Prolactin-releasing peptide
The brain peptide named for prolactin that turned out to act mostly on appetite, stress and blood pressure in animal work
Prolactin-releasing peptide (PrRP) was found in 1998 as the natural partner of the pituitary receptor GPR10 and named for its ability to release prolactin from rat pituitary cells. It comes in two lengths, PrRP31 and PrRP20. Later work showed it is a weak prolactin trigger and acts mainly in the brain: in rats and mice it signals fullness after meals, switches on the stress hormone system and raises blood pressure. In people it has only been measured, in brain, adrenal and pregnancy tissue. It is not a medicine and has no human dose.
No established human dose Details ↓
Recommended Dosing
No established human dose
Prolactin-releasing peptide has never been given to people in any study read. The human evidence is measurement only: radioimmunoassay of post-mortem brain and adrenal tissue, gene-message studies of pituitary, placenta and decidua, and experiments on human pituitary and decidual cells in culture.
Work out syringe units → · New to syringes? · All dosing data ↓ · Dose and vial tracker · Is this vial OK?
What is it?
Prolactin-releasing peptide, usually shortened to PrRP, is a brain peptide found in 1998 by researchers looking for the natural partner of an orphan receptor, hGR3, that is made in the human pituitary. The receptor is now called GPR10. The team isolated the matching peptide from hypothalamus, found that it resembled no known protein, and named it after the first thing they saw it do: make rat pituitary cells release prolactin. It works in two lengths cut from the same 87-residue precursor, which is coded by the PRLH gene. PrRP31 is the long form, and PrRP20 is simply its last 20 residues. Both end in arginine and phenylalanine with an amidated tail, the RF-amide ending that puts PrRP in the same family as neuropeptide FF.
The name has not aged well. Injected into a vein, PrRP31 did raise prolactin in rats, more in females than in males, without touching the other pituitary hormones. But it was several times weaker than thyrotropin-releasing hormone (TRH), the better-known prolactin trigger, and its nerve fibres do not reach the outer layer of the median eminence, where true releasing hormones are handed to the pituitary's blood supply. On human tissue the picture was similar: it raised prolactin output from fetal pituitary cultures by about a third, less than TRH did, and left prolactin-secreting tumour cells alone. In rat work it also made the pituitary respond far more strongly to TRH when the two were given together.
Most of the work since 2000 treats PrRP as a brain signal for fullness and stress. Neurons that make it in the brainstem switch on after a meal, and mice lacking either the peptide or GPR10 eat larger meals and become obese later in life, with weaker responses to the satiety hormone cholecystokinin and to leptin. Given into the brain of rats it cut food intake and raised heat production, though the animals stopped responding after about three days of repeated injections. The same route switched on the stress hormone pathway, raised oxytocin, raised blood pressure and heart rate through neuropeptide FF receptors rather than GPR10, woke sleeping rats and quietened absence-seizure activity in an epilepsy strain.
In people, PrRP has only been measured. A radioimmunoassay of post-mortem brain found it mainly in the hypothalamus, the medulla and the thalamus and not in the frontal or temporal cortex, with both lengths present. Its message has been found in normal pituitary and in some pituitary tumours, in placenta and decidua across pregnancy, and the peptide itself in adrenal tissue and some adrenal tumours. Blood levels in rats were tiny, around a tenth of a femtomole per millilitre, and no study read measured it in human blood. Nothing in these studies shows what a high or low PrRP level would mean for a person.
Prolactin-releasing peptide is not a medicine and has never been given to a person in any study read, so there is no human dose. Because appetite peptides like this one do little when injected outside the brain, groups developing it for obesity have attached fatty acid chains to it, as in palmitoylated PrRP31; these lipidized analogues lowered food intake and weight in obese mice, but they are different molecules with their own properties, so their studies sit under References rather than as cards here.
Mechanism of Action
PrRP is cut from a precursor made mainly in brainstem and hypothalamic neurons and acts through its own receptor, GPR10, and through neuropeptide FF receptors; the effects below come from rat and mouse work and from cultured cells.
Two lengths, one RF-amide end
PrRP31 and PrRP20 come from one PRLH precursor and share an amidated arginine-phenylalanine tail, which sits in a conserved pocket of GPR10 in cryo-EM structures.
A fullness signal in the brainstem
Brainstem PrRP neurons fire after meals and are needed for cholecystokinin to reduce eating; a separate hypothalamic group carries leptin's effect on heat production.
