$121.00 - $121.00
Rat β-Endorphin is a 31-residue endogenous opioid peptide generated from the pro-opiomelanocortin (POMC) pathway. Its N-terminal Tyr-Gly-Gly-Phe-Met sequence corresponds to the Met-enkephalin opioid motif, while the extended C-terminal region contributes additional receptor and processing properties that distinguish the intact peptide from shorter enkephalins.
The rat sequence provides a species-matched ligand for rodent opioid-receptor, pituitary and neuroendocrine studies.
Product Information
| Property | Specification |
|---|---|
| Product Name | β-Endorphin, Rat |
| Catalog No. | AS2602 |
| CAS No. | 77367-63-6 |
| 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-Val-His-Lys-Lys-Gly-Gln |
| One-Letter Sequence | YGGFMTSEKSQTPLVTLFKNAIIKNVHKKGQ |
| Peptide Length | 31 amino-acid residues |
| Molecular Formula | C157H254N42O44S |
| Molecular Weight | Approximately 3466.1 Da |
| C-Terminus | Gln-OH |
| Precursor | POMC / β-lipotropin |
| Receptor Context | μ, δ and κ opioid receptors |
Rodent-Specific C-Terminal Sequence
The N-terminal 25 residues of rat and human β-Endorphin are highly conserved, but the rat peptide diverges toward the C-terminus. Rat β-Endorphin contains Val26, His27 and Gln31, whereas the human sequence contains Ala26, Tyr27 and Glu31.
These substitutions make the rat form preferable when species-dependent opioid signaling, peptide metabolism or receptor responses are being examined in rodent systems.
Opioid Receptor Pharmacology
β-Endorphin is not a single-receptor-selective ligand. Curated pharmacological data support activity at μ, δ and κ opioid receptors, with receptor potency depending on species, assay format and receptor background.
We recommend identifying the receptor subtype experimentally rather than describing β-Endorphin simply as a μ-selective agonist.
POMC Processing Research
β-Endorphin is generated through proteolytic processing of POMC-derived β-lipotropin. Additional C-terminal cleavage can generate shorter molecular forms with different biological properties.
The intact 31-residue rat peptide can therefore serve as a reference when studying precursor processing, peptide degradation or truncated β-Endorphin products.
Analytical Considerations
The sequence contains Met5, making methionine oxidation a relevant LC-MS variable. For receptor and processing studies, intact molecular mass and chromatographic purity should be considered together.
Our Peptide Quality Control capabilities support analytical HPLC and mass spectrometry according to the selected specification.
Frequently Asked Questions
Is rat β-Endorphin identical to human β-Endorphin?
No. Both contain 31 residues, but several residues in the C-terminal region differ.
Does rat β-Endorphin act only at μ-opioid receptors?
No. β-Endorphin can interact with μ, δ and κ opioid receptors, with relative activity depending on the experimental system.