In mammals and insects, this region is rich in odorant-binding proteins that are thought to aid olfaction by assisting mass transfer of the many different organoleptic compounds that make up the olfactory landscape. This protein is one of the best-characterized mammalian odorant-binding proteins and only the third such protein structure to be solved at high resolution. The protein was crystallized in the holo form and contains an unidentifiable ligand that is probably an artefact from the Pichia pastoris expression system. Comparisons are made between this structure and a modelled OBP1 structure produced using the crystal structure of aphrodisin as a template. Comparisons are also made between OBP1 and the other two rat OBP subtypes, for which crystallographic data are unavailable. OBP1 is monomeric, which is in contrast to its previous assignment.
Organism species: Rattus norvegicus (Rat)
CATALOG NO. | PRODUCT NAME | APPLICATIONS | |
Proteins | n/a | Recombinant Odorant Binding Protein 1 (OBP1) | Recombinant Protein Customized Service Offer |
Antibodies | n/a | Monoclonal Antibody to Odorant Binding Protein 1 (OBP1) | Monoclonal Antibody Customized Service Offer |
n/a | Polyclonal Antibody to Odorant Binding Protein 1 (OBP1) | Polyclonal Antibody Customized Service Offer | |
Assay Kits | n/a | CLIA Kit for Odorant Binding Protein 1 (OBP1) | CLIA Kit Customized Service Offer |
n/a | ELISA Kit for Odorant Binding Protein 1 (OBP1) | ELISA Kit Customized Service Offer |
- "Molecular cloning of odorant-binding protein: member of a ligand carrier family."Science 241:336-339(1988) [PubMed] [Europe PMC] [Abstract]
- "Structure of rat odorant-binding protein OBP1 at 1.6 A resolution."Acta Crystallogr. D 65:403-410(2009) [PubMed] [Europe PMC] [Abstract]