Camel β-Endorphin is a 31-residue endogenous opioid peptide with the sequence YGGFMTSEKSQTPLVTLFKNAIIKNAHKKGQ. This molecular form is also associated with closely related bovine and ovine β-Endorphin sequences.

Its conserved N-terminal opioid motif and characteristic His27/Gln31 C-terminal region make it a useful comparator for human and other species-specific β-Endorphins.

Product Information

A Conserved Camel/Bovine-Like Sequence

The camel sequence is highly conserved among several ungulate β-Endorphins. Compared with human β-Endorphin, the most conspicuous changes are His27 instead of Tyr27 and Gln31 instead of Glu31.

This allows experiments to focus on a relatively small C-terminal sequence difference while maintaining the same Met-enkephalin N-terminal domain.

C-Terminal Sequence and Peptide Identity

The final residues of β-Endorphin contribute to overall charge, protease susceptibility and molecular recognition. Camel β-Endorphin terminates in the neutral amide side-chain residue Gln rather than the acidic Glu found at position 31 in human β-Endorphin.

Species identity should therefore be retained in analytical and receptor studies rather than reporting all preparations simply as “β-Endorphin.”

Research Applications

Camel β-Endorphin can support comparative opioid pharmacology, POMC peptide research, species-sequence analysis and studies of C-terminal β-Endorphin structure–function relationships.

Frequently Asked Questions

Is camel β-Endorphin identical to human β-Endorphin?

No. Their N-terminal regions are highly conserved, but the C-terminal sequence differs at several positions.

Is this sequence shared with other species?

Closely matching sequences are reported for bovine and ovine β-Endorphins.

Research Use Only.