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DPDPE TFA is selective δ-opioid receptor agonist peptide. Inhibits electrically stimulated contraction of mouse vas deferens in vitro (EC50 = 5.2 nM), and is antinociceptive in vivo.

alpha-Endorphin acetate is related peptides of the pro-opiomelanocortin family with characteristic biological activities, were purified to homogeneity from single human pituitary.

β-Endorphin (1-27) (human) acetate, existing in the hypophysis cerebri and hypothalamus, exhibits antinociception activity. β-Endorphin (1-27) (human) acetate is an agonist of opioid receptor, showing preferred affinity for μ-opioid receptor and δ-opioid

N-Acetyl-α-Endorphin acetate is an acetylated α-Endorphin at N-terminal. α-Endorphin is an endogenous opioid peptide.

β-Endorphin (β-EP) is an endogenous opioid neuropeptide with diverse biological activities. It is produced via piomelanocortin cleavage in the pituitary gland, hypothalamus, and in lymphocytes, then migrates to its sites of action which include plasma, gut, skin, placenta, cerebrospinal fluid, and cardiac tissues. β-EP induces concentration-dependent decreases in electrically stimulated contraction of the mouse vas deferens that can be reversed by the μ-opioid antagonist CTP and δ-opioid antagonist ICI 174,864. In vivo, β-EP (5 μg, i.c.v.) slows gastrointestinal transit in mice. β-EP (0.5 or 5 μg, i.c.v.) stimulates food intake in rats for 4 to 6 hours, however, this effect is not prolonged with continuous infusion. It antagonizes the appetite-suppressive effects of α-melanocyte-stimulating hormone (α-MSH) for the first three days post administration. β-EP also reduces paralytic demyelination induced by the murine coronavirus MHV-JHM in immunocompetent, but not irradiated or immune-incompetent, mice and rats.

Acetyl β-endorphin (1-26) is a neuropeptide found in rat hippocampus, brain stem, and pituitary. It is also present in the human hypothalamus, where it comprises approximately 4.9% of total β-endorphin peptides. Acetyl β-endorphin (1-26) is produced through posttranslational processing of β-endorphin and is processed similarly in rat and human hypothalamus. Levels of acetyl β-endorphin (1-26) increase in the rat pars intermedia and brain stem following chronic administration of haloperidol .

β-Endorphin (1-27) is an endogenous peptide that binds to μ-, δ-, and κ-opioid receptors (Kis = 5.31, 6.17, and 39.82 nM, respectively, in COS-1 cells expressing rat receptors). It binds to rat and mouse brain membrane preparations (IC50s = 1.1 and 5.7 nM, respectively) and induces chemotaxis of human monocytes in vitro when used at a concentration of 1 nM. Intracerebroventricular administration of β-endorphin (1-27) increases the latency to tail withdrawal in response to thermal stimulation in mice with a median antinociceptive dose (AD50) of 1,500 pmol per animal. It inhibits antinociception induced by β-endorphin in mice in response to thermal stimuli when administered at a dose of 65 pmol per animal. In rats, β-endorphin (1-27) does not affect drug-associated place preference when administered at doses up to 20 μg, i.c.v., but inhibits β-endorphin-induced place preference when administered at a dose of 10 μg per animal.

Gonadorelin Acetate (33515-09-2 free base) (Luteinizing Hormone Releasing Hormone (LH-RH)) is hypothalamic neuropeptide which plays a key role in the control of reproductive functions.

β-Endorphin is an endogenous opioid neuropeptide and opioid receptor agonist that preferentially binds to μ-opioid receptors. Produced by specific neurons within the central and peripheral nervous system, it is one of three endorphins synthesized in humans. It functions to alleviate stress, maintain homeostasis, and regulate neurological pain perception [1].

β-Endorphin (1-27) (human) is an opioid antagonist that selectively binds to μ-, δ-, and κ-opioid receptors, with dissociation constants (Kis) of 5.31, 6.17, and 39.82 nM, respectively. It inhibits analgesia induced by both β-Endorphin and etorphine [1][2].

β-Endorphin, rat (β-Lipotropin 61-91), is a neuropeptide involved in cardiovascular regulation and induces significant, lasting muscular rigidity and immobility similar to catatonia in rats [1] [2].

β-Endorphin, equine (TFA) is an endogenous opioid peptide, which binds at high affinity to both μ/δ opioid receptors.

N-Acetyl-α-Endorphin is a chemical compound consisting of α-Endorphin that has been acetylated at the N-terminal. α-Endorphin, in turn, is an endogenous opioid peptide.

α-Neoendorphin (1-8) is an 8-amino acid peptide derived from the N-terminal of α-Neoendorphin, an endogenous opioid peptide. Part of the neoendorphins, these peptides are generated through the proteolytic cleavage of prodynorphin, isolated from porcine hypothalamus and pituitary.

Endorphin Beta is A substance produced in the brain, especially in the pituitary gland, Endorphin Beta blocks the sensation of pain. Endorphin Beta is produced in response to pain, exercise, and other forms of stress. Endorphin Beta belongs to a group of

beta-Neoendorphin acetate is an agonist of κ-opioid receptor

Veldoreotide, also known as Somatoprim, is a unique somatostatin receptor subtypes 2-, 4- and 5-selective analogue which effectively reduces GH secretion in human GH-secreting pituitary adenomas, even in Octreotide non-responsive tumours.

Acetyl-β-Endorphin (human) is a polypeptide identified through polypeptide screening, a research tool primarily using immunoassays to gather active polypeptides. This method is useful for protein interactions, functional analysis, antigen epitope screening, and particularly in the study and development of active molecules.

DALDA, a highly selective μ-opioid receptor agonist with a K_i value of 1.69 nM, exhibits potent antinociceptive (pain-relieving) and respiratory effects.

Dynorphin A TFA, an endogenous opioid peptide, plays a role in inhibitory neurotransmission within the central nervous system (CNS). It acts as a highly potent kappa opioid receptor (KOR) agonist and also stimulates other opioid receptors, including mu (MOR) and delta (DOR). Furthermore, Dynorphin A TFA has been observed to induce neuronal death, making it a significant subject in neurological disease research [1] [2].

CTAP TFA, a potent and highly selective μ opioid receptor antagonist that effectively crosses the blood-brain barrier, exhibits a significant inhibition concentration (IC50) of 3.5 nM. It demonstrates extraordinary selectivity, being over 1200-fold more specific to μ opioid receptors than to δ opioid (IC50 = 4500 nM) and somatostatin receptors. This compound is primarily leveraged for researching L-DOPA-induced dyskinesia (LID) and opiate overdose or addiction [1] [2].

Tianeptine metabolite MC5, an active derivative of the atypical antidepressant tianeptine produced through β-oxidation, exhibits selective G protein activation in bioluminescence resonance energy transfer (BRET) assays. Utilizing HEK293T cells expressing the human μ-opioid receptor (MOR) over the human δ-opioid receptor (DOR; EC50s = 0.454 and >100 µM, respectively), it demonstrates specificity. Moreover, this metabolite reduces immobility in wild-type mice during the forced swim test at a dose of 30 mg/kg, an effect not observed in MOR knockout mice, suggesting its antidepressant-like activity is MOR-dependent.

Potent and selective μ opioid receptor antagonist (IC50 = 3.5 nM). Displays > 1200-fold selectivity over δ opioid and somatostatin receptors. Brain penetrant and active in vivo.