Sermorelin — wholesale 10-vial kits

Research context

Human GHRH was isolated in 1982 from pancreatic tumors that had caused acromegaly; the Guillemin laboratory reported the 44-residue amidated sequence in Science, and the Vale laboratory characterized the same factor independently. Structure–activity work soon showed that C-terminally truncated, amidated fragments keep the hormone's full intrinsic activity: in rat anterior pituitary cells, hGRF(1-29)NH₂ retained about half the potency of the full-length hormone, and activity was lost only when the chain was cut back to residues 1-19 (Ling et al., 1984). That 29-residue amidated fragment is sermorelin.

Sermorelin is unmodified in sequence, so it carries all three of native GHRH's instability points: the Ala2–Asp3 bond cleaved by dipeptidyl peptidase-4, Asn8, which rearranges to Asp and β-Asp through an aminosuccinimide intermediate, and Met27, which oxidizes (Campbell et al., Peptides, 1994). It is therefore short-acting in experimental systems, and the oxidized-methionine variant is a common impurity to watch for on a chromatogram. Each of those three liabilities is what the substitutions in Mod GRF 1-29 are designed to remove, which is why the two are run together in structure–activity panels.

Because it is the native sequence, sermorelin is the reference GHRH-receptor agonist against which engineered analogs such as Mod GRF 1-29 (CJC-1295 without DAC) and tesamorelin are compared. It is used in pituitary cell models, in studies of how GHRH-receptor signaling relates to sleep architecture and growth-hormone pulsatility, and as an analytical standard for GHRH-family peptides.

U.S. regulatory status: sermorelin acetate was approved by the FDA in December 1990 as Geref (NDA 019863), with a second application (NDA 020443) following in 1997. Drugs@FDA lists the products under both applications as discontinued, and no FDA-approved sermorelin drug product is currently marketed in the United States. The sermorelin sold by WholesalePeptide.us is a research compound supplied only for in-vitro, analytical and preclinical laboratory research.

Alanine- and Aib-scanning studies of the hGHRH(1-29)NH₂ scaffold mapped which of its 29 positions tolerate substitution and which are essential, and found several single replacements that are more potent in vitro than the full-length hormone; cyclic lactam-constrained analogs of the same fragment were more potent again (Cervini et al., Journal of Medicinal Chemistry, 1998). Sermorelin is the unmodified point of reference for all of that work, which is why it remains the comparator rather than a first-choice stabilized agonist.

Labs building a GHRH-analog panel usually order sermorelin together with Mod GRF 1-29 and tesamorelin so that the effects of the four stabilizing substitutions and of N-terminal acylation can be compared against the native sequence. Lot-specific COAs with LC-MS identity for each compound keep that comparison clean, and mixed-compound orders count toward the same wholesale tier.

Research areas

• GHRH receptor agonism (native sequence reference)
• Pituitary somatotroph cell models
• GHRH signaling and sleep-architecture research
• Structure–activity comparisons with engineered GHRH analogs
• DPP-4 cleavage and Asn8 rearrangement studies
• Methionine-oxidation impurity profiling

U.S. regulatory status of the compound (as an active ingredient): No FDA-approved sermorelin product is currently marketed in the U.S. (Geref was discontinued). The material sold here is a research reference chemical, not a drug product.

Handling and storage

• Store lyophilized vials at −20 °C, sealed, protected from light and moisture.
• Let the vial reach room temperature before opening to limit condensation on the powder.
• Met27 oxidizes readily; use degassed buffers and minimize air exposure of reconstituted material.
• Aliquot reconstituted material and freeze once; avoid repeated freeze–thaw.