PepGenexShop our research products

Sermorelin

Also identified as GHRH (1-29) amide, GRF(1-29)NH2, hGRF(1-29), Sermorelin acetate

Growth-hormone-releasing hormone analogue, GHRH (1-29)

Sequence: Tyr-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala-Arg-Lys-Leu-Leu-Gln-Asp-Ile-Met-Ser-Arg-NH2

Molecular weight
3357.9
Molecular formula
C149H246N44O42S
CAS
86168-78-7
Published studies reviewed
6

FOR RESEARCH USE ONLY. NOT FOR HUMAN OR VETERINARY USE. NOT FOR HUMAN CONSUMPTION.

Compounds described on this site are supplied solely for laboratory research. They are not offered for human or veterinary use or for clinical use, and they are not intended to diagnose, mitigate, cure or prevent any disease.

Sermorelin is the first 29 residues of human growth-hormone-releasing hormone with an amidated C-terminus, also printed as GHRH(1-29)NH2 or GRF(1-29)NH2, and it is neither CJC-1295 nor the tetrasubstituted modified GRF (1-29). Six publications are reviewed: two laboratory studies of structure-activity and enzymatic breakdown, a pharmacokinetic study in healthy men, and three human studies in older men and children whose reports include several measures that did not change. Drugs@FDA lists two approved applications for sermorelin acetate with the products under both discontinued, and PepGenex research material is not those products.

At a glance

Also identified as
GHRH (1-29) amide, GRF(1-29)NH2, hGRF(1-29), Sermorelin acetate
Class
Growth-hormone-releasing hormone analogue, GHRH (1-29)
Target or mechanism
Agonist — Growth-hormone-releasing hormone receptor
Evidence types represented
in vitro, human
Published studies reviewed
6
Regulatory and registry records
1
Last reviewed
2026-09-24
U.S. FDA status
Drugs@FDA lists two approved applications for sermorelin acetate, and the products under both are listed as discontinued. Source: Drugs@FDA, Applications NDA 019863 and NDA 020443.

Overview

Sermorelin is the first 29 amino acids of human growth-hormone-releasing hormone, amidated at the C-terminus. The literature also prints it as GHRH(1-29)NH2, GRF(1-29)NH2 and hGRF(1-29); those names all identify this molecule.

⚠️ It is not CJC-1295 and not the modified (tetrasubstituted) GRF (1-29) forms. Those are separate molecules with their own pages, and nothing recorded for them applies here.

The publications collected on this page are of three kinds: laboratory work on which residues of the 1-29 amide matter for receptor activation and on how the peptide is broken down; a pharmacokinetic study in 30 healthy men that also measured growth-hormone release; three human studies — one in older men, two in children — that reported a mixture of findings, including several measures that did not change and a growth rate that was not sustained after the peptide was stopped.

Regulatory status

Drugs@FDA lists two approved applications for sermorelin acetate, and the products under both are listed as discontinued. PepGenex research materials are not those products, are not FDA approved, and are not for human or veterinary use.

Source: Drugs@FDA, Applications NDA 019863 and NDA 020443. Verified 2026-09-24.

Mechanism under investigation

Sermorelin
Agonist
  • Growth-hormone-releasing hormone receptor

The laboratory work recorded here scans the 1-29 amide residue by residue and reports which positions are required for the fragment to release growth hormone from pituitary cells, which the authors describe as an analysis of the features important for receptor activation. A second laboratory publication reports that the peptide is cleaved by dipeptidyl peptidase IV to GRF(3-29)NH2, which it describes as inactivated. The human studies measured growth-hormone release and pharmacokinetics; none of them characterised receptor binding.

Scope of the published work

Areas investigated
  • Structure-activity relationships
  • Enzymatic degradation
  • Pharmacokinetics
  • Growth-hormone release
  • Growth rate in children
Models used
  • Rat pituitary cell assays
  • Rat intestinal brush-border membranes
  • Human studies in healthy volunteers
  • Uncontrolled human studies

Every human figure on this page was recorded in a controlled study, under supervision, using material prepared for that study, in a population selected by its entry criteria. It is not the research material PepGenex supplies and no result here transfers to it.

