Bombesin is a 14-amino-acid C-terminally amidated peptide originally identified in amphibian tissue and widely used in experimental studies of bombesin-family receptors.

Its C-terminal sequence is closely related to the receptor-active region of mammalian gastrin-releasing peptide (GRP), making Bombesin a useful ligand for GRPR pharmacology and comparative peptide–receptor studies.

Product Information

Bombesin Receptor Pharmacology

The C-terminal Trp-Ala-Val-Gly-His-Leu-Met-NH₂ region is highly related to the corresponding receptor-interacting region of mammalian GRP.

Bombesin is therefore widely used as a pharmacological ligand in studies involving GRPR/BB2 and related bombesin-family receptor systems.

Human GRP remains a distinct endogenous mammalian ligand, so the two peptides should not be treated as chemically interchangeable.

Research Applications

Bombesin can support receptor-binding assays, GPCR signaling studies, ligand internalization experiments and development of receptor-targeted peptide constructs.

Researchers comparing Bombesin with GRP or labeled derivatives can explore the Gastrin, GRP & Bombesin Peptides collection.

Experimental Considerations

C-terminal amidation and N-terminal pyroglutamate are part of the defined Bombesin structure. These features should be confirmed when comparing synthetic preparations or modified analogs.

For quantitative assays, our Peptide Quality Control capabilities support HPLC and mass-spectrometric characterization according to the selected specification.

Frequently Asked Questions

Is Bombesin the endogenous human GRPR ligand?

No. Human GRP is an endogenous mammalian ligand. Bombesin is an amphibian peptide with related receptor pharmacology.

Can Bombesin analogs be synthesized?

Sequence substitutions, labeling, spacers and conjugation strategies can be evaluated through Chemical Peptide Synthesis.

Research Use Only.