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Human β-Endorphin is a 31-residue endogenous opioid peptide derived from pro-opiomelanocortin. Its N-terminal Tyr-Gly-Gly-Phe-Met sequence is identical to Met-enkephalin, while the remaining 26 residues create a substantially larger ligand with receptor and processing properties distinct from the isolated pentapeptide.
As the native human sequence, β-Endorphin provides an important reference ligand for opioid receptor pharmacology and POMC-derived peptide biology.
Product Information
| Property | Specification |
|---|---|
| Product Name | β-Endorphin, Human |
| Catalog No. | AS2600 |
| CAS No. | 61214-51-5 |
| Sequence | Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-Ser-Gln-Thr-Pro-Leu-Val-Thr-Leu-Phe-Lys-Asn-Ala-Ile-Ile-Lys-Asn-Ala-Tyr-Lys-Lys-Gly-Glu |
| One-Letter Sequence | YGGFMTSEKSQTPLVTLFKNAIIKNAYKKGE |
| Peptide Length | 31 amino-acid residues |
| Molecular Formula | C158H251N39O46S |
| Molecular Weight | Approximately 3465.0 Da |
| C-Terminus | Glu-OH |
| Precursor | POMC / β-lipotropin |
Met-Enkephalin Motif within a Larger Endogenous Ligand
The first five residues of β-Endorphin form the canonical Met-enkephalin sequence. The additional C-terminal residues alter receptor interaction, peptide lifetime and enzymatic processing, so full-length β-Endorphin should not be treated as simply a longer version of Met-enkephalin.
Activity across the Opioid Receptor Family
Curated pharmacological data show that β-Endorphin can activate μ, δ and κ opioid receptors. Strong μ- and δ-receptor activity has been documented, while κ activity is more assay- and species-dependent.
We recommend stating the specific receptor and species whenever quantitative affinity or signaling data are compared.
Human Sequence as a Comparative Reference
Human β-Endorphin differs from several non-human forms mainly in the C-terminal region. Tyr27 and Glu31 are particularly useful sequence markers when the human peptide is compared with camel, equine or porcine β-Endorphin.
The human sequence can therefore serve as a reference for natural species variation as well as truncation and processing studies.
Research Applications
Applications include opioid receptor signaling, ligand binding, neuroendocrine research, POMC processing, peptide degradation and comparative β-Endorphin structure–activity studies.
Related endogenous opioid peptides can be explored in our Neurotransmitters & Neuropeptides collection.
Frequently Asked Questions
How many residues are in human β-Endorphin?
The intact human peptide contains 31 amino-acid residues.
Does the sequence contain Met-enkephalin?
Yes. Residues 1-5 are Tyr-Gly-Gly-Phe-Met, the Met-enkephalin sequence.