• Description

  • Application Data


Bombesin is a widely expressed in the CNS and GI tract and has a wide range of physiological functions; contains N-terminal pyroglutamyl.

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Application Data

Catalogue number crb1000583
Molecular Weight 1618.8
Sequence (one letter code)


Sequence (three letter code)


Modifications where Pyr is pyroglutamyl
Purity >95%
cas 31362-50-2
Storage -20°C

Harti et al., (1989). Effects of capsaicin in rat and pigeon on peripheral nerves containing substance P and calcitonin gene-related peptide. Cell Tissue Res. 256(3): 465. doi: 10.1007/BF00225594.


Shimizu et al (2016) A Stress-Related Peptide Bombesin Centrally Induces Frequent Urination through Brain Bombesin Receptor Types 1 and 2 in the Rat. J. Pharmacol. Exp. Ther. 356(3) 693 PMID: 26729307

Sancho et al (2011) Bombesin Receptor-Mediated Imaging and Cytotoxicity: Review and Current Status. Curr. Drug Deliv. 8(1) 79 PMID: 21034419

Manufactured in: United Kingdom
Data Sheet Material Safety Data Sheet (MSDS)

Bombesin was originally isolated from the skin of the European fire-bellied toad (Bombina bombina) and has two known homologues in mammals; neuromedin B (NMB) and gastrin-releasing peptide (GRP).

Bombesin-like peptides are involved in many physiological functions including: regulation of food intake; anxiety and fear–related behaviour; thermoregulation; stress response; learning and memory and in the stimulation of smooth muscle contraction. Bombesin is also a tumour marker for small cell carcinoma in the lung; gastric cancer; pancreatic cancer, and neuroblastoma.

The receptors for these two peptides are G-protein-coupled receptors known as bombesin receptor type 1 (BB1; also known as NMB receptor) and bombesin receptor type 2 (BB2; also known as GRP- receptor). Bombesin shows high affinity to both of these receptor subtypes. These bombesin-like peptides and their receptors are widely distributed in the central nervous system (CNS) and gastrointestinal (GI) tract.

This peptide contains an N-terminal pyroglutamyl to prevent the intramolecular cyclisation of the N-terminal of glutamine to N‐pyroglutamate (pGlu).


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