Amino Science Labs sells research peptides exclusively to qualified researchers and laboratories for in vitro and laboratory use. Please confirm before continuing.
By proceeding you affirm the statements above are true. Products are not for human or veterinary use, not for use in diagnostic procedures, and have not been evaluated by the U.S. Food and Drug Administration. Full disclaimer.
🔥 FREE SHIPPING ON ORDERS OVER $250 🔥
Research Peptide
Sermorelin research compound.
Fast shipping
Same-day dispatch
Third-party tested
U.S. accredited labs
99%+ purity
HPLC verified
29AA
SEQUENCE
GHRH(1-29)NH2 — shortest bioactive fragment
1997
FDA APPROVED
As Geref for GH deficiency
2-5x
GH RELEASE
Pulsatile secretion increase
200+
PUBLICATIONS
Extensive clinical trial data
3358Da
MOL. WEIGHT
Synthetic GHRH analogue
Free shipping
on orders over $150
Quality guarantee
99%+ purity verified
Secure checkout
256-bit SSL encryption
Research
Sermorelin is a synthetic 29-amino-acid peptide amide (CAS 86168-78-7; molecular formula C149H246N44O42S) that corresponds to the biologically defined N-terminal fragment of growth-hormone-releasing hormone, and it is often written in the literature as GRF(1-29) or GHRH(1-29)-NH2. This 1-29 segment is the shortest sequence of the parent 44-residue hormone that retains the full receptor-recognition motif studied in vitro, which is why sermorelin became a standard reference peptide for investigating the growth-hormone-releasing hormone receptor (GHRHR). Supplied here at a 10 mg fill, it is intended strictly as an in-vitro and preclinical research material and has no consumer application.
As a truncated analog of the full-length hormone, sermorelin is a useful model for studying how structure maps to receptor engagement: researchers have used it to probe which residues in the 1-29 span drive binding at GHRHR, a class-B G-protein-coupled receptor. Because the C-terminus is amidated and the chain is comparatively short, sermorelin is frequently cited as a benchmark against which longer-acting or backbone-modified GHRH analogs are compared in enzymatic-stability and receptor-activation assays. The research surrounding it remains preliminary and ongoing, and observations from cell-based or rodent systems should not be extrapolated to human or animal outcomes. Nothing here constitutes medical advice.
Published investigations involving sermorelin are predominantly in-vitro and rodent-model in nature and center on the GHRH receptor signaling axis. Reported experimental lines of inquiry include receptor-binding and competition assays at GHRHR, cyclic-AMP accumulation as a downstream readout of class-B GPCR activation in transfected or pituitary-derived cell lines, and comparative degradation studies examining cleavage of the peptide by dipeptidyl peptidase-IV (DPP-IV), which acts near the N-terminus and is a recurring focus when GHRH analogs are characterized for enzymatic stability.
These references describe experimental laboratory work only. They are not medical claims, are not evidence of safety or efficacy in humans or animals, and should not be interpreted as guidance for any use outside a controlled research environment.
Each research lot is supplied as a lyophilized white powder and characterized before release so that the material described on the Certificate of Analysis (COA) matches the sequence and mass expected for the 29-residue peptide amide. Identity and purity are established with orthogonal analytical methods, which separates purity (how much of the sample is the target peptide) from identity (confirmation that the target is the correct molecule). Because sermorelin contains a single methionine residue, oxidation-related variants are among the process impurities that reversed-phase methods are designed to resolve from the main peak.
The COA accompanying each product is the definitive analytical record for that specific lot. Because purity and mass can vary slightly between synthesis batches, researchers should reference the COA tied to the lot number received rather than generic specifications when documenting experimental inputs, and retain it alongside experimental records to support reproducibility and traceability.
As a lyophilized peptide, sermorelin is hygroscopic and sensitive to repeated temperature cycling; its single methionine also makes it prudent to minimize prolonged exposure to air and light in solution. Standard laboratory practice is to allow sealed vials to equilibrate to room temperature before opening to reduce condensation, to reconstitute with an appropriate research-grade solvent under aseptic technique, and to aliquot the reconstituted stock into single-use portions so that freeze-thaw cycles are limited. Detailed temperature and stability windows for lyophilized, reconstituted, and working solutions appear in the storage table on this page.
Sermorelin is a synthetic 29-amino-acid peptide amide (CAS 86168-78-7, formula C149H246N44O42S) that corresponds to the N-terminal 1-29 fragment of growth-hormone-releasing hormone, commonly written GRF(1-29) or GHRH(1-29)-NH2. That fragment is the shortest sequence of the parent hormone that retains the receptor-recognition region studied in vitro, which is why it is used as a reference GHRH peptide. It is supplied here at a 10 mg fill strictly for in-vitro and laboratory research.
It ships as a lyophilized (freeze-dried) white powder in a sealed vial containing 10 mg of peptide. Lyophilization improves shelf stability for a research peptide and lets the researcher reconstitute with a solvent of their choice under aseptic conditions when preparing in-vitro experiments. Handling and temperature windows are detailed in the storage table on this page.
Purity is measured by reversed-phase HPLC and reported as a percentage of total peak area (typically ≥98% for this listing), while identity is confirmed by mass spectrometry (ESI-MS or MALDI-TOF) against the theoretical mass for the amidated 29-residue sequence. The lot-specific COA documents both values plus appearance and net peptide content, and is the authoritative analytical record for the exact material you receive.
Published work is predominantly in-vitro and rodent-model and focuses on the GHRH receptor axis: receptor-binding and displacement assays at GHRHR, cAMP-based functional readouts of Gs-coupled signaling, and enzymatic-stability studies examining DPP-IV cleavage near the peptide's N-terminus. Sermorelin also serves as the GHRH(1-29) reference in structure-activity comparisons. This research is preliminary and ongoing and does not establish any human or animal outcome.
This product is sold strictly for in-vitro research and laboratory use only. It is not intended for human or animal consumption, diagnostic purposes, or therapeutic application.
By purchasing this product, you confirm that you are a qualified researcher operating within an appropriate laboratory environment and will use this compound in accordance with all applicable local, state, and federal regulations.
Amino Science Labs assumes no liability for misuse of this product outside of its intended research application.
Related
The sequence contains one methionine residue, which can form oxidation-related variants. Reversed-phase HPLC methods used for release are designed to resolve the main peak from these oxidation impurities and from truncated sequences, and it is standard practice to limit exposure of solutions to air and light. This is why laboratories treat oxidation control as part of characterizing and storing the material rather than an afterthought.
No. This material is supplied strictly for in-vitro and laboratory research use by qualified researchers. It is not a drug, supplement, or food, is not intended for human or animal consumption or any diagnostic or therapeutic purpose, and nothing on this page constitutes medical advice.
