Compound reference
Sermorelin
Growth Hormone Research · vial. For laboratory research use only. Not for human or veterinary consumption, diagnostic use, therapeutic use, or clinical use.
Chemistry identity
Reference identifiers
COA documentation
Lot record status
COA per lot - on requestView Lab ReportsPublished literature
Research context
Peer-reviewed literature referencing this compound, provided for research context.
A potentially effective drug for patients with recurrent glioma: sermorelin2021
Chang Y, Huang R, Zhai Y, Huang L, Feng Y, Wang D, et al.
Annals of translational medicine
Using computational drug-sensitivity modeling of transcriptomic profiles from over 1,000 glioma patients, researchers computed sermorelin sensitivity scores and found associations with cell-cycle regulatory gene expression and immune-checkpoint pathway activity in glioma-derived datasets, illustrating a bioinformatic approach to studying GHRH-pathway peptide pharmacology in oncology research models.
Interactions of GRF(1-29)NH2 with plasma proteins and their effects on the release of the peptide from a PLAGA matrix2005
Mariette B, Coudane J, Vert M
Journal of controlled release : official journal of the Controlled Release Society
In vitro and rat-model pharmacology research examined how GRF(1-29)NH2 (sermorelin) interacts with plasma proteins such as albumin and immunoglobulins, causing precipitation, and characterized its release kinetics from a bioresorbable PLAGA polymer matrix implanted subcutaneously in rats, informing peptide delivery-system research.
The involvement of dipeptidyl peptidase IV in brush-border degradation of GRF(1-29)NH2 by intestinal mucosal cells1995
Bai JP, Chang LL
The Journal of pharmacy and pharmacology
Using rat intestinal brush-border membrane preparations, this study identified dipeptidyl peptidase IV (DPP-IV) as the primary enzyme responsible for degrading GRF(1-29)NH2 (sermorelin) into the inactive GRF(3-29)NH2 fragment, and showed that an enzyme-resistant analog demonstrated markedly greater stability, informing structure-stability research on GHRH-peptide analogs.
Does growth hormone releasing factor desensitize the somatotroph? Interpretation of responses of growth hormone during and after 10-hour infusion of GRF 1-29 amide in man1986
Davis JR, Sheppard MC, Shakespear RA, Lynch SS, Clayton RN
Clinical endocrinology
This pharmacodynamic research study infused GRF(1-29) amide (sermorelin) over 10 hours in adult male research subjects and monitored pulsatile GH output, finding that GH pulses continued throughout the infusion without a clear reduction in total secretion, while a subsequent GH bolus response was variably reduced -- research addressing whether prolonged GHRH-receptor stimulation desensitizes pituitary somatotroph cells.
Structural requirements for the activation of rat anterior pituitary adenylate cyclase by growth hormone-releasing factor (GRF): discovery of (N-Ac-Tyr1, D-Arg2)-GRF(1-29)-NH2 as a GRF antagonist on membranes1985
Robberecht P, Coy DH, Waelbroeck M, Heiman ML, de Neef P, Camus JC, et al.
Endocrinology
Using rat anterior pituitary membrane homogenates, this foundational structure-activity study characterized how GRF(1-29)-NH2 (sermorelin) and related analogs activate adenylate cyclase signaling, mapping which amino-acid positions in the sequence are required for receptor activation and identifying a modified analog that instead acts as a competitive receptor antagonist -- establishing core GHRH-receptor pharmacology.
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This product is intended strictly for research and laboratory use only. It is designated for in vitro testing and experimental purposes. Any use involving human or animal consumption is prohibited by law. All information provided on this website is for educational purposes only. This product must only be handled by licensed, qualified professionals. It is not intended for use as a drug, food, or cosmetic, and must not be misused, mislabeled, or misrepresented as such.