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KPV (Lysine-Proline-Valine) is a synthetic tripeptide classified as a C-terminal fragment of alpha-melanocyte stimulating hormone (alpha-MSH), a tridecapeptide hormone that has been studied across multiple biological research domains including inflammatory signaling, immune regulation, and epithelial biology. The compound comprises three amino acids in the sequence lysine-proline-valine, corresponding to positions 11 through 13 of the parent alpha-MSH sequence, and was first identified and characterized in published scientific literature during research investigating the biologically active fragments of alpha-MSH and their independent receptor interaction profiles. In research environments, KPV is frequently studied in relation to inflammatory pathway signaling, melanocortin receptor interaction research, and cellular mechanisms associated with epithelial barrier function and mucosal biology in laboratory models. Scientists have explored its receptor binding characteristics and intracellular signaling behavior within controlled experimental models focused on inflammatory regulatory pathways, with particular attention to its studied capacity to interact with cellular signaling systems independently of the full-length parent hormone sequence.
Research Applications
KPV has been examined in several areas of laboratory research, including:
These research applications focus on understanding how synthetic tripeptide fragments derived from alpha-MSH interact with receptor systems and intracellular signaling networks involved in inflammatory regulatory pathways.
Mechanism and Pathway Context
Research has investigated KPV for its interaction with melanocortin receptor systems, specifically MC1R and MC3R receptor subtypes that are expressed across multiple tissue types and that published research has associated with inflammatory signal modulation in laboratory models. Studies have explored how this tripeptide interacts with receptor-independent intracellular signaling mechanisms that influence NF-kB pathway activity and downstream cytokine expression in cell culture research systems, with published findings suggesting that KPV interaction with these pathways does not require full melanocortin receptor activation in all experimental contexts examined.
In experimental settings, researchers analyze how KPV enters cells through peptide transporter mechanisms, with published research examining the role of the oligopeptide transporter PepT1 in facilitating intracellular accumulation of the tripeptide in intestinal epithelial cell research models. Laboratory investigations have examined how PepT1-mediated cellular uptake of KPV relates to its observed effects on inflammatory signaling pathway activity in these cell culture systems, with studies reporting that experimental conditions inhibiting PepT1 transporter activity attenuate the intracellular signaling observations associated with KPV in intestinal cell research models.
Laboratory investigations also evaluate how KPV interaction with intracellular signaling systems influences downstream inflammatory mediator expression, with published cell culture research examining changes in TNF-alpha, IL-6, IL-1 beta, and NF-kB pathway activity markers as primary experimental endpoints in inflammatory signaling research models. Studies have explored the concentration-dependent characteristics of these observations in cell culture systems, with published research reporting that nanomolar concentrations of KPV have been associated with measurable changes in inflammatory pathway marker expression in controlled experimental settings.
Research Summary
KPV was first identified and characterized as part of broader research into the biologically active fragments of alpha-MSH, following investigations into which portions of the parent hormone sequence retained inflammatory signaling activity independently of the full-length tridecapeptide structure. Early peptide research explored synthetic fragments of alpha-MSH to identify the minimal amino acid sequence responsible for the anti-inflammatory signaling properties observed in alpha-MSH research models, with the C-terminal tripeptide KPV emerging as a compound of significant research interest due to its studied receptor interaction profile and independence from melanotropic activity in experimental systems.
Scientific investigations have examined its biochemical characteristics, PepT1 transporter interaction activity, and intracellular inflammatory pathway signaling interactions within mucosal and epithelial cell culture research models. Published preclinical literature has explored KPV in rodent models of intestinal inflammation, with animal model studies examining inflammatory cell infiltration, mucosal integrity parameters, and cytokine expression markers as primary experimental endpoints in these preclinical systems.
Current research continues to explore how synthetic tripeptides derived from alpha-MSH interact with inflammatory receptor systems and intracellular signaling pathways, with KPV representing a well-documented subject of ongoing laboratory investigation across intestinal biology, skin biology, and inflammatory signaling research domains.