Limitations

Evidence represented on this page: in vitro and human. No animal research is represented. The page reviews 6 published studies, and each figure is reported for the study that published it; results are not pooled across studies. 1 of these publications carries a note on whether it studied this exact material.

Common questions

What is Sermorelin?

Sermorelin is the first 29 amino acids of human growth-hormone-releasing hormone, amidated at the C-terminus.

How does Sermorelin work, according to the published research?

The laboratory work recorded here scans the 1-29 amide residue by residue and reports which positions are required for the fragment to release growth hormone from pituitary cells, which the authors describe as an analysis of the features important for receptor activation. A second laboratory publication reports that the peptide is cleaved by dipeptidyl peptidase IV to GRF(3-29)NH2, which it describes as inactivated. The human studies measured growth-hormone release and pharmacokinetics; none of them characterised receptor binding.

  • The authors state that the combined results allowed an analysis of the structural features in the native peptide that are important for receptor activation, and that reinforcing amphiphilicity, helicity and peptide dipolar effects produced several more potent analogues. (Cervini et al., 1998, PMID 9513600)
  • States that GRF(1-29)NH2 is degraded mainly by dipeptidyl peptidase IV in plasma, giving GRF(3-29)NH2, which the publication describes as inactivated. In rat intestinal brush-border membranes, gradient HPLC, mass balance analysis and inhibitor studies identified GRF(3-29)NH2 as the major metabolite of GRF(1-29)NH2, formed by the action of the same enzyme. (Bai et al., 1995, PMID 8583376)

What has published research on Sermorelin found, and what are its limits?

This page records 6 publications, reporting laboratory (in vitro) work in 2, human work in 4. Each is listed with its identifier under References.

Human studies represented: Schwartz et al., 2000, PMID 10905389; Vittone et al., 1997, PMID 9005976; Thorner et al., 1996, PMID 8772599; Wilton et al., 1993, PMID 8329825.

Evidence represented on this page: in vitro and human.

No animal research is represented.

The page reviews 6 published studies, and each figure is reported for the study that published it; results are not pooled across studies.

1 of these publications carries a note on whether it studied this exact material.

Every human figure on this page was recorded in a controlled study, under supervision, using material prepared for that study, in a population selected by its entry criteria. It is not the research material PepGenex supplies and no result here transfers to it.

Is Sermorelin approved by the U.S. FDA?

Drugs@FDA lists two approved applications for sermorelin acetate, and the products under both are listed as discontinued. PepGenex research materials are not those products, are not FDA approved, and are not for human or veterinary use.

Source: Drugs@FDA, Applications NDA 019863 and NDA 020443. Verified 2026-09-24.

What risks have published studies of Sermorelin reported?

2 published human studies on this page report adverse events or safety measurements. Each is listed with its publication in the adverse-events section of this page.

Trial events do not establish a complete safety profile.

What adverse events have been reported in published studies of Sermorelin?

Adverse events and safety measurements as reported by the published human studies on this page. Each entry is attributed to its publication.

Vittone et al., 1997, PMID 9005976

Design and population
Eleven healthy, ambulatory, non-obese men aged 64 to 76 years with low baseline IGF-I concentrations were studied at home as outpatients, receiving GHRH for 6 weeks. Measurements before and after were growth-hormone concentrations in blood sampled every 20 minutes from 8:00 PM to 8:00 AM; morning IGF-I, IGF binding protein-3 and growth-hormone binding protein; muscle strength; muscle histology; normalised phosphocreatine abundance and intracellular pH in forearm muscle by phosphorus nuclear magnetic resonance spectroscopy during sustained and ramped exercise; dual-energy x-ray absorptiometry; lipids; and glucose, insulin and growth hormone during an oral glucose tolerance test.
Events reported
No significant adverse effects were observed.

Thorner et al., 1996, PMID 8772599

Design and population
A multicentre, open-label study of GHRH-(1-29) given for up to 1 year in 110 previously untreated prepubertal growth-hormone-deficient children, of whom 86 were eligible for efficacy analysis. The main outcome measures, monitored every 3 to 6 months, were linear growth (height velocity), bone-age progression, and safety measures including clinical chemistry.
Events reported
No adverse changes in general biochemical or hormonal analyses were noted. No change in fasting glucose concentration or excessive generation of insulin-like growth factor I occurred, and overall GHRH was well tolerated.