Stress, hormones and blood pressure
In rats it switches on corticotropin-releasing hormone neurons, raises oxytocin, makes the pituitary respond more to TRH and raises blood pressure through neuropeptide FF receptors.
Published Research
These are studies of prolactin-releasing peptide itself, in either of its two lengths, read from their PubMed abstracts: the discovery paper, measurements of the peptide and its message in human tissue, cultures of human pituitary and decidual cells, and rat and mouse work in which it was injected, deleted or blocked. No study read gave PrRP to a person.
Found as the partner of an orphan pituitary receptor
The authors cloned an orphan receptor, hGR3, that is made specifically in the human pituitary, and then searched hypothalamic extracts for whatever switched it on. The peptide they found shared no sequence with any known protein. Because it strongly triggered prolactin release from rat anterior pituitary cells, they named it prolactin-releasing peptide and put it forward as a candidate for the long-missing prolactin-releasing hormone.
Mostly in brain and pituitary, barely in blood
A sandwich enzyme immunoassay built on two monoclonal antibodies found PrRP throughout the rat brain and pituitary, highest in the hypothalamus. Outside the nervous system only the adrenal gland held a meaningful amount. Plasma averaged 0.13 fmol/mL. Chromatography showed both PrRP31 and PrRP20 in the hypothalamus, but only the 31-residue form in adrenal tissue and plasma, so different tissues seem to keep different lengths.
Raises prolactin in live rats, more in females
Intravenous PrRP31 raised plasma prolactin in rats in a dose-related way. In females a 50 nmol/kg dose worked within 25 minutes at several stages of the oestrous cycle, with the strongest response around proestrus; males needed ten times as much. Other pituitary hormones did not change. The authors read the sex and cycle differences as a sign that oestrogen sets how sensitive the pituitary is to the peptide.
Its message in normal human pituitary and in tumours
Using RT-PCR, the group found PrRP message in all five normal human pituitaries tested but in only 5 of 11 prolactinomas. Every prolactinoma that made it had responded to dopamine-agonist treatment, while those without it had responded poorly or only partly. It also turned up in about half of growth hormone tumours and non-functioning tumours, and the receptor's message was present in every sample, normal or not.
Raises oxytocin when given into the brain
Earlier anatomy had shown PrRP nerve endings touching oxytocin cells in two hypothalamic nuclei. Injected into the brain ventricles of conscious rats, the peptide raised plasma oxytocin in both sexes and vasopressin in females only. The authors suggest it tunes the large hypothalamic neurons that release these two hormones, especially the oxytocin cells.
Mapped in the human brain
A radioimmunoassay with an antiserum against human PrRP31, which read PrRP20 equally well, measured the peptide in post-mortem brain from six people. The hypothalamus held the most, about 912 fmol per gram of tissue, followed by the medulla oblongata and the thalamus; the frontal and temporal lobes held too little to detect. Chromatography found both lengths. Even in the hypothalamus the amount was lower than that of TRH or vasoactive intestinal peptide, two other peptides that can release prolactin.
A feeding signal more than a releasing hormone
This paper argued that PrRP is unlikely to be a classical pituitary-releasing hormone: no stained fibres reach the outer median eminence, and it is weaker than TRH at releasing prolactin both in the dish and in animals. Instead, its message fell during fasting and during lactation, and giving the peptide reduced food intake and body weight in rats, pointing to a role in energy balance.
First test on human pituitary cells
Human PrRP31 was added to cultures of fetal and adult human pituitary tissue and of pituitary tumours. In fetal cultures it raised prolactin output by up to 35%, with the full effect at 10 nM, a little less than TRH managed; adding oestradiol strengthened the response and let it raise growth hormone too. It had no effect on prolactin from prolactinoma cells, but it raised growth hormone by about a quarter in several growth hormone-secreting tumours.
Made in placenta and decidua, without the receptor
PrRP message was found in human placenta and decidua throughout pregnancy and rose somewhat in mid-pregnancy. Treating cultured endometrial and decidual cells with 1 microM PrRP31 did not change their prolactin output, and the decidua did not make the receptor's message. The authors concluded that the peptide made in these tissues has some other job in pregnancy.
Found in early-pregnancy decidua and nudged its prolactin
In first-trimester decidua from planned terminations, antibody staining placed PrRP in both gland and stromal cells, and cultured stromal cells carried the message for the peptide and for its receptor. Adding synthetic PrRP raised their prolactin output to about 135% of control. This conflicts with the placenta and decidua study above on whether the receptor is present, a disagreement the papers read do not settle.
