended strictly for laboratory research and development purposes.