Trial events do not establish a complete safety profile.

Published research

Grouped by the kind of study. Select one to narrow what is shown below.

Laboratory (in vitro)(2)

Laboratory (in vitro)

Human growth hormone-releasing hormone hGHRH(1-29)-NH2: systematic structure-activity relationship studies.

Cervini LA, Donaldson CJ, Koerber SC, Vale WW, Rivier JE., Journal of Medicinal Chemistry, 1998;41(5):717-727

published

Material identity not established. The scans in this publication were run on the [Nle27] variant of the 1-29 amide, and potencies are given relative to hGHRH(1-40)-OH. It maps the 1-29 amide sequence this compound is made of; it is not a study of the unsubstituted peptide itself.

  • Reports two complete and two partial structure-activity scans of the active fragment of human growth-hormone-releasing hormone, [Nle27]-hGHRH(1-29)-NH2. Replacing single residues with alanine identified [Ala8], [Ala9], [Ala15], [Ala22] and [Ala28, Nle27] as 2 to 6 times more potent than the hGHRH(1-40)-OH standard in vitro, while [Ala1], [Ala3], [Ala5], [Ala6], [Ala10], [Ala11], [Ala13], [Ala14] and [Ala23] showed nearly complete loss of potency.
  • The authors state that the combined results allowed an analysis of the structural features in the native peptide that are important for receptor activation, and that reinforcing amphiphilicity, helicity and peptide dipolar effects produced several more potent analogues.
View publication →
Laboratory (in vitro)

The involvement of dipeptidyl peptidase IV in brush-border degradation of GRF(1-29)NH2 by intestinal mucosal cells.

Bai JP, Chang LL., Journal of Pharmacy and Pharmacology, 1995;47(8):698-701

published

  • States that GRF(1-29)NH2 is degraded mainly by dipeptidyl peptidase IV in plasma, giving GRF(3-29)NH2, which the publication describes as inactivated. In rat intestinal brush-border membranes, gradient HPLC, mass balance analysis and inhibitor studies identified GRF(3-29)NH2 as the major metabolite of GRF(1-29)NH2, formed by the action of the same enzyme.
  • A separate molecule tested alongside it, [desNH2Tyr1,D-Ala2,Ala15]-GRF(1-29)NH2, which resists plasma dipeptidyl peptidase IV, was much more stable than GRF(1-29)NH2 in enterocytes.
Context

The degradation work explains why the human pharmacokinetics look the way they do: dipeptidyl peptidase IV cuts two residues off the front of the peptide, and what is left is described as inactivated. The analogue that resists that enzyme, tested in the same publication, is a different molecule — which is the whole reason the modified GRF (1-29) forms exist, and the reason they are recorded on their own page rather than this one.

View publication →

Human study (phase not stated)(4)

Human study (phase not stated)n = 24

Growth during and after a trial of growth hormone releasing hormone 1-29 in children with idiopathic short stature or growth hormone neurosecretory dysfunction.

Schwartz ID, Grunt JA, Berg S, Jacobson JD, Moore WV, Howard CP., Journal of Pediatric Endocrinology & Metabolism, 2000;13(6):645-650

published

GHRH 1-29 given for 6 months was studied in 16 slowly growing prepubertal children with idiopathic short stature and 8 similar children with growth-hormone neurosecretory dysfunction. Each child had endogenous growth-hormone evaluation by both pharmacological and physiological testing, had stimulated values above 10 µg/l, and was grouped by pooled 12-hour overnight growth hormone below or at least 3 µg/l. Each was followed every three months for one year.

  • Both groups showed similar significant increases in their rates of growth during the 6-month period, and there were no significant differences between the two groups throughout the study other than in endogenous growth-hormone concentrations.
  • Six months after the peptide was stopped, overall rates of growth were not significantly different from the rates recorded before it was started, although a subset — 6 of 21 — continued to grow at a rate significantly greater than before. The authors conclude that, despite prior reports to the contrary, children with growth-hormone neurosecretory dysfunction do not experience a sustained increase in growth rate once it is discontinued.
Limitations

