Anti-Opioid δ Receptor antibody produced in rabbit

Opioid peptides are endogenous neuromodulators that play a major role in nociception by interacting with several membrane receptors. Molecular cloning techniques have characterized the nucleotide sequence of several distinct opioid receptors, including the δ-, κ- and μ-opioid receptors.¹ The cloned receptors are highly homologous (65%), differing only at the N- and C-termini and at the extracelluar loops that confer binding specificity. All three receptors interact with heterotrimeric G proteins.
δ-Opioid receptors (DOR) are located postsynaptically on pallidostriatal feedback neurons. DORs also modulate nociception presynaptically in the periaqueductal gray where immunolabeling of DOR has been shown to be intracellular and often associated with large dense-core vesicles. Additionally, receptor autoradiographic investigations have localized DORs to the external plexiform layer of the olfactory bulb, the nucleus accumbens, several layers of the cerebral cortex and several nuclei of the amygdala.

References
1. Goldstein, A. Trends Pharmacol. Sci., 8, 456-459 (1987).

Peptide corresponding to the carboxy-terminal of the opioid δ receptor covalently attached onto a carrier protein.

The antiserum is specific for the COOH terminal of the opioid δ receptor.

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