Product Specifications
Storage and Handling
This product is supplied as a lyophilized research peptide powder. For laboratory stability purposes, storage under refrigerated or frozen conditions is recommended following reconstitution, with long-term storage at -20 degrees Celsius or below appropriate for maintaining compound integrity in laboratory settings. Proper laboratory handling procedures should be followed to maintain compound integrity during research applications.
Research Use Disclaimer
FOR RESEARCH USE ONLY. This product is intended strictly for laboratory research purposes. It is not intended for human or veterinary use.
Scientific Background
KPV belongs to the class of alpha-MSH derived synthetic tripeptides, a subgroup of melanocortin peptide research compounds that emerged from investigations into the structural determinants of alpha-MSH biological activity in laboratory models. The glycine-histidine-lysine sequence of the parent hormone alpha-MSH was extensively characterized during research into melanocortin peptide biology in the 1980s and 1990s, with the identification of KPV as the C-terminal active fragment representing a significant finding in the published literature on minimal active sequences within neuropeptide hormones.
The alpha-MSH parent hormone belongs to the melanocortin peptide family derived from proopiomelanocortin (POMC), a precursor protein that gives rise to multiple biologically active peptide fragments including adrenocorticotropic hormone (ACTH), beta-endorphin, and the melanocyte stimulating hormones. KPV was identified during systematic research into the alpha-MSH sequence designed to determine which portions of the tridecapeptide structure were responsible for its studied anti-inflammatory signaling properties in experimental models, with published research characterizing its retention of inflammatory pathway signaling activity without the melanotropic effects associated with the full-length hormone in experimental systems.
Its classification as a tripeptide fragment rather than a full-length hormone makes it a useful tool in peptide structure-activity relationship research, allowing scientists to examine how minimal peptide sequences interact with intracellular signaling systems and receptor-independent cellular pathways in controlled laboratory models. The compound’s small molecular size and characterized relationship to the parent alpha-MSH hormone have made it a frequently studied research tool in investigations of inflammatory biology, epithelial barrier function, and melanocortin peptide pharmacology research.
Its studied interaction with the PepT1 transporter system has been of particular research interest, as this uptake mechanism provides a distinct cellular entry pathway that published research has examined in the context of intestinal epithelial cell biology and mucosal inflammatory signaling research models. [INTERNAL LINK: Melanocortin receptor signaling research]
Key Research Areas
Intestinal Inflammatory Signaling Research Laboratory studies have explored KPV as a model compound for examining melanocortin peptide fragment interaction with intestinal inflammatory signaling pathways and mucosal biology in controlled experimental models. Published research by Dalmasso and colleagues in Gastroenterology (2008) examined KPV in intestinal cell culture systems and rodent models of intestinal inflammation, reporting on NF-kB pathway activity, cytokine expression markers, and mucosal integrity parameters in these experimental systems. These investigations help researchers understand how synthetic alpha-MSH derived tripeptides interact with PepT1-mediated cellular uptake systems and downstream intracellular inflammatory signaling networks in intestinal research models.
Melanocortin Receptor and Intracellular Signaling Research Research has examined how KPV interacts with melanocortin receptor subtypes and receptor-independent intracellular signaling mechanisms in cell culture research systems, with published studies investigating the relationship between KPV cellular uptake and NF-kB pathway modulation in inflammatory cell models. These investigations help researchers understand how C-terminal fragments of alpha-MSH engage with intracellular signaling systems that regulate pro-inflammatory cytokine expression in controlled experimental settings, and how these interactions compare to the receptor pharmacology of the full-length parent hormone in laboratory research models.
Epithelial Barrier Function Research Laboratory studies have explored KPV in epithelial cell culture research models examining tight junction protein expression, transepithelial integrity parameters, and epithelial barrier function markers under inflammatory challenge conditions in controlled experimental settings. Published research has examined KPV in corneal epithelial research models, with investigators reporting on epithelial defect parameters and cellular recovery markers in experimental systems treated with the tripeptide relative to control conditions. These investigations help researchers understand how synthetic melanocortin peptide fragments interact with epithelial cell signaling systems involved in barrier function maintenance in laboratory models.
