Product Title: KPV X 10mg
URL handle: kpv-10mg-biolongevity-labs
SKU: KPV-10MG
Brand: Biolongevity Labs
Current URL: https://fmihealth.com/products/kpv-10mg-biolongevity-labs
Meta Title: KPV X 10mg
Meta Description: Description--KPV is the C‑terminal tripeptide fragment of α‑melanocyte stimulating hormone (α‑MSH). As a small, bioactive peptide, it reproduces many of α‑MSH’s anti‑inflammatory, antimicrobial, and tissue‑protective activities, while avoiding full‑length melanocortin receptor signaling in certain contexts. Its compact
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Description HTML:
<p>Description--<!--StartFragment -->KPV is the C‑terminal tripeptide fragment of α‑melanocyte stimulating hormone (α‑MSH). As a small, bioactive peptide, it reproduces many of α‑MSH’s anti‑inflammatory, antimicrobial, and tissue‑protective activities, while avoiding full‑length melanocortin receptor signaling in certain contexts. Its compact structure makes it a useful research tool for studying innate immune regulation, mucosal defense, and novel anti‑inflammatory mechanisms.</p> <p> </p> <p><strong>Mechanistic Claims</strong></p> <ul> <li> <strong>Anti‑Inflammatory Action:</strong> Suppresses pro‑inflammatory cytokines and leukocyte activation.</li> <li> <strong>Antimicrobial Activity:</strong> Exhibits candidacidal and bactericidal effects, reported for α‑MSH C‑terminal fragments including KPV.</li> <li> <strong>Mucosal &amp; Epithelial Protection:</strong> Accelerates epithelial repair in corneal and other epithelial models.</li> <li> <strong>Anti‑Fibrotic &amp; Immunomodulatory Effects:</strong> Reduces fibrosis and shifts macrophage phenotypes in preclinical studies.</li> <li> <strong>Innate Immune Regulation:</strong> Provides a simplified model for studying α‑MSH‑derived peptide activity.</li> </ul> <p> </p> <p><strong>Research Applications</strong></p> <ul> <li>Inflammation and cytokine modulation studies</li> <li>Antimicrobial peptide research (fungal and bacterial models)</li> <li>Mucosal defense and epithelial wound healing investigations</li> <li>Fibrosis and macrophage phenotype modulation studies</li> <li>Exploratory therapeutic models in immune regulation</li> </ul> <p> </p> <p><strong>KPV Research Insights</strong></p> <ul> <li>Small tripeptide fragment (Lys–Pro–Val) derived from α‑MSH.</li> <li>Retains many anti‑inflammatory and antimicrobial properties of the parent hormone.</li> <li>Studied for roles in immune modulation, wound healing, and tissue protection.</li> <li>Evidence remains largely preclinical, with promising activity in epithelial and immune models.</li> <li>Provided in lyophilized form (freeze‑dried, filler‑free) to preserve purity and shelf life.</li> </ul> <p><!--EndFragment --><br></p> <p><strong>Research Overview</strong></p> <p>KPV (Lys-Pro-Val) is a C-terminal tripeptide fragment of alpha-melanocyte-stimulating hormone (alpha-MSH, positions 11-13) that has been studied for its anti-inflammatory properties in laboratory settings. Research demonstrates KPV operates through melanocortin receptor-independent pathways, making it distinct from its parent molecule.</p> <p> </p> <p><strong>Molecular Mechanisms</strong></p> <p>KPV enters cells via the PepT1 oligopeptide transporter with high affinity (Km ~160 μM in Caco2 cells). Studies show the peptide accumulates in the nucleus within 5 hours, where it competitively disrupts the interaction between p65RelA and importin-α3, blocking NFκB nuclear translocation.^[1]</p> <p>At nanomolar concentrations (10 nM), KPV also suppresses all three major MAPK subfamilies (ERK1/2, JNK, p38) in intestinal epithelial cells. This mechanism occurs independently of melanocortin receptors and reduces inflammatory cytokine expression.^[2]</p> <p> </p> <p><strong>Gastrointestinal Inflammation Models</strong></p> <p>Oral KPV administration in murine DSS and TNBS colitis models demonstrated significant reductions in:</p> <ul> <li> <p>Colonic myeloperoxidase activity (~50% decrease, p&lt;0.05)</p> </li> <li> <p>Pro-inflammatory cytokine mRNA (IL-6, IL-12, TNF-α, IFN-γ)</p> </li> <li> <p>Epithelial damage and inflammatory cell infiltration</p> </li> <li> <p>Body weight loss and colon shortening</p> </li> </ul> <p>Research indicates KPV’s efficacy correlates with PepT1 expression, which becomes upregulated in inflamed colonic epithelium and immune cells during IBD (inflammatory bowel disease).