VIP
VIP
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Product details
VIP (vasoactive intestinal peptide) is a 28-amino-acid neuropeptide distributed across nervous and immune tissue. It belongs to the VPAC-receptor ligand class, signalling through two class B G-protein-coupled receptors, VPAC1 and VPAC2, both coupled to Gs and the generation of cyclic AMP.
In the published preclinical literature, VIP has been characterised at the molecular level for how it is recognised by these receptors: receptor-cloning and functional-expression work mapped its stimulation of adenylate cyclase and cyclic-AMP production in cultured cells, and cryo-electron-microscopy and molecular-dynamics studies resolved how the peptide inserts into the receptor binding cleft and the contacts that distinguish VPAC1, VPAC2, and the related PAC1 receptor. It is supplied as a research compound and is not intended for human or veterinary use.
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Research
VIP has been characterised in preclinical laboratory models. The primary studies below, in molecular-cloning, cultured-cell, and cell-free structural assays, recorded receptor-binding, adenylate-cyclase, and cyclic-AMP endpoints, with the work centred on how the peptide is recognised by its VPAC1 and VPAC2 receptors. The literature is preclinical; it describes the compound, not any outcome in humans.
3 preclinical studies indexed · receptor cloning and cyclic-amp signalling and receptor-family binding and selectivity (structural) · links open on PubMed
Receptor cloning and cyclic-AMP signalling 2 studies
In vitro
Functional expression and tissue distribution of a novel receptor for vasoactive intestinal polypeptide
A complementary-DNA clone for the VIP receptor was isolated and functionally expressed in cultured cells, where the peptide stimulated adenylate cyclase as the measured endpoint, placing the receptor in the Gs-protein-coupled class B family alongside the secretin receptor.
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In vitro
The VIP2 receptor: molecular characterisation of a cDNA encoding a novel receptor for vasoactive intestinal peptide
A second VIP receptor complementary-DNA was cloned and expressed in cultured COS-7 cells, where vasoactive intestinal peptide and the related peptides stimulated cyclic-AMP production; the cloned receptor shared roughly half its amino-acid sequence with the first VIP receptor as the measured molecular endpoint.
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Receptor-family binding and selectivity (structural) 1 study
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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