Antimicrobial Peptide Research Experimental models have explored KPV in antimicrobial research contexts, with published studies examining its interaction with bacterial and fungal research models including Staphylococcus aureus and Candida albicans experimental systems in controlled laboratory settings. These investigations help researchers understand how short synthetic peptide fragments derived from alpha-MSH interact with microbial cellular systems and how these interactions relate to the broader antimicrobial peptide research literature examining melanocortin-derived compounds in preclinical experimental models.
Pathway Interaction Overview
Research has examined KPV for its interaction with melanocortin receptor systems including MC1R and MC3R subtypes expressed in immune and epithelial cell populations, and for its studied engagement with PepT1-mediated transporter mechanisms that published research has examined as a cellular uptake pathway in intestinal epithelial cell research models.
Laboratory studies investigate how intracellular accumulation of KPV following PepT1-mediated uptake influences NF-kB pathway activity, IkB-alpha protein stability, and downstream pro-inflammatory cytokine expression in cell culture experimental systems, with published research reporting on these intracellular signaling parameters as primary mechanistic endpoints in inflammatory pathway research models.
Scientists analyze how KPV pathway interaction may influence downstream signaling events that regulate inflammatory mediator expression and epithelial cell signaling activity within the documented research contexts for this compound, providing researchers with mechanistic data across melanocortin peptide pharmacology, intracellular inflammatory signaling, and epithelial biology research domains.
Literature Overview
Scientific literature surrounding KPV addresses the intersection of melanocortin peptide fragment pharmacology, inflammatory signaling biology, and epithelial barrier function research, with the compound independently documented across preclinical and cell culture laboratory investigations spanning several decades of published scientific literature.
Key themes explored in laboratory research include:
These investigations help expand scientific understanding of how synthetic tripeptide fragments derived from alpha-MSH interact with intracellular inflammatory signaling systems and epithelial cell biology research models.
References
Researchers interested in the biochemical and signaling characteristics of KPV are encouraged to review peer reviewed publications within these scientific databases.
There are no reviews yet.
Only logged in customers who have purchased this product may leave a review.
KPV (Lysine-Proline-Valine) is a synthetic tripeptide classified as a C-terminal fragment of alpha-melanocyte stimulating hormone (alpha-MSH), a tridecapeptide hormone that has been studied across multiple biological research domains including inflammatory signaling, immune regulation, and epithelial biology. The compound comprises three amino acids in the sequence lysine-proline-valine, corresponding to positions 11 through 13 of the parent alpha-MSH sequence, and was first identified and characterized in published scientific literature during research investigating the biologically active fragments of alpha-MSH and their independent receptor interaction profiles. In research environments, KPV is frequently studied in relation to inflammatory pathway signaling, melanocortin receptor interaction research, and cellular mechanisms associated with epithelial barrier function and mucosal biology in laboratory models. Scientists have explored its receptor binding characteristics and intracellular signaling behavior within controlled experimental models focused on inflammatory regulatory pathways, with particular attention to its studied capacity to interact with cellular signaling systems independently of the full-length parent hormone sequence.
Research Applications
KPV has been examined in several areas of laboratory research, including:
These research applications focus on understanding how synthetic tripeptide fragments derived from alpha-MSH interact with receptor systems and intracellular signaling networks involved in inflammatory regulatory pathways.
Mechanism and Pathway Context
Research has investigated KPV for its interaction with melanocortin receptor systems, specifically MC1R and MC3R receptor subtypes that are expressed across multiple tissue types and that published research has associated with inflammatory signal modulation in laboratory models. Studies have explored how this tripeptide interacts with receptor-independent intracellular signaling mechanisms that influence NF-kB pathway activity and downstream cytokine expression in cell culture research systems, with published findings suggesting that KPV interaction with these pathways does not require full melanocortin receptor activation in all experimental contexts examined.
