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NORTHVERITY / VIP10

VIP10

10 mg × 10 vials

For laboratory procurement

VIP10 10 mg × 10 vials · VIP10 · Catalog illustration—not an actual packaging photo.
Catalog illustration—not an actual packaging photo.
Procurement details
Catalog number
VIP10
Listed specification
10 mg
Vials per pack
10 vials
Current supply lot
Lot documents with your quote

Compound profile

VIP is an amidated 28-residue peptide processed from a larger precursor and studied as a ligand of VPAC receptors.

Identity

Sequence
H-HSDAVFTDNYTRLRKQMAVKKYLNSILN-NH2
Residues
28
Molecular formula
C147H238N44O42S
Average molecular weight
3325.847 g/mol
Monoisotopic mass (calculated)
3323.7561 Da
CAS number
Not recorded
Strengths
5–10 mg
Other names
Vasoactive intestinal peptide

The sequence follows the amidated peptide in UniProt P01282. Opened PubChem name records described the free-acid form, so their CID and CAS were not assigned here. Formula and average weight were computed from the sourced sequence. SMILES was not verified.

Identity data from: UniProtKB P01282 · computed from the sequence

Residue diagram of VIP
Drawn from the verified identity data on this page.

Research overview

VIP is vasoactive intestinal peptide, a 28-residue peptide whose C-terminal asparagine is amidated. UniProt identifies it within a larger precursor that also contains other processed peptides. Receptor research describes VIP recognition by VPAC1 and VPAC2, members of the class B G-protein-coupled receptor family. The first cited review examines how the extracellular receptor domain contributes to ligand binding and how receptor activation connects to adenylyl cyclase. It brings together site-directed mutagenesis, photoaffinity labeling, nuclear magnetic resonance and molecular modeling. These methods address different aspects of the interaction between a peptide ligand and the receptor that recognizes it [1].

A subsequent structural study determined active receptor complexes by cryo-electron microscopy, including a VIP–VPAC1 receptor complex associated with Gs. Comparison with PACAP-containing complexes and molecular-dynamics analyses examined ligand binding and receptor selectivity. The resulting structures describe the arrangements captured in those experimental complexes, while simulations explore possible motions around them. This combination supplies a molecular framework for comparing related peptide–receptor systems. It does not mean that all members of the receptor family recognize each ligand in exactly the same way, or that precursor peptides and mature amidated VIP have identical molecular identities [2].

Laboratory storage and handling

Keep the sealed vial cold, dry and protected from light, following the conditions in the documentation supplied with the lot. Let the vial reach room temperature before opening to limit moisture condensation. Avoid repeated freezing and thawing of laboratory stocks. Record the lot identifier and the material form with each experiment, and use standard laboratory protective equipment.

Questions about VIP

Which terminal form is described here?

The sequence describes mature VIP with an amidated C-terminal asparagine, as annotated in UniProt P01282. It is distinct from the corresponding free-acid peptide.

Which receptor subtypes are discussed?

The review discusses the VPAC1 and VPAC2 subtypes within class B G-protein-coupled receptors, emphasizing ligand recognition, signaling and receptor-associated proteins [1].

What did the structural study examine?

The structural work examined active peptide–receptor complexes, including VIP with VPAC1 and Gs, using cryo-electron microscopy together with comparative analyses and molecular dynamics [2].

References

  1. VPAC receptors: structure, molecular pharmacology and interaction with accessory proteins. Br J Pharmacol 2012. PMID 21951273
  2. Understanding VPAC receptor family peptide binding and selectivity. Nat Commun 2022. PMID 36385145

Identity data checked on 2026-10-03. Literature summaries describe published research models and are not specifications of any product lot.

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2 catalog entries

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