PX1 Research provides high-purity Lys-Pro-Val (KPV) tripeptide engineered specifically for in vitro and preclinical research applications. Every batch undergoes rigorous third-party analytical testing, including RP-HPLC and mass spectrometry, ensuring optimal chemical integrity and lot-to-lot consistency for demanding laboratory assays.
PX1 Research provides high-purity Lys-Pro-Val (KPV) tripeptide engineered specifically for in vitro and preclinical research applications. Every batch undergoes rigorous third-party analytical testing, including RP-HPLC and mass spectrometry, ensuring optimal chemical integrity and lot-to-lot consistency for demanding laboratory assays.
When qualified investigators seek to buy KPV research peptide material for laboratory experimentation, securing compounds with documented sequence fidelity, high chemical purity, and quantified endotoxin levels is essential. KPV (Lysine-Proline-Valine) is a C-terminal tripeptide fragment of alpha-melanocyte-stimulating hormone (α-MSH) synthesized for in vitro assays and animal models evaluating inflammatory signal modulation, mucosal immunity, and epithelial barrier dynamics.
PX1 Research supplies USA-manufactured KPV 5mg alongside our broader catalog of research peptides. Each lot is independently analyzed by an ISO 17025 accredited laboratory to verify sequence identity via mass spectrometry (MS) and chromatographic purity exceeding 98% via reverse-phase high-performance liquid chromatography (RP-HPLC).
KPV is a synthetic tripeptide consisting of L-lysine, L-proline, and L-valine residues ($H-Lys-Pro-Val-OH$). With a molecular formula of $C_{16}H_{30}N_{4}O_{4}$ and a monoisotopic molecular weight of approximately 342.43 g/mol, KPV retains the core anti-inflammatory sequence motif found in parent pro-opiomelanocortin (POMC) derived peptides, specifically $\alpha$-MSH (residues 11–13).
Unlike its parent molecule $\alpha$-MSH, KPV lacks the melanogenic signaling capabilities associated with earlier amino acid sequences in the full-length peptide chain. This structural truncation allows researchers to evaluate specific immunomodulatory signaling pathways without inducing pigmentary pathways or non-target receptor interactions in cellular models. The presence of the central proline residue imparts conformational restriction, contributing to relative enzymatic stability in tissue culture mediums compared to linear, non-proline-containing short peptides.
Investigators cataloging small bioactive peptides often evaluate KPV in tandem with other endogenous signaling fragments available in the PX1 research library to determine structure-activity relationships across various cell types.
Preclinical literature demonstrates that KPV exerts its primary biological actions by modulating intracellular inflammatory cascades, particularly the nuclear factor kappa B (NF-$\kappa$B) pathway. In vitro studies utilizing intestinal epithelial cells (such as Caco-2 and HT-29 lines) show that KPV enters enterocytes via the oligopeptide transporter PepT1 (SLC15A1). Once internalized, the tripeptide inhibits the translocation of active NF-$\kappa$B p65 subunits into the nucleus.
By restricting NF-$\kappa$B nuclear entry, KPV suppresses the transcriptional activation of key pro-inflammatory cytokines, including tumor necrosis factor-alpha (TNF-$\alpha$), interleukin-1 beta (IL-1$\beta$), interleukin-6 (IL-6), and interleukin-8 (IL-8). Additionally, cellular assays indicate that KPV may decrease the expression of inducible nitric oxide synthase (iNOS), thereby mitigating excessive intracellular reactive nitrogen species generation during simulated inflammatory stress.
Researchers evaluating mucosal signaling pathways frequently cross-reference KPV with related melanocortin derivative models and immune-modulating agents detailed in our alpha-MSH signaling overview.
A primary focus of KPV investigation centers on gastrointestinal pathophysiology and mucosal membrane stabilization. In rodent models of experimental colitis—such as dextran sulfate sodium (DSS) and 2,4,6-trinitrobenzenesulfonic acid (TNBS) induced inflammation—preclinical administration of KPV has been shown to reduce histological damage scores, attenuate myeloperoxidase (MPO) activity, and preserve mucosal architecture.
In vitro models measuring transepithelial electrical resistance (TEER) across confluent epithelial monolayers indicate that KPV exposure helps maintain tight junction protein distribution, specifically zonula occludens-1 (ZO-1) and occludin. By stabilizing these intercellular structures, KPV mitigates pathological hyperpermeability induced by pro-inflammatory cytokine challenge.
Furthermore, nanotechnology-enabled delivery research has evaluated oral nanoparticle formulations of KPV targeted to the inflamed colon. These studies demonstrate localized accumulation in mucosal tissue, leading to enhanced local anti-inflammatory effects without systemic exposure, providing a valuable model for targeted peptide delivery systems.
In comparative preclinical research focused on tissue repair and gastrointestinal barrier preservation, investigators frequently examine KPV alongside other regulatory peptides. While KPV acts primarily as a PepT1-transported NF-$\kappa$B inhibitor, compounds such as BPC-157 operate through distinct angiogenic and growth factor upregulation pathways, including VEGFR2 and focal adhesion kinase (FAK) activation. Meanwhile, tight-junction regulators like Larazotide Acetate function as zonulin receptor antagonists, directly preventing the disassembly of intercellular tight junctions without directly suppressing cytoplasmic NF-$\kappa$B transcription.
The distinct mechanisms of these three compounds are summarized below for comparative assay design:
To ensure precise, reproducible experimental outcomes when you buy KPV research peptide stock, analytical verification must go beyond basic manufacturer self-reporting. PX1 Research adheres to rigorous quality control standards, subjecting every batch to independent analysis at accredited, third-party laboratory facilities in the United States.
