β-endorphin

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, rat (β-Lipotropin 61-91), a neuropeptide, plays a role in cardiovascular regulation and has been shown to cause significant, lasting muscular rigidity and immobility, akin to catatonia, in rats [1] [2].

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.

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

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].

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.

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

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].

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

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.

γ-1-MSH, amide acetate (72629-65-3 free base), a putative hormone in the N-terminal region of the ACTH/beta- endorphin (beta-EP) precursor protein, was studied by RIA with an antiserum against gamma 3-MSH in ACTH-producing mouse pituitary tumor cells, AtT-20/D16v.

[Tyr^0] Corticotropin Releasing Factor, ovine, is a hypothalamic hormone sourced from sheep that prompts the secretion of adrenocorticotropic hormone (ACTH) and β-endorphin [1] [2].

Dynorphins are a class of opioid peptides that arise from the precursor protein prodynorphin. When prodynorphin is cleaved during processing by proprotein convertase 2 (PC2), multiple active peptides are released: dynorphin A, dynorphin B, and α/β-neo-end

[DPro5] Corticotropin Releasing Factor, human, rat, a selective R2 agonist of corticotropin-releasing factor/hormone (CRF), is a hypothalamic hormone that prompts the release of adrenocorticotropic hormone (ACTH) and β-endorphin. Unlike typical agents, it does not induce anxiogenic effects but instead influences learning and memory processes in rats [1].