KPV is a tripeptide (Lys-Pro-Val) corresponding to the C-terminal three residues of alpha-melanocyte-stimulating hormone (alpha-MSH). It is widely studied as an anti-inflammatory fragment that retains alpha-MSH's immunomodulatory activity without its pigmentary effects, making it a favored tool for investigating inflammatory signaling pathways. Puritide Research supplies KPV as a high-purity, research-use-only material, synthesized for in vitro and animal-model work and backed by third-party-verified certificates of analysis so your data rests on consistent, documented quality.
Product Specifications
- Application
- Anti-inflammatory signaling and NF-kB pathway research (alpha-MSH fragment)
- Appearance
- Solid, white lyophilized powder in a sealed glass vial
- Chemical Formula
- C16H30N4O4
- PubChem SID
- 125672
- CAS Number
- 67727-97-3
- Molecular Weight
- ~342.43 g/mol
- Synonyms
- KPV, Lys-Pro-Val, H-Lys-Pro-Val-OH, alpha-MSH (11-13)
- Storage
- Store at ≤25°C, sealed, away from heat, light, and moisture. For extended storage, keep lyophilized and refrigerated or frozen.
What Is KPV?
KPV is a synthetic tripeptide composed of the amino acids lysine, proline, and valine (Lys-Pro-Val). It corresponds to positions 11 to 13 of alpha-melanocyte-stimulating hormone (alpha-MSH), a 13-residue neuropeptide with well-documented anti-inflammatory and immunomodulatory activity.
Research indicates that this short C-terminal fragment retains much of alpha-MSH's anti-inflammatory character while lacking the pigment-stimulating (melanotropic) activity of the full peptide. This separation of function is a central reason KPV is used as a clean probe for inflammatory signaling in experimental systems.
Present understanding derives from in vitro assays and animal models. Findings should be interpreted within their experimental context and not treated as established clinical outcomes. Puritide Research supplies KPV strictly for laboratory use; it is not approved for human or veterinary application.
KPV Mechanism of Action (Research Only)
KPV is studied for its ability to modulate inflammatory signaling, most notably the NF-kB pathway, in intestinal epithelial and immune cell models. The observations below reflect biochemical assays and cell-culture studies and should be read strictly in a research context.
NF-kB Pathway Modulation
A primary focus of KPV research is its association with reduced NF-kB activation. In cell models the tripeptide has been linked to preserved IkB-alpha and diminished nuclear translocation of NF-kB, events connected to lower expression of pro-inflammatory cytokines such as TNF-alpha, IL-1beta, and IL-6 under experimental conditions.
Cellular Uptake via PepT1
KPV has been characterized as a substrate for PepT1, a di- and tripeptide transporter expressed in intestinal epithelial cells and induced in immune cells during inflammation. PepT1-mediated uptake is studied as a route by which the tripeptide reaches intracellular signaling compartments in these models.
Researchers use KPV to examine anti-inflammatory signaling that is decoupled from melanocortin-driven pigmentation, comparing it with the parent alpha-MSH and related fragments to characterize structure-activity relationships under defined conditions rather than to establish physiological effects.
KPV Research Applications
KPV is investigated across cell-based and preclinical studies as a compact anti-inflammatory probe derived from alpha-MSH. The observations below derive from biochemical studies, cell assays, and animal models, and should be interpreted within their respective settings.
Inflammatory Signaling and Mucosal Models
A primary application is studying NF-kB-associated inflammatory signaling in intestinal epithelial and immune cell cultures, including models of inflammatory bowel disease. KPV is used to examine cytokine expression, IkB-alpha stability, and transporter-mediated uptake under controlled conditions.
KPV is also applied in dermatological and mucosal inflammation models, where researchers study anti-inflammatory activity that is separated from the pigmentary effects of the parent hormone.
Structure-Activity and Comparative Peptide Studies
Because KPV is a minimal active fragment of alpha-MSH, it is used in structure-activity research comparing it with the full peptide and related tripeptides such as KdPT. These studies aim to map which residues confer anti-inflammatory activity rather than to establish therapeutic outcomes.
Laboratory Safety & Handling (Research Use Only)
KPV is a synthetic, lyophilized research peptide for laboratory investigation only. It should be handled by qualified personnel in controlled environments, in accordance with institutional policies, laboratory safety procedures, and applicable regulations. As an investigational material, laboratories should implement practices that prioritize material integrity, traceability, and reproducibility.
Handling & Storage Guidelines
Follow institutional SOPs, chemical hygiene plans, and approved protocols; wear appropriate PPE (lab coat, gloves, eye protection); and use engineering controls where required. Record lot numbers, storage conditions, and handling activities, and retain Certificates of Analysis and batch documentation to support traceability and audit readiness.
Store material under the conditions specified in product documentation, protected from excessive heat, moisture, and direct light. Maintain consistent conditions throughout the study period and monitor storage records as part of quality assurance. Consistent handling and documentation support reliable, reproducible outcomes.
Certificate of Analysis & Quality Assurance
Each KPV batch ships with a third-party-verified Certificate of Analysis, providing transparent, research-grade quality control. The CoA includes a purity assessment (HPLC / reverse-phase chromatography), mass-spectrometry identity confirmation, and lot number, testing date, and method documentation.
Researchers may request sample CoAs (PDF) ahead of purchase to confirm testing parameters, analytical methods, and batch consistency, and are encouraged to perform independent verification.