In adrenal glands and adrenal tumours
Tissue from autopsies and surgery showed the receptor's message in human brain, pituitary, adrenal glands and a range of adrenal and nerve-cell tumours, with by far the strongest signal in pheochromocytomas. Radioimmunoassay found the peptide in normal adrenal tissue at about 0.16 pmol per gram, in four of six pheochromocytomas at widely varying levels, in one neuroblastoma and in some adrenocortical tumours.
Wakes sleeping rats and damps absence seizures
The reticular thalamic nucleus, which carries many PrRP receptors, helps generate sleep rhythms and the spike-wave discharges of absence epilepsy. Brain injections of 1-10 nmol in sleeping rats cut sleep oscillations and produced quick, lasting waking. Higher amounts suppressed spike-wave discharges in a rat strain bred for absence seizures, and in thalamic slices the peptide reduced rhythmic burst firing.
Its effect on weight faded within three days
A single brain injection of 4 nmol in free-feeding rats caused a rise in body temperature lasting four hours and more message for UCP-1, the heat-producing protein of brown fat. Twice-daily injections cut weight gain beyond what matched food restriction alone for the first two to three days, after which the rats no longer responded. The authors conclude PrRP lowers food intake and raises energy use over the short to medium term.
Needed for cholecystokinin to curb eating in mice
Brain injections of 1-4 nmol PrRP reduced feeding in normal mice after a fast and at night. In mice lacking GPR10, neither PrRP nor cholecystokinin, a gut hormone released after meals, reduced food intake. The feeding drop and stress-hormone rise caused by bacterial lipopolysaccharide were the same with or without the receptor, so the loss was specific to these satiety signals.
A messenger in the brain's stress response
After brain injection in rats, about 80% of the corticotropin-releasing hormone cells in the paraventricular nucleus showed activity markers, and plasma corticosterone rose within 30 minutes. Restraint, pain and inflammation all raised PrRP message in brainstem cell groups. Giving an antibody against PrRP first blunted the activation of the paraventricular nucleus by a painful stimulus.
Weak alone, but it amplified TRH
In rat pituitary cultures and in female rats, PrRP on its own raised prolactin several times less than TRH, and in animals it produced a slow, steady rise rather than a peak. Combined with TRH, it boosted the prolactin response 10- to 30-fold in culture and up to threefold in rats. Two pituitary growth factors, FGF-2 and EGF, reduced the PrRP effect in culture.
Mice without it grow obese
Brainstem neurons that make PrRP were switched on soon after rodents ate. Mice bred without PrRP became obese and fat later in life because they ate larger meals, and they responded less to cholecystokinin and leptin, while six other appetite peptides in the hypothalamus were unchanged. In normal rats, a brain injection of an antibody that blocks PrRP made meals larger. The authors propose that PrRP carries fullness signals inside the brain.
Raises blood pressure through neuropeptide FF receptors
In conscious rats, a brain injection of PrRP raised blood pressure and heart rate. RF9, a blocker of neuropeptide FF receptors, prevented this, and the effect was still there in OLETF rats, whose GPR10 gene is defective. In brain slices PrRP reduced inhibitory signals onto paraventricular neurons, again blocked by RF9. The authors conclude that some of its brain actions run through NPFF receptors, probably NPFF2, rather than GPR10.
Makes the heart beat more forcefully
Heart muscle carries many PrRP binding sites. In isolated perfused rat hearts, PrRP at 1-100 nM increased the force of contraction in a dose-related way. Blocking cAMP breakdown did not add to the effect, while blocking protein kinase C alpha or the phosphatases PP1 and PP2A together made it larger. The authors describe a direct, cAMP-independent effect on contraction that other signals hold in check.
Two groups of neurons, two jobs
In mice, PrRP neurons in the dorsomedial hypothalamus responded to leptin, and removing leptin receptors from just these cells blocked leptin's heat-producing effect and caused obesity. A separate, leptin-insensitive group of PrRP neurons in the brainstem was needed for cholecystokinin to reduce eating. Restoring the peptide in the brainstem of PrRP-deficient mice brought back the cholecystokinin response, while the hypothalamic cells had to be restored to bring back leptin's thermogenic effect.