In eleven older men over six weeks, growth-hormone release rose but IGF-I did not, and weight, imaging measures of muscle and fat, muscle histology, lipids and the glucose tolerance test were all unchanged; the authors' own reading is that the regimen studied is less effective than an alternative regimen. In 24 children with idiopathic short stature or growth-hormone neurosecretory dysfunction, growth rates rose during the six months and were back to their starting rates six months after it stopped. In a larger open-label study of 110 growth-hormone-deficient children, mean height velocity rose from 4.1 cm/yr at baseline to 8.0 cm/yr at 6 months and 7.2 cm/yr at 12 months; that abstract reports nothing about growth after the peptide was stopped, and the two groups of children are not the same population, so neither result stands in for the other. None of these studies had a placebo group, which is a further reason to hold all of them loosely.

View publication →
Human study (phase not stated)n = 11

Vittone et al., 1997 (title withheld on this site; see the publication record)

Vittone J, Blackman MR, Busby-Whitehead J, et al., Metabolism: Clinical and Experimental, 1997;46(1):89-96

published

Eleven healthy, ambulatory, non-obese men aged 64 to 76 years with low baseline IGF-I concentrations were studied at home as outpatients, receiving GHRH for 6 weeks. Measurements before and after were growth-hormone concentrations in blood sampled every 20 minutes from 8:00 PM to 8:00 AM; morning IGF-I, IGF binding protein-3 and growth-hormone binding protein; muscle strength; muscle histology; normalised phosphocreatine abundance and intracellular pH in forearm muscle by phosphorus nuclear magnetic resonance spectroscopy during sustained and ramped exercise; dual-energy x-ray absorptiometry; lipids; and glucose, insulin and growth hormone during an oral glucose tolerance test.

  • Mean nocturnal growth-hormone release increased (P < .02), as did the area under the growth-hormone peak (P < .006) and growth-hormone peak amplitude (P < .05), with no change in growth-hormone pulse frequency and no change in IGF-I, IGF binding protein-3 or growth-hormone binding protein.
  • Weight, body mass index, waist-to-hip ratio, dual-energy x-ray absorptiometry measures of muscle and fat, muscle histology, lipids, and the glucose, insulin and growth-hormone responses to the oral glucose tolerance test did not change. Exercise-mediated changes in phosphocreatine abundance and intracellular pH were also unaltered.
  • Two of six measures of muscle strength — upright row (P < .02) and shoulder press (P < .04) — and one test of muscle endurance, abdominal crunch (P < .03), increased. The other four strength measures did not.
  • Exercise-mediated changes in normalised phosphocreatine abundance and intracellular pH were not altered, but significant relationships between those changes and indices of muscle strength were decreased or abolished. The authors state that GHRH may increase muscle strength, and that it alters baseline relationships between muscle strength and muscle bioenergetics in a manner consistent with a reduced need for anaerobic metabolism during exercise.
  • No significant adverse effects were observed.
  • The authors conclude that these data suggest the regimen of GHRH studied is less effective than an alternative regimen at eliciting growth-hormone- and IGF-I-mediated effects.
Limitations

In eleven older men over six weeks, growth-hormone release rose but IGF-I did not, and weight, imaging measures of muscle and fat, muscle histology, lipids and the glucose tolerance test were all unchanged; the authors' own reading is that the regimen studied is less effective than an alternative regimen. In 24 children with idiopathic short stature or growth-hormone neurosecretory dysfunction, growth rates rose during the six months and were back to their starting rates six months after it stopped. In a larger open-label study of 110 growth-hormone-deficient children, mean height velocity rose from 4.1 cm/yr at baseline to 8.0 cm/yr at 6 months and 7.2 cm/yr at 12 months; that abstract reports nothing about growth after the peptide was stopped, and the two groups of children are not the same population, so neither result stands in for the other. None of these studies had a placebo group, which is a further reason to hold all of them loosely.

View publication →
Human study (phase not stated)n = 110

Thorner et al., 1996 (title withheld on this site; see the publication record)

Thorner M, Rochiccioli P, Colle M, et al., The Journal of Clinical Endocrinology & Metabolism, 1996;81(3):1189-1196

published

A multicentre, open-label study of GHRH-(1-29) given for up to 1 year in 110 previously untreated prepubertal growth-hormone-deficient children, of whom 86 were eligible for efficacy analysis. The main outcome measures, monitored every 3 to 6 months, were linear growth (height velocity), bone-age progression, and safety measures including clinical chemistry.

