KPV | Peptide Reference Material
RESEARCH PEPTIDE

KPV | Peptide Reference Material

Melanocortin-Derived Tripeptide — Research Peptide
$29.00
KPV (Lys-Pro-Val) is the three-residue C-terminal alpha-MSH(11–13) sequence. Published cell and mouse studies examined KPV uptake and inflammatory-signaling readouts in defined intestinal epithelial response models. For research use only; not for human or veterinary use.
✓ Identity Verified
✓ Batch Documentation
✓ QR Lot Verification
✓ Research Use Only
✓ U.S. Fulfillment
✓ Batch Verification Available View verification →
Lot Verification Variant-specific documentation
Traceable Lots VBL lot identification
Primary Literature Peer-reviewed sources
Research Use Only Laboratory research materials

Scientific Specifications

Reference characteristics for laboratory research materials.

CAS Number
67727-97-3
Purity
≥98%
Molecular Formula
C16H30N4O4
Molecular Weight
342.43
Appearance
White lyophilized powder
Storage
-20°C
Research Classification
Research Use Only (RUO). Not for human or veterinary use.

SCIENTIFIC OVERVIEW

Scientific background and research classification for this laboratory reference material.

KPV is the linear tripeptide Lys-Pro-Val and corresponds to the C-terminal alpha-MSH(11–13) sequence. The reported alpha-MSH sequence terminates in Lys-Pro-Val; KPV is therefore an alpha-MSH-derived fragment rather than the full 13-residue parent peptide. PubChem CID 125672 lists the alpha-MSH(11–13) / Lys-Pro-Val compound record.

Experimental interest in KPV includes defining which observations associated with alpha-MSH-derived peptides can be examined in a short C-terminal fragment. In a mouse picryl-chloride ear-swelling experiment, alpha-MSH(11–13) produced dose-related changes in that model. In separate cell and mouse studies, KPV was examined in intestinal epithelial/immune cell systems and induced mouse-colitis models. These are experimental findings, not established human effects.

In the Dalmasso study, KPV uptake and signaling readouts were examined in defined Caco2-BBE and HT29-Cl.19A intestinal epithelial cell lines, Jurkat T cells, and DSS/TNBS mouse-colitis systems. The study reported PepT1-associated KPV uptake in its cell systems and changes in NF-kappaB/MAP kinase and cytokine readouts under the tested conditions. No source in this dossier establishes human efficacy, safety, pharmacokinetics, dosing, or product-lot performance.

Primary Research Category
Immune Regulation
Material Type
Lyophilized Peptide
Intended Use
Laboratory Research
Research Categories
Immune Regulation Inflammation Melanocortin Biology Cytokine Signaling

Mechanism of Action

Molecular interaction profile describing how this research material engages receptor systems and influences downstream biological signaling pathways.

KPV's origin from the C-terminal alpha-MSH(11–13) region provides a melanocortin-related structural context, but it does not establish that KPV acts through classical melanocortin-receptor agonism. In a murine colitis study using mice with nonfunctional MC1R, observed KPV effects were reported as at least partly independent of MC1R signaling. The cited evidence therefore does not support assigning KPV a definitive receptor target.

Transport and downstream signaling should be distinguished. In Caco2-BBE intestinal epithelial cells, KPV uptake was studied by radiolabeled transport experiments and competition with a PepT1 substrate. In cytokine-stimulated Caco2-BBE cells and hPepT1-transfected HT29-Cl.19A cells, the study reported PepT1-associated coupling to reduced NF-kappaB reporter activity under its experimental conditions. This supports a transport/uptake relationship in those cell systems, not a universal uptake mechanism or human absorption claim.

In the same intestinal/immune cell study, KPV was associated with reduced NF-kappaB and MAP kinase signaling readouts and lower pro-inflammatory cytokine secretion in specified cultured systems. In immortalized human bronchial epithelial cells, a separate study reported KPV-associated reductions in NF-kappaB reporter activity, IL-8, eotaxin, and MMP-9 readouts, with observations involving I-kappaB-alpha stabilization and reduced p65RelA nuclear translocation. These cell-model observations do not establish a direct binding target, a universal downstream mechanism, or a human clinical effect. MC3R dependence in that study applied to gamma-MSH, not KPV.

In DSS/TNBS and CD45RBhi transfer mouse-colitis models, KPV was associated with model-specific histologic, myeloperoxidase, cytokine-mRNA, recovery, or weight readouts. The precise downstream mechanism remains incompletely characterized and these preclinical models do not establish therapeutic or preventive effects in humans.

Biological Pathways
  • NF-κB Signaling
  • Inflammatory Signaling
Primary Organ Systems
  • Gastrointestinal System
  • Immune System

Research Documentation

Laboratory documentation is presented when available for the selected product specification and current lot.

