The standard CAS number assigned to the KPV tripeptide (Lysine-Proline-Valine) is 67910-15-8. Representing the C-terminal tripeptide sequence of alpha-melanocyte-stimulating hormone (α-MSH), KPV is widely evaluated in preclinical models for its potent anti-inflammatory properties and mucosal barrier modulation.
The standard CAS number assigned to the KPV tripeptide (Lysine-Proline-Valine) is 67910-15-8. Representing the C-terminal tripeptide sequence of alpha-melanocyte-stimulating hormone (α-MSH), KPV is widely evaluated in preclinical models for its potent anti-inflammatory properties and mucosal barrier modulation.
In chemical databases and analytical literature, the primary reference key for the tripeptide Lysine-Proline-Valine (Lys-Pro-Val) is the KPV CAS number: 67910-15-8. This chemical abstract service registry number unambiguously identifies the specific peptide structure across international chemical registries and analytical safety data sheets (SDS). KPV is an endogenous-derived tripeptide consisting of three L-amino acid residues linked via standard peptide bonds: L-lysine, L-proline, and L-valine.
When purchasing compounds for cellular assays or animal models, confirming the exact KPV CAS number ensures researchers receive the intended tripeptide sequence rather than larger fragments or alternative isomers of alpha-melanocyte-stimulating hormone (α-MSH). In its standard acetate salt form, KPV exhibits high aqueous solubility, making it ideal for standard buffer preparations used in cell culture and in vitro biochemical evaluations available in our all peptides catalog.
The molecular formula of free-base KPV is C16H30N4O4, corresponding to a monoisotopic molecular weight of 342.2267 g/mol and a nominal molecular mass of approximately 342.44 g/mol. The primary structural motif consists of an N-terminal positively charged lysine residue, a central rigid proline ring that introduces structural constraints, and a hydrophobic C-terminal valine residue.
Analytical physical properties of high-purity laboratory grade KPV include a lyophilized white to off-white powder appearance, a net positive charge at physiological pH (pH 7.4) due to the basic side chain of lysine, and an isoelectric point (pI) above 8.5. Researchers studying peptide transport mechanisms frequently track the chemical physical traits via analytical profiles documented across our research library hub.
Preclinical studies indicate that KPV retains key biological activities of its parent molecule, α-MSH, without exhibiting the pigmentary effects mediated by melanocortin-1 receptor (MC1R) activation in cutaneous tissues. The tripeptide operates primarily by entering target cells and downregulating intracellular inflammatory cascades.
In vitro data demonstrate that KPV acts directly on the nuclear factor kappa B (NF-κB) pathway. Mechanistically, intracellular uptake of KPV inhibits the translocation of the NF-κB p65 subunit into the nucleus. This inhibition prevents the downstream transcriptional activation of pro-inflammatory cytokines, including tumor necrosis factor-alpha (TNF-α), interleukin-1 beta (IL-1β), and interleukin-6 (IL-6). Researchers investigating novel cytokine modulators frequently cross-reference KPV with related anti-inflammatory molecules listed under our research peptides tag.
A major area of preclinical investigation for KPV centers on intestinal mucosal integrity and experimental colitis models. Rodent models utilizing dextran sulfate sodium (DSS) or 2,4,6-trinitrobenzenesulfonic acid (TNBS) to induce intestinal inflammation have demonstrated that KPV administration modulates mucosal damage and attenuates systemic inflammatory markers.
In vitro assays using Caco-2 cell monolayers suggest that KPV preserves epithelial tight junction architecture. Specifically, KPV exposure maintains the expression and localization of tight junction proteins, such as Zonula Occludens-1 (ZO-1) and Occludin, during inflammatory challenge. Consequently, KPV is frequently deployed alongside other gut-barrier research peptides, such as BPC-157 and Larazotide acetate, to evaluate synergistic mucosal repair mechanisms.
When evaluating compounds targeting inflammatory pathways and epithelial tissue repair, researchers commonly compare KPV against other established reference peptides. While KPV specifically targets intracellular NF-κB transport and α-MSH-mediated pathways, alternative compounds operate via distinct molecular targets.
For instance, BPC-157 works primarily by upregulating growth factor expression (such as VEGF and FAK) and accelerating tissue granulation. Contrastingly, VIP peptide acts through specific GPCR signaling pathways (VPAC1 and VPAC2) to regulate local immune response and vascular tone. Meanwhile, LL-37 provides antimicrobial host defense while modulating innate immune cell recruitment. Understanding these mechanistic differences allows laboratories to select the exact molecular candidate required for their specific assay design.