In experimental settings, researchers analyze how KPV enters cells through peptide transporter mechanisms, with published research examining the role of the oligopeptide transporter PepT1 in facilitating intracellular accumulation of the tripeptide in intestinal epithelial cell research models. Laboratory investigations have examined how PepT1-mediated cellular uptake of KPV relates to its observed effects on inflammatory signaling pathway activity in these cell culture systems, with studies reporting that experimental conditions inhibiting PepT1 transporter activity attenuate the intracellular signaling observations associated with KPV in intestinal cell research models.
Laboratory investigations also evaluate how KPV interaction with intracellular signaling systems influences downstream inflammatory mediator expression, with published cell culture research examining changes in TNF-alpha, IL-6, IL-1 beta, and NF-kB pathway activity markers as primary experimental endpoints in inflammatory signaling research models. Studies have explored the concentration-dependent characteristics of these observations in cell culture systems, with published research reporting that nanomolar concentrations of KPV have been associated with measurable changes in inflammatory pathway marker expression in controlled experimental settings.
Research Summary
KPV was first identified and characterized as part of broader research into the biologically active fragments of alpha-MSH, following investigations into which portions of the parent hormone sequence retained inflammatory signaling activity independently of the full-length tridecapeptide structure. Early peptide research explored synthetic fragments of alpha-MSH to identify the minimal amino acid sequence responsible for the anti-inflammatory signaling properties observed in alpha-MSH research models, with the C-terminal tripeptide KPV emerging as a compound of significant research interest due to its studied receptor interaction profile and independence from melanotropic activity in experimental systems.
Scientific investigations have examined its biochemical characteristics, PepT1 transporter interaction activity, and intracellular inflammatory pathway signaling interactions within mucosal and epithelial cell culture research models. Published preclinical literature has explored KPV in rodent models of intestinal inflammation, with animal model studies examining inflammatory cell infiltration, mucosal integrity parameters, and cytokine expression markers as primary experimental endpoints in these preclinical systems.
Current research continues to explore how synthetic tripeptides derived from alpha-MSH interact with inflammatory receptor systems and intracellular signaling pathways, with KPV representing a well-documented subject of ongoing laboratory investigation across intestinal biology, skin biology, and inflammatory signaling research domains.
Product Specifications
Storage and Handling
This product is supplied as a lyophilized research peptide powder. For laboratory stability purposes, storage under refrigerated or frozen conditions is recommended following reconstitution, with long-term storage at -20 degrees Celsius or below appropriate for maintaining compound integrity in laboratory settings. Proper laboratory handling procedures should be followed to maintain compound integrity during research applications.
Research Use Disclaimer
FOR RESEARCH USE ONLY. This product is intended strictly for laboratory research purposes. It is not intended for human or veterinary use.
Scientific Background
KPV belongs to the class of alpha-MSH derived synthetic tripeptides, a subgroup of melanocortin peptide research compounds that emerged from investigations into the structural determinants of alpha-MSH biological activity in laboratory models. The glycine-histidine-lysine sequence of the parent hormone alpha-MSH was extensively characterized during research into melanocortin peptide biology in the 1980s and 1990s, with the identification of KPV as the C-terminal active fragment representing a significant finding in the published literature on minimal active sequences within neuropeptide hormones.
The alpha-MSH parent hormone belongs to the melanocortin peptide family derived from proopiomelanocortin (POMC), a precursor protein that gives rise to multiple biologically active peptide fragments including adrenocorticotropic hormone (ACTH), beta-endorphin, and the melanocyte stimulating hormones. KPV was identified during systematic research into the alpha-MSH sequence designed to determine which portions of the tridecapeptide structure were responsible for its studied anti-inflammatory signaling properties in experimental models, with published research characterizing its retention of inflammatory pathway signaling activity without the melanotropic effects associated with the full-length hormone in experimental systems.
Its classification as a tripeptide fragment rather than a full-length hormone makes it a useful tool in peptide structure-activity relationship research, allowing scientists to examine how minimal peptide sequences interact with intracellular signaling systems and receptor-independent cellular pathways in controlled laboratory models. The compound’s small molecular size and characterized relationship to the parent alpha-MSH hormone have made it a frequently studied research tool in investigations of inflammatory biology, epithelial barrier function, and melanocortin peptide pharmacology research.