Batch Verified
Independent Batch Verification

Independent laboratory verification for this batch:

  • Identity Confirmation
  • HPLC Purity Analysis
  • Net Peptide Content
  • Endotoxin Testing
  • Analytical Chromatogram
  • Independent Laboratory Verification
View Batch Verification →
Scientific References
Peer-Reviewed Literature

Explore published literature, clinical investigations, and foundational scientific research.

View References →
Laboratory Resources
Technical Guidance

Storage guidance, handling recommendations, analytical methods, and laboratory best practices.

Related Research
Companion Materials

Discover complementary research materials frequently studied alongside this compound.

Research Center

Source-supported research categories for this laboratory reference material.

Identity Context
alpha-MSH(11–13) Peptide Biology

KPV is the Lys-Pro-Val C-terminal tripeptide of alpha-MSH(11–13). Experimental work has used this short fragment to examine which alpha-MSH-derived observations can be studied apart from the full 13-residue parent peptide. The fragment relationship provides structural context; it does not establish that KPV shares all parent-peptide receptor pharmacology.

Browse References →
Cell Model
Intestinal Epithelial Transport Models

In defined Caco2-BBE and HT29-Cl.19A intestinal epithelial cell systems, KPV uptake was studied using radiolabeled transport experiments, PepT1-substrate competition, and NF-kappaB reporter readouts. These experiments support PepT1-associated transport/uptake in those models; they do not establish human absorption or explain all downstream effects.

Browse References →
Experimental Readouts
Inflammatory Signaling Readouts

In cytokine-stimulated intestinal epithelial and immune cell systems, the cited study reported KPV-associated changes in NF-kappaB and MAP kinase readouts and pro-inflammatory cytokine secretion. A separate immortalized bronchial epithelial-cell study reported KPV-associated NF-kappaB, IL-8, eotaxin, MMP-9, I-kappaB-alpha, and p65RelA readouts. These are model-specific observations, not an established human mechanism or direct receptor claim.

Browse References →
Preclinical Models
Experimental Inflammation Models

Published KPV studies include picryl-chloride ear-swelling experiments and DSS, TNBS, and CD45RBhi transfer mouse-colitis models, with reported model-specific histologic, myeloperoxidase, cytokine-mRNA, recovery, or weight readouts. These preclinical findings do not establish therapeutic or preventive effects in humans.

Browse References →

Research Library

Curated peer-reviewed literature selected to provide scientific context for this research material.

Preclinical Study•The FASEB Journal• 1989

Antiinflammatory activity of a COOH-terminal fragment of the neuropeptide alpha-MSH

Foundational report that the COOH-terminal fragment of alpha-MSH (the Lys-Pro-Val tripeptide) possesses anti-inflammatory activity, establishing KPV as the anti-inflammatory C-terminal fragment of the neuropeptide.
Velora Research Insight
Founding characterization of KPV's anti-inflammatory activity as an α-MSH C-terminal fragment. Discovery-class evidence from the Lipton laboratory; the independent origin of the KPV anti-inflammatory literature.
PubMed →
Mechanistic Study•Gastroenterology• 2008

PepT1-mediated tripeptide KPV uptake reduces intestinal inflammation

Mechanistic study reporting that KPV is taken up by intestinal epithelial and immune cells via the di/tripeptide transporter PepT1 and reduces intestinal inflammation, including attenuation of NF-κB pathway activation.
Velora Research Insight
Proximal mechanism anchor: PepT1-mediated intracellular uptake and NF-κB attenuation. Merlin-lab lineage (shared with VSE-PUB-000067) — counted as one independent lineage, not two.
PubMed →DOI →
Preclinical Study•Inflammatory Bowel Diseases• 2008

Melanocortin-derived tripeptide KPV has anti-inflammatory potential in murine models of inflammatory bowel disease

Independent study reporting anti-inflammatory potential of the melanocortin-derived tripeptide KPV in murine models of inflammatory bowel disease.
Velora Research Insight
Independent preclinical corroboration of KPV anti-inflammatory activity in IBD models. Kucharzik/Münster lineage — independent of the Lipton and Merlin lineages.
PubMed →DOI →
Preclinical Study•Molecular Therapy• 2017

Orally Targeted Delivery of Tripeptide KPV via Hyaluronic Acid-Functionalized Nanoparticles Efficiently Alleviates Ulcerative Colitis

Preclinical study reporting that orally administered hyaluronic-acid-functionalized nanoparticles delivering KPV alleviated experimental ulcerative colitis in a mouse model.
Velora Research Insight
Translational delivery context for KPV in experimental ulcerative colitis. Merlin-lab lineage (shared with VSE-PUB-000065) — not an additional independent lineage.
PubMed →DOI →