Orexin A, also known as Hypocretin-1, is a 33-residue neuropeptide with a highly constrained molecular architecture. The mature peptide contains an N-terminal pyroglutamate, two intramolecular disulfide bonds and a C-terminal amide.

The sequence is conserved across human, bovine, mouse and rat, allowing the same defined molecular form to be used in several mammalian research systems.

Product Information

A Bicyclic Orexin Scaffold

Four cysteine residues generate two crossed disulfide bridges, creating a compact N-terminal domain unlike the linear structure of Orexin B. Correct oxidative folding is therefore part of the molecular identity of Orexin A.

The N-terminal pyroglutamate further differentiates the mature peptide from unprocessed precursor sequences.

Dual Orexin Receptor Agonism

Orexin A is an endogenous agonist at both OX1R and OX2R and is generally more balanced between the receptor subtypes than Orexin B. This makes it useful as a reference ligand when receptor-selective analogs are evaluated.

Quality Considerations

For Orexin A, correct mass alone does not fully establish native structure because disulfide connectivity must also be correct. We recommend considering oxidative folding together with chromatographic purity and MS identity.

Our Peptide Quality Control capabilities can support analytical characterization.

Frequently Asked Questions

How many disulfide bonds are in Orexin A?

Two: Cys6-Cys12 and Cys7-Cys14.

Is the sequence conserved across human, mouse, rat and bovine?

Yes. This mature Orexin A sequence is conserved across these species.

Research Use Only.