VIP
Also known as Vasoactive intestinal peptide, Vasoactive intestinal polypeptide
VIP is a 28-residue neuropeptide of the secretin/glucagon superfamily. A research-use profile: its neuropeptide-family lineage, receptor context, and how it's handled.
VIP — vasoactive intestinal peptide — is a genuine neuropeptide, not a fragment or a synthetic mimic. It was first characterized in the gut, which is where its name comes from, but it is now understood as a widely distributed signaling peptide with its own place in a well-defined family tree. That family membership is the right lens for understanding it.
This page describes the established facts: the peptide superfamily it belongs to, the receptor system it is studied through, and how it is handled in a lab. It does not make therapeutic or outcome claims.
VIP is a naturally occurring 28-amino-acid neuropeptide belonging to the secretin/glucagon peptide superfamily. It is a full-length neuropeptide rather than a fragment; at 28 residues its sequence is described here rather than enumerated to avoid transcription error.
A member of the secretin/glucagon superfamily
VIP is a 28-residue peptide that belongs to a related group of signaling peptides — the secretin/glucagon superfamily, which also includes secretin, glucagon, GHRH, and PACAP among others. Members of this superfamily share structural relationships and a common evolutionary origin, and PACAP in particular is a close relative of VIP.
This lineage is what makes VIP a 'neuropeptide' in the fullest sense: it is a native signaling molecule with defined family relatives, not a designed research construct. Naming its family is the most useful single fact for placing it, because so much of the comparative literature treats VIP and its superfamily neighbors together.
The VPAC receptor context
VIP is studied through its interaction with the VPAC receptors — VPAC1 and VPAC2 — which are G-protein-coupled receptors it shares with its close relative PACAP. Describing VIP through this receptor system is the standard way the research literature frames its signaling, and it is why VIP research often overlaps with PACAP research.
These receptors place VIP in neuroendocrine and vascular signaling research contexts. As always on this page, that describes where the peptide is studied — the systems and receptors involved — not any promised effect.
Handling a full-length neuropeptide
Because VIP is a native 28-residue neuropeptide rather than a short synthetic fragment, careful handling matters for reproducible characterization. A certificate of analysis should confirm the mass and a dominant chromatographic peak consistent with the intended 28-residue peptide, tied to a batch identifier. Every lot we list is tied to its own certificate — verify yours by its batch number.
These are research areas the compound is associated with in the literature — not medical claims or intended uses.
Handling & storage
Supplied lyophilized. Stored sealed and cold; reconstituted with bacteriostatic water only when a protocol requires it, then kept refrigerated. As a full-length neuropeptide it warrants careful, consistent handling — follow accepted laboratory practice and lot-specific guidance.
Verify a certificate by lot →Common questions
Vasoactive intestinal peptide (sometimes vasoactive intestinal polypeptide). It was first characterized in intestinal tissue, which is the origin of the name.
The secretin/glucagon superfamily, whose members include secretin, glucagon, GHRH, and PACAP. PACAP is a particularly close relative of VIP.
The VPAC receptors — VPAC1 and VPAC2 — which are G-protein-coupled receptors that VIP shares with its relative PACAP.
This monograph is a research-use reference. It describes composition and the contexts in which the compound has been studied — it is not medical advice, a description of effects, or a recommendation for use. Sold strictly for laboratory and research use; not for human or animal consumption.