  • Mean height velocity for the group increased from 4.1 ± 0.9 cm/yr at baseline to 8.0 ± 1.5 cm/yr after 6 months. At 6 months, 74% of the children were considered to have a good response.
  • Mean height velocity for the group was 7.2 ± 1.3 cm/yr after 12 months, against 4.1 ± 0.9 cm/yr at baseline. The authors conclude that GHRH-(1-29) was effective in increasing height velocity in growth-hormone-deficient children.
  • The ratio of the change in bone age to height age was not significantly different from unity at 12 months (1.04 ± 0.58; P = 0.63).
  • No adverse changes in general biochemical or hormonal analyses were noted. No change in fasting glucose concentration or excessive generation of insulin-like growth factor I occurred, and overall GHRH was well tolerated.
Limitations

In eleven older men over six weeks, growth-hormone release rose but IGF-I did not, and weight, imaging measures of muscle and fat, muscle histology, lipids and the glucose tolerance test were all unchanged; the authors' own reading is that the regimen studied is less effective than an alternative regimen. In 24 children with idiopathic short stature or growth-hormone neurosecretory dysfunction, growth rates rose during the six months and were back to their starting rates six months after it stopped. In a larger open-label study of 110 growth-hormone-deficient children, mean height velocity rose from 4.1 cm/yr at baseline to 8.0 cm/yr at 6 months and 7.2 cm/yr at 12 months; that abstract reports nothing about growth after the peptide was stopped, and the two groups of children are not the same population, so neither result stands in for the other. None of these studies had a placebo group, which is a further reason to hold all of them loosely.

View publication →
Human study (phase not stated)n = 30

Wilton et al., 1993 (title withheld on this site; see the publication record)

Wilton P, Chardet Y, Danielson K, Widlund L, Gunnarsson R., Acta Paediatrica. Supplement, 1993;388:10-15

published

GHRH(1-29)-NH2 was given by two different routes to 30 healthy men aged 19 to 43 years, with pharmacokinetic measurement and measurement of growth-hormone release.

  • Given intravenously, the lowest amount tested elicited significant release of growth hormone. Maximal release, with mean growth-hormone peaks of about 90 mU/l, was obtained at higher amounts.
  • GHRH(1-29)-NH2 was rapidly eliminated after it was given intravenously, while growth-hormone concentrations stayed raised for about 3 hours. Absorption through the nasal mucosa was low, with a bioavailability of only 3 to 5 per cent.
  • Growth-hormone release after the peptide was given into the nose was related to the amount given; a comparable response needed a substantially larger amount by that route than intravenously. The response to repeated nasal use was sustained, and there was no suppression of growth-hormone secretion during the night following a day on which it had been given repeatedly by that route.
Context

The human studies here measured hormone concentrations and how fast the peptide leaves the blood. Growth hormone rose, briefly, in a way related to the amount given; the peptide itself was cleared quickly. What happened to the people in whom those concentrations rose was measured in three studies — one in older men, two in children — and each is recorded on this page with the measures that changed and the measures that did not.

View publication →

Compared with related compounds

Classification, structure, recorded targets, evidence types and FDA status only, each read from the two compounds' own pages. These comparisons do not compare study results.

Sermorelin and Tesamorelin

Growth-hormone-releasing hormone analogues recorded at the same receptor.

SermorelinTesamorelin
ClassificationGrowth-hormone-releasing hormone analogue, GHRH (1-29)Growth-hormone-releasing hormone analogue
StructureSequence Tyr-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala-Arg-Lys-Leu-Leu-Gln-Asp-Ile-Met-Ser-Arg-NH2; formula C149H246N44O42SFormula C221H366N72O67S
Targets recordedAgonist: Growth-hormone-releasing hormone receptorAgonist: Growth-hormone-releasing hormone receptor
Evidence types representedin vitro, humanhuman
Status with the U.S. FDADrugs@FDA lists two approved applications for sermorelin acetate, and the products under both are listed as discontinued. Source: Drugs@FDA, Applications NDA 019863 and NDA 020443.An FDA approved drug product containing tesamorelin exists. Source: Drugs@FDA, Application BLA 022505.