Our comprehensive quality verification process includes:
1. Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC): Confirms a chromatographic purity threshold of equal to or greater than 98.0%. RP-HPLC isolates the target tripeptide peak from potential synthesis side-products, truncated sequences, or residual reagents. 2. Electrospray Ionization Mass Spectrometry (ESI-MS): Verifies exact mass fidelity, matching the theoretical mass-to-charge ratio ($m/z$) of Lys-Pro-Val ($[M+H]^+ = 343.24\text{ m/z}$) to rule out amino acid substitutions or incorrect linkages. 3. Bacterial Endotoxin Testing (LAL Assay): Quantitative Limulus Amebocyte Lysate assay testing ensures endotoxin levels remain strictly controlled (< 0.01 EU/mg), preventing confounding pyrogenic cellular responses in sensitive cell culture or animal assays. 4. Lot-Specific Certificates of Analysis (COA): Publicly accessible COA documentation detailing exact purity percentages, mass spectral charts, and batch tracking parameters.
For laboratories requiring bulk inventory or customized analytical parameters for high-throughput screening projects, dedicated options are available through our wholesale lab account portal.
KPV is supplied as a lyophilized (freeze-dried) sterile powder to maximize chemical stability during transport and storage. Proper reconstitution protocols must be observed to maintain peptide integrity prior to in vitro or preclinical administration.
Laboratory Reconstitution Protocol: • Solvent Selection: Reconstitute lyophilized KPV using sterile laboratory-grade Bacteriostatic Water (0.9% benzyl alcohol) or sterile Phosphate-Buffered Saline (PBS, pH 7.4) depending on experimental requirements. • Reconstitution Procedure: Allow the glass vial to equilibrate to room temperature before introducing the solvent. Gently introduce the diluent down the inner glass wall of the vial using a sterile pipette or syringe. Avoid forceful jetting directly onto the lyophilized cake. • Mixing: Swirl the vial with gentle rotational movements until complete dissolution occurs. Do not vortex or violently agitate the solution, as mechanical shear forces can cause peptide aggregation or denaturation. • Concentration Calculation: For a standard 5 mg vial, adding 2.0 mL of diluent yields a working stock concentration of 2.5 mg/mL (2,500 $\mu$g/mL).
Maintaining proper thermal management is crucial for preserving the chemical stability of KPV tripeptide stock over extended periods.
Lyophilized Powder Storage: Store dry lyophilized KPV at -20°C in a desiccated environment. Under these conditions, the un-reconstituted compound remains stable for up to 24 months from the date of manufacture. For short-term transit, the lyophilized peptide tolerates ambient room temperatures without measurable degradation.
Reconstituted Solution Storage: Once reconstituted into liquid stock, store solutions at 2°C to 8°C for immediate short-term use (up to 7–14 days). For longer-term storage of liquid stock, divide the solution into single-use laboratory micro-aliquots and store at -80°C. Avoid repeated freeze-thaw cycles, which introduce thermal stress that accelerates peptide bond hydrolysis.
Shipping & Fulfillment: Orders placed through PX1 Research are processed with same-day dispatch (Monday through Friday) from our centralized logistics facilities in California and Arizona, ensuring rapid, reliable delivery to institutional research labs nationwide.
What is the certified purity level when I buy KPV research peptide from PX1 Research?
Every lot of KPV supplied by PX1 Research is verified via RP-HPLC to meet or exceed a minimum purity threshold of 98.0%. Batch-specific Certificates of Analysis (COAs) detailing mass spectrometry and HPLC purity data are available for every shipment.
How is KPV peptide sequence identity confirmed?
Sequence identity is confirmed using Electrospray Ionization Mass Spectrometry (ESI-MS), verifying the exact monoisotopic mass and target structural ion peak corresponding to the Lys-Pro-Val amino acid sequence.
What is the molecular weight and sequence of KPV?
KPV is a tripeptide with the chemical sequence H-Lys-Pro-Val-OH (Lysine-Proline-Valine) and a monoisotopic molecular weight of 342.43 g/mol.
Are PX1 Research peptides tested for bacterial endotoxins?
Yes. Every peptide lot undergoes Limulus Amebocyte Lysate (LAL) testing to ensure endotoxin content is rigorously controlled below strict threshold limits (<0.01 EU/mg) to prevent non-specific pyrogenic reactions in experimental models.
What solvent is recommended for reconstituting KPV for cell culture research?
For in vitro cellular assays, sterile Phosphate-Buffered Saline (PBS, pH 7.4) or sterile water for injection is typically recommended. For multi-use laboratory stock solutions, sterile bacteriostatic water containing 0.9% benzyl alcohol may be utilized.
How should reconstituted KPV solutions be stored long-term?
Reconstituted KPV stock solutions should be aliquoted into single-use cryogenic tubes and stored at -80°C to minimize degradation and eliminate repeated freeze-thaw cycles.
Does KPV require cold-chain shipping during transit?
Lyophilized KPV powder is thermally stable at ambient temperatures during standard shipping durations. Upon receipt at the laboratory facility, dry vials should be transferred immediately to long-term storage at -20°C or -80°C.
Where does PX1 Research ship KPV products from?
All PX1 Research orders are manufactured in the USA and dispatched directly from our optimized logistics hubs located in California and Arizona, with same-day fulfillment for orders placed Monday through Friday.
All products are sold strictly for laboratory and research use only. Not for human or veterinary use, diagnosis, treatment or consumption. Statements have not been evaluated by the FDA.