Silencing it eased cancer weight loss in rats
Rats with liver tumours develop anorexia and wasting. Switching off PrRP production in the brainstem's nucleus of the solitary tract with a viral gene-silencing tool reduced their weight loss and loss of appetite and left their leg muscles heavier than in tumour-bearing controls. Corticosterone rose early in both groups but fell back to baseline by day 21 only in the silenced rats.
Linked to stress coping and sleep in rats
In male rats, PrRP-containing fibres reached the melanin-concentrating hormone neurons that help regulate sleep and mood, and PrRP quietened these neurons in brain slices. After sleep deprivation, a brain injection reduced the number of these neurons active in REM sleep. Rats that coped poorly with prolonged stress showed overactive PrRP cells and depleted PrRP and receptor in that brain region. The receptor was also reduced in the same region in post-mortem brains of people who died by suicide.
How the receptor grips its RF-amide tail
Cryo-electron microscopy showed PrRP bound to its receptor while the receptor was coupled to either a Gq or a Gi protein. A conserved polar pocket holds the amidated end that RF-amide peptides share, and comparison with neuropeptide Y receptors showed both shared and distinct ways of engaging that ending. The authors offer the structures as a basis for designing selective drugs for this receptor.
No Established Human Dose
Prolactin-releasing peptide has never been given to people in any study read. The human evidence is measurement only: radioimmunoassay of post-mortem brain and adrenal tissue, gene-message studies of pituitary, placenta and decidua, and experiments on human pituitary and decidual cells in culture. The amounts injected into rat and mouse brains are animal research conditions and do not translate into a human amount, and the fatty-acid analogues tested in obese mice are different molecules, so there is no dose to state.
What this rests on: PMID 11068103, PMID 11397894, PMID 12126742.
Educational information, not medical advice. The doses on this page come from approved labels, published studies and, where no study exists, amounts reported by users. None is a recommendation for you. An unapproved compound has no established safe or effective human dose, and products sold for “research use only” are not made or tested for people. Talk to a doctor before acting on anything on this site, including before you start, stop or change any medicine or dose. Full medical disclaimer.
What a Buyer Needs to Know
What is sold, how it is mixed, stored and taken, and what is known about its safety, quality and legal status. Each part names its source. Where we have none, it says unknown.
What is sold
Unknown: we hold no label and no published test that says what forms or vial sizes Prolactin-releasing peptide is sold in. A vial's own label is a seller's claim, not a source.
Mixing a vial: a worked example
Unknown: no human dose of Prolactin-releasing peptide has been established (see No Established Human Dose below), so there is no amount to work out. The reconstitution calculator does the arithmetic for any vial, water and dose.
Storage before and after mixing
Unknown: no label or published stability study on file says how to store Prolactin-releasing peptide, before or after mixing. The mixing guide sets out the general rules, with their sources: keep a mixed vial in the fridge, and use it promptly, as the bacteriostatic water label says of any drug dissolved in it. The 28 days often quoted is the limit for an opened multiple-dose vial from a manufacturer, an outer limit set for sterility, not a time a mixed solution has been shown to keep. Nobody has published how long Prolactin-releasing peptide stays intact once mixed.
How it is taken
Unknown: with no established human dose, there is no established way of taking Prolactin-releasing peptide. What the human studies gave and how is set out under No Established Human Dose.
What to expect, and when
Unknown: no cited half-life and no label or trial duration on this page says how long Prolactin-releasing peptide lasts or how long it was given. Results reported in the studies are under Published Research.
Side effects, and when to stop or get help
From the Side Effects section: In rats, a brain injection raised blood pressure and heart rate (PMID 19821834); In rats, a brain injection raised corticosterone, a stress hormone (PMID 16730416); No human safety data exist: every human study read measured it in tissue or tested it on cells (PMID 11068103). Full list and cautions ↓
When to stop or get help: unknown; no label or trial on file sets rules for stopping Prolactin-releasing peptide. Treat a severe or unexpected reaction as a reason to stop and see a doctor.
Source: the Side Effects section below (“Prolactin-releasing peptide has not been given to people, so no human side effects are known”).
Interactions
Unknown: a PubMed search for human interaction studies of Prolactin-releasing peptide (reviewed 2026-11-03) found none. Unknown is not the same as safe to combine.
Every peptide's record, with its source: the interaction matrix.
Checking what you bought
Unknown: no published independent test of Prolactin-releasing peptide products is in our lab-results database yet, so how products sold under this name measure up is not known.