Its studied interaction with the PepT1 transporter system has been of particular research interest, as this uptake mechanism provides a distinct cellular entry pathway that published research has examined in the context of intestinal epithelial cell biology and mucosal inflammatory signaling research models. [INTERNAL LINK: Melanocortin receptor signaling research]
Key Research Areas
Intestinal Inflammatory Signaling Research Laboratory studies have explored KPV as a model compound for examining melanocortin peptide fragment interaction with intestinal inflammatory signaling pathways and mucosal biology in controlled experimental models. Published research by Dalmasso and colleagues in Gastroenterology (2008) examined KPV in intestinal cell culture systems and rodent models of intestinal inflammation, reporting on NF-kB pathway activity, cytokine expression markers, and mucosal integrity parameters in these experimental systems. These investigations help researchers understand how synthetic alpha-MSH derived tripeptides interact with PepT1-mediated cellular uptake systems and downstream intracellular inflammatory signaling networks in intestinal research models.
Melanocortin Receptor and Intracellular Signaling Research Research has examined how KPV interacts with melanocortin receptor subtypes and receptor-independent intracellular signaling mechanisms in cell culture research systems, with published studies investigating the relationship between KPV cellular uptake and NF-kB pathway modulation in inflammatory cell models. These investigations help researchers understand how C-terminal fragments of alpha-MSH engage with intracellular signaling systems that regulate pro-inflammatory cytokine expression in controlled experimental settings, and how these interactions compare to the receptor pharmacology of the full-length parent hormone in laboratory research models.
Epithelial Barrier Function Research Laboratory studies have explored KPV in epithelial cell culture research models examining tight junction protein expression, transepithelial integrity parameters, and epithelial barrier function markers under inflammatory challenge conditions in controlled experimental settings. Published research has examined KPV in corneal epithelial research models, with investigators reporting on epithelial defect parameters and cellular recovery markers in experimental systems treated with the tripeptide relative to control conditions. These investigations help researchers understand how synthetic melanocortin peptide fragments interact with epithelial cell signaling systems involved in barrier function maintenance in laboratory models.
Antimicrobial Peptide Research Experimental models have explored KPV in antimicrobial research contexts, with published studies examining its interaction with bacterial and fungal research models including Staphylococcus aureus and Candida albicans experimental systems in controlled laboratory settings. These investigations help researchers understand how short synthetic peptide fragments derived from alpha-MSH interact with microbial cellular systems and how these interactions relate to the broader antimicrobial peptide research literature examining melanocortin-derived compounds in preclinical experimental models.
Pathway Interaction Overview
Research has examined KPV for its interaction with melanocortin receptor systems including MC1R and MC3R subtypes expressed in immune and epithelial cell populations, and for its studied engagement with PepT1-mediated transporter mechanisms that published research has examined as a cellular uptake pathway in intestinal epithelial cell research models.
Laboratory studies investigate how intracellular accumulation of KPV following PepT1-mediated uptake influences NF-kB pathway activity, IkB-alpha protein stability, and downstream pro-inflammatory cytokine expression in cell culture experimental systems, with published research reporting on these intracellular signaling parameters as primary mechanistic endpoints in inflammatory pathway research models.
Scientists analyze how KPV pathway interaction may influence downstream signaling events that regulate inflammatory mediator expression and epithelial cell signaling activity within the documented research contexts for this compound, providing researchers with mechanistic data across melanocortin peptide pharmacology, intracellular inflammatory signaling, and epithelial biology research domains.
Literature Overview
Scientific literature surrounding KPV addresses the intersection of melanocortin peptide fragment pharmacology, inflammatory signaling biology, and epithelial barrier function research, with the compound independently documented across preclinical and cell culture laboratory investigations spanning several decades of published scientific literature.
Key themes explored in laboratory research include:
These investigations help expand scientific understanding of how synthetic tripeptide fragments derived from alpha-MSH interact with intracellular inflammatory signaling systems and epithelial cell biology research models.
References
Researchers interested in the biochemical and signaling characteristics of KPV are encouraged to review peer reviewed publications within these scientific databases.
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