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Vasoactive Intestinal Peptide is a neuropeptide composed of 28 amino acids. It was originally isolated from intestinal tissue and belongs to the glucagon/secretin superfamily of signaling peptides. Since its discovery in 1970, VIP has been studied extensively in controlled experimental settings for its potential influence on smooth muscle relaxation, receptor signaling, and immune regulation.
Said S.I., Mutt V. (1970).
The peptide was first isolated by Sami Said and Viktor Mutt from porcine small intestine, initially characterized by its vasodilatory activity. Early experiments focused on its structural relationship to secretin and glucagon and on its broad range of physiological actions. Over time, studies broadened into neural, respiratory, endocrine, and immune systems, where VIP consistently demonstrated properties of interest in the context of molecular signaling and biological regulation.
Said S.I., Mutt V. (1972).
VIP Structure

CAS #: 40077-57-4
Molecular Formula: C₁₄₇H₂₃₈N₄₄O₄₂S
Molecular Weight: 3325.8 g/mol
PubChem ID: 53314964
VIP has been studied in vascular, gastrointestinal, neural, and immune models, with reports of activity in smooth muscle relaxation, cyclic AMP signaling, cytokine modulation, and circadian regulation. Research also highlights signaling roles in preclinical systems, supporting cellular integrity and pathway dynamics. Key Areas of Research:
Vascular: Vasodilation, smooth muscle, blood flow
Gastrointestinal: Secretion, motility, epithelium
Neural: VPAC receptors, cyclic AMP, circadian
Immune: Cytokine modulation, T cells, anti-inflammatory
Together, these findings suggest broad experimental utility for VIP across multiple biological pathways. Its activity in vascular, gastrointestinal, neural, and immune models provides a foundation for exploring diverse aspects of molecular biology. By influencing processes such as smooth muscle relaxation, receptor signaling, and immune modulation, VIP offers a versatile platform for research into pathway dynamics and systemic resilience within experimental settings.
Delgado M., Ganea D., Amino Acids, 2013
References
Said S.I., Mutt V. (1970). Polypeptide with broad biological activity: isolation from small intestine.
Said S.I., Mutt V. (1972). Isolation from porcine intestinal wall of a vasoactive octacosapeptide related to secretin and to glucagon.
Delgado M., Ganea D. (2013). Vasoactive intestinal peptide: a neuropeptide with pleiotropic immune functions.
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