To read a certificate of analysis, paste it into the COA decoder; it checks the measured mass against Prolactin-releasing peptide's expected mass, 3,664.2 Da, from this entry's molecular data. Trust & Verification explains what independent testing can and cannot show.
Legal status
US: Research Chemical (Not a medicine anywhere in the sources read: Drugs@FDA (openFDA) returns no record for prolactin-releasing peptide (November 3, 2026)). Sport: Not on the 2026 List.
Country by country ↓ · Regulatory tracker
Source: this entry's approval status and the WADA Prohibited List, as in Legal Status below.
Side Effects & Contraindications
Reported Side Effects
Prolactin-releasing peptide has not been given to people, so no human side effects are known.
Contraindications & Cautions
No product label exists. These cautions follow from the evidence.
Legal Status
Prolactin-releasing peptide is an endogenous research peptide; it is not approved as a medicine anywhere in the sources read.
Frequently Asked Questions
?What is prolactin-releasing peptide?
A peptide made mainly in the brainstem and hypothalamus, found in 1998 as the natural partner of the receptor GPR10. It exists in a 31-residue form, PrRP31, and a 20-residue form, PrRP20, which is the end of the longer one.
?Does it actually release prolactin?
It can, in rat and human pituitary cells and in live rats, but it is weaker than TRH and does not reach the pituitary the way true releasing hormones do. Most researchers now see it mainly as a brain signal for fullness and stress.
?Is it a drug or a supplement?
Neither. No medicine contains it, no regulator has approved it, and no study read gave it to a person. In people it has only been measured in tissue.
?What are the lipidized PrRP analogues?
Versions with a fatty acid chain attached, such as palmitoylated PrRP31, designed to last longer and reach the brain after injection under the skin. They reduced food intake and weight in obese mice, but they are separate molecules that have not been tested in people in any study read.
?What is the difference between PrRP31 and PrRP20?
Length. Both are cut from the same precursor and share the same last 20 residues, including the amidated end that binds the receptor. Both were found in human hypothalamus.
?Is there a safe dose?
No dose exists. The only amounts given were to rats and mice, mostly straight into the brain, and those cannot be turned into a human amount.
References
- [pubmed] Hinuma S, et al. "A prolactin-releasing peptide in the brain." Nature, 1998;393(6682):272-6. PMID: 9607765.
- [pubmed] Matsumoto H, et al. "Distribution and characterization of immunoreactive prolactin-releasing peptide (PrRP) in rat tissue and plasma." Biochem Biophys Res Commun, 1999;257(2):264-8. PMID: 10198200.
- [pubmed] Matsumoto H, et al. "Stimulation of prolactin release by prolactin-releasing peptide in rats." Biochem Biophys Res Commun, 1999;259(2):321-4. PMID: 10362506.
- [pubmed] Zhang X, et al. "Expression of prolactin-releasing peptide and its receptor messenger ribonucleic acid in normal human pituitary and pituitary adenomas." J Clin Endocrinol Metab, 1999;84(12):4652-5. PMID: 10599733.
- [pubmed] Maruyama M, et al. "Central administration of prolactin-releasing peptide stimulates oxytocin release in rats." Neurosci Lett, 1999;276(3):193-6. PMID: 10612638.
- [pubmed] Lawrence CB, et al. "Alternative role for prolactin-releasing peptide in the regulation of food intake." Nat Neurosci, 2000;3(7):645-6. PMID: 10862694.
- [pubmed] Takahashi K, et al. "Regional distribution of immunoreactive prolactin-releasing peptide in the human brain." Peptides, 2000;21(10):1551-5. PMID: 11068103.
- [pubmed] Rubinek T, et al. "Prolactin (PRL)-releasing peptide stimulates PRL secretion from human fetal pituitary cultures and growth hormone release from cultured pituitary adenomas." J Clin Endocrinol Metab, 2001;86(6):2826-30. PMID: 11397894.
- [pubmed] Yasui Y, et al. "Expression of prolactin-releasing peptide in human placenta and decidua." Endocr J, 2001;48(3):397-401. PMID: 11523913.
- [pubmed] Reis FM, et al. "Expression of prolactin-releasing peptide and its receptor in the human decidua." Mol Hum Reprod, 2002;8(4):356-62. PMID: 11912284.