^[1]</p> <p> </p> <p><strong>Airway and Pulmonary Studies</strong></p> <p>In bronchial epithelial cells (16HBE14o-), KPV reduced TNFα-induced inflammatory responses:</p> <ul> <li> <p>NFκB reporter activity decreased at concentrations ≥1 μg/ml</p> </li> <li> <p>IL-8 mRNA reduced by ~35% (p&lt;0.05)</p> </li> <li> <p>MMP-9 gelatinolytic activity returned to baseline levels</p> </li> <li> <p>Eotaxin secretion significantly attenuated</p> </li> </ul> <p>These findings suggest potential applications in respiratory inflammation research models.^[2]</p> <p> </p> <p><strong>Immune Cell Modulation</strong></p> <p>Human Jurkat T cells and intestinal immune populations express functional PepT1, enabling KPV uptake. Studies demonstrate that 10 nM KPV stabilizes IκBα protein levels and reduces IL-8 transcription by ~40% following TNFα stimulation.</p> <p>During inflammatory conditions, PepT1 expression increases in lamina propria macrophages and peripheral T cells, providing disease-activated delivery pathways for peptide-based research tools.^[1]</p> <p> </p> <p><strong>Dermatological Research</strong></p> <p>KPV retains anti-inflammatory activity without activating MC1R, the melanogenesis receptor. This property makes it useful for skin inflammation research where pigmentation effects would confound results.^[3]</p> <p>Stereoisomers like KdPT (Lys-D-Pro-Thr) show enhanced proteolytic stability. Research on sebocytes demonstrated KdPT suppresses IL-1β-mediated cytokine signaling, relevant to acne pathogenesis studies.</p> <p> </p> <p><strong>Structure-Activity Relationships</strong></p> <p>The tripeptide KPV represents the minimal α-MSH sequence retaining anti-inflammatory activity. Deletion studies confirm truncation beyond KPV eliminates efficacy.^[4]</p> <p>D-amino acid substitutions (KdPV, KPdV, dKPV) preserve activity while enhancing proteolytic resistance. Glycoalkylation of the lysine residue increases stability but eliminates antimicrobial properties, demonstrating structure-dependent bioactivity profiles.^[5]</p> <p><strong>Research Use Only:</strong><span> </span>KPV is intended for in vitro laboratory research and experimental protocols. All findings referenced represent preclinical research models and are not validated for therapeutic applications.</p> <p>References</p> <ol> <li>Dalmasso G, Charrier–Hisamuddin L, Thu Nguyen HT, Yan Y, Sitaraman S, Merlin D. PepT1-Mediated Tripeptide KPV Uptake Reduces Intestinal Inflammation. Elsevier BV; 2008.<span> </span><a href="https://doi.org/10.1053/j.gastro.2007.10.026" rel="noopener" target="_blank">https://doi.org/10.1053/j.gastro.2007.10.026</a> </li> <li>Land S. Inhibition of cellular and systemic inflammation cues in human bronchial epithelial cells by melanocortin-related peptides: mechanism of KPV action and a role for MC3R agonists. International Journal of Physiology, Pathophysiology and Pharmacology 2012;4 2:59–73.</li> <li>Böhm M, Luger T. Are melanocortin peptides future therapeutics for cutaneous wound healing?. Wiley; 2019.<span> </span><a href="https://doi.org/10.1111/exd.13887" rel="noopener" target="_blank">https://doi.org/10.1111/exd.13887</a> </li> <li>Luger TA, Brzoska T. α-MSH related peptides: a new class of anti-inflammatory and immunomodulating drugs. Elsevier BV; 2007.<span> </span><a href="https://doi.org/10.1136/ard.2007.079780" rel="noopener" target="_blank">https://doi.org/10.1136/ard.2007.079780</a> </li> <li>Songok AC, Panta P, Doerrler WT, Macnaughtan MA, Taylor CM. Structural modification of the tripeptide KPV by reductive “glycoalkylation” of the lysine residue. Public Library of Science (PLoS); 2018.<span> </span><a href="https://doi.org/10.1371/journal.pone.0199686" rel="noopener" target="_blank">https://doi.org/10.1371/journal.pone.0199686</a> </li> </ol> <p><br>Label--</p> <table> <thead> <tr> <th>Property</th> <th>Value</th> </tr> </thead> <tbody> <tr> <td>Peptide Sequence</td> <td>Lys-Pro-Val (H-Lys-Pro-Val-OH)</td> </tr> <tr> <td>Molecular Formula</td> <td>C16H30N4O4</td> </tr> <tr> <td>Molecular Weight</td> <td>342.43 g/mol</td> </tr> <tr> <td>CAS Number</td> <td>67727-97-3</td> </tr> <tr> <td>PubChem CID</td> <td>125672</td> </tr> <tr> <td>Synonyms</td> <td>α-MSH(11-13), ACTH(11-13), MSH(11-13)</td> </tr> </tbody> </table> <p> </p> <p>Dosage--<strong>This PRODUCT IS INTENDED AS A RESEARCH CHEMICAL ONLY.</strong><span> This designation allows the use of research chemicals strictly for in vitro testing and laboratory experimentation only. All product information available on this website is for educational purposes only.  This product should only be handled by licensed, qualified professionals. This product is not a drug, food, or cosmetic and may not be misbranded, misused or mislabeled as a drug, food or cosmetic.</span></p>

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