Sermorelin and CJC-1295 (no DAC)

Growth-hormone-releasing hormone analogues.

SermorelinCJC-1295 (no DAC)
ClassificationGrowth-hormone-releasing hormone analogue, GHRH (1-29)Growth-hormone-releasing hormone analogue without drug affinity complex
StructureSequence Tyr-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala-Arg-Lys-Leu-Leu-Gln-Asp-Ile-Met-Ser-Arg-NH2; formula C149H246N44O42SNot recorded on its page
Targets recordedAgonist: Growth-hormone-releasing hormone receptorNo target recorded on its page
Evidence types representedin vitro, humanin vitro, animal
Status with the U.S. FDADrugs@FDA lists two approved applications for sermorelin acetate, and the products under both are listed as discontinued. Source: Drugs@FDA, Applications NDA 019863 and NDA 020443.Not shown (no Drugs@FDA application record verified for this page)

Sermorelin and Ipamorelin

Growth-hormone secretagogues recorded at different receptors: the growth-hormone-releasing hormone receptor, and the GHRP-type receptor.

SermorelinIpamorelin
ClassificationGrowth-hormone-releasing hormone analogue, GHRH (1-29)Growth-hormone secretagogue (GHRP-type receptor agonist)
StructureSequence Tyr-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala-Arg-Lys-Leu-Leu-Gln-Asp-Ile-Met-Ser-Arg-NH2; formula C149H246N44O42SSequence Aib-His-D-2-Nal-D-Phe-Lys-NH2; formula C38H49N9O5
Targets recordedAgonist: Growth-hormone-releasing hormone receptorAgonist: GHRP-type (growth-hormone secretagogue) receptor
Evidence types representedin vitro, humanin vitro, animal, human
Status with the U.S. FDADrugs@FDA lists two approved applications for sermorelin acetate, and the products under both are listed as discontinued. Source: Drugs@FDA, Applications NDA 019863 and NDA 020443.Not shown (no Drugs@FDA application record verified for this page)

References

Published studies reviewed (6)

  1. Human growth hormone-releasing hormone hGHRH(1-29)-NH2: systematic structure-activity relationship studies. — Cervini LA, Donaldson CJ, Koerber SC, Vale WW, Rivier JE., Journal of Medicinal Chemistry, 1998;41(5):717-727
    DOI 10.1021/jm970618s · PMID 9513600
  2. The involvement of dipeptidyl peptidase IV in brush-border degradation of GRF(1-29)NH2 by intestinal mucosal cells. — Bai JP, Chang LL., Journal of Pharmacy and Pharmacology, 1995;47(8):698-701
    DOI 10.1111/j.2042-7158.1995.tb05863.x · PMID 8583376
  3. Wilton et al., 1993 (title withheld on this site; see the publication record) — Wilton P, Chardet Y, Danielson K, Widlund L, Gunnarsson R., Acta Paediatrica. Supplement, 1993;388:10-15
    DOI 10.1111/j.1651-2227.1993.tb12827.x · PMID 8329825
  4. Vittone et al., 1997 (title withheld on this site; see the publication record) — Vittone J, Blackman MR, Busby-Whitehead J, et al., Metabolism: Clinical and Experimental, 1997;46(1):89-96
    DOI 10.1016/s0026-0495(97)90174-8 · PMID 9005976
  5. Thorner et al., 1996 (title withheld on this site; see the publication record) — Thorner M, Rochiccioli P, Colle M, et al., The Journal of Clinical Endocrinology & Metabolism, 1996;81(3):1189-1196
    DOI 10.1210/jcem.81.3.8772599 · PMID 8772599
  6. Growth during and after a trial of growth hormone releasing hormone 1-29 in children with idiopathic short stature or growth hormone neurosecretory dysfunction. — Schwartz ID, Grunt JA, Berg S, Jacobson JD, Moore WV, Howard CP., Journal of Pediatric Endocrinology & Metabolism, 2000;13(6):645-650
    DOI 10.1515/jpem.2000.13.6.645 · PMID 10905389

Regulatory and registry records (1)

  1. Drugs@FDA, Applications NDA 019863 and NDA 020443
    Cited for the regulatory status statement on this page. Verified 2026-09-24.

Continue learning