Because laboratory findings depend strictly on chemical consistency, research-grade compounds must adhere to rigid purity and analytical characterization standards. The identity of KPV (CAS 67910-15-8) should always be confirmed via Electrospray Ionization Mass Spectrometry (ESI-MS) to verify the expected 342.44 g/mol mass signature.
Purity must be validated using Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC). PX1 Research guarantees a minimum analytical purity of 99% for every lot. Furthermore, because bacterial endotoxins can confound cell culture assays by independently activating NF-κB pathways, every batch undergoes chromogenic LAL testing to verify endotoxin levels below 0.01 EU/mg. Laboratories establishing strict experimental protocol parameters can review lot-specific documentation prior to placing orders through our wholesale lab portal.
Proper handling and storage protocols are critical for maintaining peptide integrity over extended experimental timelines. Lyophilized KPV powder should be stored at -20°C or -80°C in a desiccated environment away from direct light exposure to prevent moisture absorption and peptide degradation.
For in vitro reconstitution, lyophilized KPV should be dissolved in sterile, cell-culture-grade water or sterile phosphate-buffered saline (PBS, pH 7.4). Because KPV is highly soluble in aqueous media, gentle manual swirling is sufficient; energetic vortexing or sonication should be avoided to prevent mechanical shearing. Reconstituted stock solutions should be aliquoted into single-use polypropylene microcentrifuge tubes and stored at -80°C to eliminate damaging freeze-thaw cycles. To purchase analytical-grade single vials, visit the official KPV peptide product page.
PX1 Research is committed to supplying US-manufactured, ISO 17025 and GMP-compliant research materials for academic and corporate research facilities. Every lot of KPV undergoes rigorous third-party analytical testing prior to release, ensuring full lot traceability and absolute chemical fidelity.
Orders are dispatched same-day (Monday through Friday) directly from centralized fulfillment centers located in California and Arizona. By maintaining cold-chain integrity and rapid shipping schedules, PX1 Research ensures that research reagents arrive in optimal condition for immediate experimental deployment.
What is the kpv cas number?
The CAS registry number for the KPV tripeptide (Lysine-Proline-Valine) is 67910-15-8. This unique numerical identifier is used internationally to reference the chemical compound in scientific literature and safety data sheets.
What is the molecular formula and weight of KPV?
KPV has a chemical formula of C16H30N4O4 and a molecular weight of approximately 342.44 g/mol (monoisotopic mass: 342.2267 g/mol).
What amino acid sequence corresponds to CAS 67910-15-8?
CAS 67910-15-8 corresponds to the tripeptide sequence Lysine-Proline-Valine (Lys-Pro-Val or KPV), which represents the C-terminal sequence of alpha-melanocyte-stimulating hormone (α-MSH).
How is KPV purity tested at PX1 Research?
PX1 Research evaluates KPV purity using Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) paired with Mass Spectrometry (ESI-MS). Each lot must meet or exceed a 99% purity threshold accompanied by an independent Certificate of Analysis (COA).
What are the endotoxin limits for laboratory-grade KPV?
All KPV produced by PX1 Research is LAL-tested for bacterial endotoxins and guaranteed to contain less than 0.01 EU/mg, preventing background activation in immunological and cell culture assays.
How should KPV be reconstituted for in vitro research?
Reconstitution should be performed under sterile conditions using cell-culture-grade water or PBS (pH 7.4). After dissolving, stock solutions should be aliquoted and frozen at -80°C to prevent degradation.
Is KPV derived from alpha-MSH?
Yes, KPV represents the active C-terminal tripeptide fragment of alpha-melanocyte-stimulating hormone (α-MSH) that mediates anti-inflammatory signaling independently of melanogenesis.
What preclinical models are most commonly studied with KPV?
KPV is extensively studied in DSS- and TNBS-induced colitis rodent models, skin inflammatory assays, and in vitro Caco-2 epithelial barrier permeability studies.
Where does PX1 Research ship KPV orders from?
PX1 Research ships all research compounds same-day (Monday through Friday) directly from dispatch facilities located in California and Arizona.
Is KPV approved for human therapeutic or medical use?
No. KPV provided by PX1 Research is strictly designated for laboratory research use only (in vitro and preclinical animal research). It is not intended for human consumption, therapeutic, or clinical applications.
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.