VIP – Research-Grade Vasoactive Intestinal Peptide

Vasoactive Intestinal Peptide (VIP) is a synthetic research analog of an endogenous neuropeptide composed of 28 amino acid residues and belonging to the secretin–glucagon peptide family. VIP is structurally characterized by a linear peptide backbone and a C-terminal amidation that influences its biochemical behavior. In laboratory research settings, VIP is utilized as a reference material for studying neuropeptide signaling models, peptide–receptor interaction dynamics, and comparative structure–function relationships within secretin-family peptides.

Due to its defined sequence and moderate peptide length, VIP exhibits physicochemical properties that differ from both short regulatory peptides and larger protein hormones. This enables researchers to examine receptor-mediated signaling, peptide stability, and degradation behavior in vitro without the complexity introduced by multi-domain proteins. Its consistent synthetic composition supports controlled use in mechanistic assays, comparative peptide studies, and exploratory biochemical research conducted under controlled laboratory conditions.