- [pubmed] Takahashi K, et al. "Expression of prolactin-releasing peptide and its receptor in the human adrenal glands and tumor tissues of adrenocortical tumors, pheochromocytomas and neuroblastomas." Peptides, 2002;23(6):1135-40. PMID: 12126742.
- [pubmed] Lin SH, et al. "Prolactin-releasing peptide (PrRP) promotes awakening and suppresses absence seizures." Neuroscience, 2002;114(1):229-38. PMID: 12207968.
- [pubmed] Ellacott KL, et al. "Repeated administration of the anorectic factor prolactin-releasing peptide leads to tolerance to its effects on energy homeostasis." Am J Physiol Regul Integr Comp Physiol, 2003;285(5):R1005-10. PMID: 14557233.
- [pubmed] Mera T, et al. "Prolactin-releasing peptide is a potent mediator of stress responses in the brain through the hypothalamic paraventricular nucleus." Neuroscience, 2006;141(2):1069-1086. PMID: 16730416.
- [pubmed] Bechtold DA, et al. "Prolactin-releasing Peptide mediates cholecystokinin-induced satiety in mice." Endocrinology, 2006;147(10):4723-9. PMID: 16794001.
- [pubmed] Spuch C, et al. "Prolactin-releasing Peptide (PrRP) increases prolactin responses to TRH in vitro and in vivo." Endocrine, 2007;31(2):119-24. PMID: 17873321.
- [pubmed] Lin SH. "Prolactin-releasing peptide." Results Probl Cell Differ, 2008;46:57-88. PMID: 18204826.
- [pubmed] Takayanagi Y, et al. "Endogenous prolactin-releasing peptide regulates food intake in rodents." J Clin Invest, 2008;118(12):4014-24. PMID: 19033670.
- [pubmed] Ma L, et al. "Prolactin-releasing peptide effects in the rat brain are mediated through the Neuropeptide FF receptor." Eur J Neurosci, 2009;30(8):1585-93. PMID: 19821834.
- [pubmed] Kónyi A, et al. "Prolactin-releasing peptide regulates cardiac contractility." Regul Pept, 2010;159(1-3):9-13. PMID: 19616582.
- [pubmed] Dodd GT, et al. "The thermogenic effect of leptin is dependent on a distinct population of prolactin-releasing peptide neurons in the dorsomedial hypothalamus." Cell Metab, 2014;20(4):639-49. PMID: 25176149.
- [pubmed] Maletínská L, et al. "Novel lipidized analogs of prolactin-releasing peptide have prolonged half-lives and exert anti-obesity effects after peripheral administration." Int J Obes (Lond), 2015;39(6):986-93. PMID: 25771926.
- [pubmed] Pražienková V, et al. "Prolactin-Releasing Peptide: Physiological and Pharmacological Properties." Int J Mol Sci, 2019;20(21). PMID: 31653061.
- [pubmed] Navarro I Batista K, et al. "Brainstem prolactin-releasing peptide contributes to cancer anorexia-cachexia syndrome in rats." Neuropharmacology, 2020;180:108289. PMID: 32890590.
- [pubmed] Alexopoulou F, et al. "Lipidated PrRP31 metabolites are long acting dual GPR10 and NPFF2 receptor agonists with potent body weight lowering effect." Sci Rep, 2022;12(1):1696. PMID: 35105898.
- [pubmed] Vas S, et al. "Prolactin-Releasing Peptide Contributes to Stress-Related Mood Disorders and Inhibits Sleep/Mood Regulatory Melanin-Concentrating Hormone Neurons in Rats." J Neurosci, 2023;43(5):846-862. PMID: 36564184.
- [pubmed] Li Y, et al. "Molecular mechanism of prolactin-releasing peptide recognition and signaling via its G protein-coupled receptor." Cell Discov, 2024;10(1):91. PMID: 39223120.
- [pubmed] Škrlová M, et al. "The prolactin-releasing peptide system: Physiological functions and therapeutic potential in obesity." Neurobiol Dis, 2026;228:107554. PMID: 42532155.
Sources & Citations
Every study on this page was read from its PubMed record on November 3, 2026. The sequences, precursor positions and the amidated C-terminus come from UniProt P81277; regulatory status comes from Drugs@FDA (openFDA), read the same day. Grey Peptides sells nothing and links to no vendor.
Medical Disclaimer: This content is for educational and informational purposes only. It is not medical advice, and nothing here is an instruction to obtain or use any compound. Talk to a licensed clinician about your own situation.