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Research Peptide
Semaglutide research compound
Fast shipping
Same-day dispatch
Third-party tested
U.S. accredited labs
99%+ purity
HPLC verified
31AA
SEQUENCE LENGTH
Modified GLP-1 analogue
~7days
HALF-LIFE
Extended via albumin binding
3000+
PUBLICATIONS
Most studied GLP-1 RA compound
94%
HOMOLOGY
To native human GLP-1
2017
FDA APPROVED
For type 2 diabetes (Ozempic)
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on orders over $150
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99%+ purity verified
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Research
This listing supplies semaglutide (CAS 910463-68-2, molecular formula C187H291N45O59) as a lyophilized peptide reference material for in-vitro and preclinical laboratory work only. Semaglutide is a synthetic acylated analog of human glucagon-like peptide-1 (GLP-1), engineered from the GLP-1(7-37) backbone rather than isolated from a natural source. Its defining structural features, frequently cited in the research literature, are three deliberate modifications: substitution of alanine at position 8 with 2-aminoisobutyric acid (Aib) to hinder dipeptidyl peptidase-IV (DPP-IV) cleavage, an arginine substitution at position 34, and attachment of a C18 diacid fatty-acid chain through a gamma-glutamate/mini-PEG spacer to a lysine at position 26. Together these make it a substantially larger and more chemically complex molecule than native GLP-1, which is reflected in its high-molecular-weight formula and its handling requirements.
The material is intended for qualified researchers characterizing GLP-1 receptor pharmacology, peptide stability, and analog behavior on the bench. It is offered as a characterized reference compound only. All descriptions below concern the research substance itself, its documented study history in laboratory models, and standard handling of a freeze-dried peptide standard; none are statements about outcomes in humans or animals.
The preclinical and in-vitro literature around semaglutide centers on its identity as a GLP-1 receptor (GLP-1R) agonist and on the pharmacological consequences of its acylation and Aib substitution. The themes below are described strictly as observations in laboratory systems, are preliminary and ongoing, and do not establish effects in humans:
Because experimental parameters such as cell type, receptor construct, concentration range, and endpoint vary widely between reports, cross-study generalization is not supported by the current data. Researchers reviewing this literature typically treat it as mechanistic and hypothesis-generating; observations in isolated cells or animal models do not establish results in other biological systems. This information is educational only and is not medical advice.
Research Context
Findings summarized here derive from isolated-cell, receptor-pharmacology, and preclinical model studies. They are hypothesis-generating, have not been established as clinical outcomes, and are provided as neutral scientific background, not as a claim of safety or efficacy and not as medical advice.
For a modified 31-residue peptide bearing a lipophilic acyl side chain, analytical verification is central to reproducible results, because both sequence fidelity and correct fatty-acid conjugation must be confirmed. Research-grade semaglutide is typically assessed by reversed-phase high-performance liquid chromatography (RP-HPLC) to quantify chromatographic purity, reported as area-percent of the main peak; lots supplied here are specified at ≥99% purity. The chromatographic method resolves the target from related species such as truncated sequences and des-acyl impurities that lack the side chain.
Identity is confirmed by mass spectrometry (commonly ESI-MS or MALDI-TOF), matching the observed mass against the theoretical value for the C187H291N45O59 composition and thereby verifying both the peptide backbone and the presence of the C18 diacid modification rather than the unmodified analog. A lot-specific Certificate of Analysis (COA) documents these analyses. Because a lyophilized peptide vial contains counter-ion and residual water alongside the peptide, the net peptide mass can differ from the gross fill weight, so reviewing the lot-matched COA for purity, mass-spec identity, and net peptide content before use is standard practice and directly affects the accuracy of calculated stock concentrations.
The following describes conventional handling of lyophilized research peptides and is not instruction for human or animal use. Sealed semaglutide powder is kept cold, desiccated, and protected from light. Because the acylated peptide is amphiphilic and can be sensitive to surface adsorption and freeze-thaw cycling, sealed vials are generally equilibrated to room temperature before opening to limit condensation, then reconstituted under aseptic technique in a documented research-grade solvent. Aliquoting reconstituted stock into single-use portions limits repeated freeze-thaw that can degrade peptide integrity. Specific temperature and time windows for lyophilized, reconstituted, and working solutions appear in the storage specifications on this page.
Semaglutide (CAS 910463-68-2) is a synthetic acylated analog of human GLP-1(7-37), engineered with an Aib8 substitution, an Arg34 substitution, and a C18 diacid fatty-acid chain conjugated at Lys26 through a gamma-glutamate/mini-PEG spacer. It is supplied as a lyophilized (freeze-dried) peptide for in-vitro and preclinical laboratory research as a GLP-1 receptor agonist reference compound. It is a research chemical for laboratory use only, not a therapeutic product, and not for human or animal consumption.
It shares the GLP-1(7-37) backbone but carries three engineered changes: 2-aminoisobutyric acid replaces alanine at position 8, arginine replaces lysine at position 34, and a C18 diacid fatty-acid chain is attached at position 26 via a spacer. In research contexts the Aib8 substitution is significant because it hinders DPP-IV cleavage, while the fatty-acid chain promotes reversible albumin binding, both of which contribute to its extended measurable half-life in experimental systems relative to native GLP-1.
Laboratory studies characterize it as an agonist at the GLP-1 receptor, a G-protein-coupled receptor, with downstream cyclic-AMP signaling used as an in-vitro endpoint in receptor-transfected or endocrine-derived cell lines. Additional research examines its enzymatic stability versus native GLP-1 and the albumin-binding behavior driven by its fatty-acid chain. These are mechanistic, model-based observations from preliminary and ongoing research and do not establish effects in humans.
Purity is assessed by reversed-phase HPLC and reported as area-percent of the main chromatographic peak, with lots here specified at ≥99%. Mass spectrometry (ESI-MS or MALDI-TOF) confirms the molecular mass against the C187H291N45O59 composition, verifying both the peptide backbone and the presence of the C18 diacid modification. A lot-specific Certificate of Analysis (COA) records these results along with net peptide content.
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.
A lyophilized peptide vial contains counter-ion and residual water in addition to the peptide, so the net peptide mass can be lower than the gross fill weight. Reviewing the lot-matched COA for reported net peptide content and HPLC purity lets researchers calculate accurate stock concentrations, which is essential for reproducible in-vitro work. Archiving the COA with experimental records also supports traceability.
No. This material is a research chemical supplied strictly for in-vitro and preclinical laboratory research 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 or a claim of safety or efficacy.
