📄 Certificate of Analysis available on request
Restock in progress. Add your email and we will tell you the moment this compound is back in stock.
One email when this is back in stock. No spam, unsubscribe anytime.
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.
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.
In vitro
Functional expression and tissue distribution of a novel receptor for vasoactive intestinal polypeptide
Ishihara et al. · 1992 · Neuron
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.
Read the study ↗
In vitro
The VIP2 receptor: molecular characterisation of a cDNA encoding a novel receptor for vasoactive intestinal peptide
Lutz et al. · 1993 · FEBS Letters
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.
Read the study ↗
Full documentation, on the record. A Certificate of Analysis and a Safety Data Sheet are available on request for every batch.
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.