Biotin-Bombesin is a biotin-labeled Bombesin analog designed for affinity-based detection and receptor-interaction studies.

The listed construct introduces an N-terminal Biotin-Glu structure while retaining the conserved amidated C-terminal Bombesin sequence associated with receptor interaction.

Product Information

Labeling Strategy

The C-terminal Bombesin region remains intact, while N-terminal chemistry differs from native pyroglutamate-containing Bombesin.

Positioning the biotin label away from the conserved C-terminal receptor-interacting sequence can support affinity-based workflows while preserving the principal peptide pharmacophore.

The modification still changes molecular mass and physicochemical behavior. We recommend treating labeled and unlabeled Bombesin as distinct experimental materials.

Research Applications

Biotin-Bombesin can support streptavidin capture, ligand–receptor interaction studies, peptide detection and development of GRPR-oriented assay systems.

Native and modified ligands can be compared within the Gastrin, GRP & Bombesin Peptides collection.

Experimental Planning

When receptor affinity or signaling is a quantitative endpoint, an unlabeled Bombesin reference can help determine whether biotinylation changes ligand behavior.

Alternative labeling positions, spacer designs and related conjugates can be evaluated through Chemical Peptide Synthesis.

Frequently Asked Questions

Is Biotin-Bombesin identical to native Bombesin?

No. N-terminal biotinylation changes the molecular structure and mass while retaining the principal C-terminal Bombesin sequence.

Should native Bombesin be included as a control?

We recommend an unlabeled reference when receptor affinity, signaling or internalization is measured quantitatively.

Research Use Only.