KISSPEPTIN
KISSPEPTIN
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Product details
Kisspeptin is a peptide encoded by the KISS1 gene and the natural ligand of KISS1R, the G protein coupled receptor formerly known as GPR54. It belongs to the receptor-binding RFamide peptide class.
In the published preclinical literature, kisspeptin has been characterised at the molecular and cellular level as an agonist at the KISS1R (GPR54) receptor: in cell-based assays it binds and activates the receptor and engages phospholipase C, calcium, and MAP-kinase signalling, and in rodent brain-slice electrophysiology it acts on the ion channels of gonadotropin-releasing-hormone neurons. It is supplied as a research compound and is not intended for human or veterinary use.
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supplied for laboratory research only
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Research
Kisspeptin has been characterised in preclinical laboratory models. The primary studies below, in cultured cells and in rodent brain-slice electrophysiology, measured receptor-binding and receptor-activation endpoints at the KISS1R (GPR54) receptor and the ion-channel behaviour of gonadotropin-releasing-hormone neurons. The literature is preclinical; it describes the compound, not any outcome in humans.
3 preclinical studies indexed · receptor binding and activation and ion-channel mechanism in neurons · links open on PubMed
Ion-channel mechanism in neurons 2 studies
Animal model
Kisspeptin excites gonadotropin-releasing hormone neurons through a phospholipase C and calcium-dependent pathway regulating multiple ion channels
In acute brain slices from transgenic mice, perforated-patch electrophysiology and calcium imaging recorded the firing of gonadotropin-releasing-hormone neurons and mapped the kisspeptin response to a phospholipase C and calcium-dependent pathway acting on multiple ion channels as electrophysiological endpoints.
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Animal model
Kisspeptin depolarizes gonadotropin-releasing hormone neurons through activation of TRPC-like cationic channels
In mouse brain slices, voltage-clamp and current-clamp recordings measured a concentration-dependent depolarisation of gonadotropin-releasing-hormone neurons, with the underlying current traced to the inhibition of inwardly rectifying potassium channels and the activation of TRPC-like cationic channels as measured endpoints.
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Links open the original study on PubMed. For research and educational purposes, descriptive of the published preclinical literature, not therapeutic claims about any ai-peptides product. A Certificate of Analysis and a Safety Data Sheet are available on request for every batch.
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