Semaglutide

Supplied as a sterile lyophilized powder, Semaglutide 10 mg arrives in a light-protected vial labeled with its lot number for traceability, along with reconstitution and storage guidance for research applications. Semaglutide is a synthetic, 31-amino-acid peptide and GLP-1 receptor agonist with the molecular formula C₁₈₇H₂₉₁N₄₅O₅₉, a molecular weight of approximately 4,113.6 g/mol, and CAS number 910463-68-2. The peptide backbone follows the sequence His-Aib-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Val-Ser-Ser-Tyr-Leu-Glu-Gly-Gln-Ala-Ala-Lys-Glu-Phe-Ile-Ala-Trp-Leu-Val-Arg-Gly-Arg-Gly, with three modifications relative to native human GLP-1(7-37) that define its identity as a distinct research analog rather than a direct copy of the endogenous hormone. At position 2, 2-aminoisobutyric acid (Aib) replaces the naturally occurring alanine residue; because Aib is a sterically hindered, non-proteinogenic amino acid, it is not recognized as a cleavage site by dipeptidyl peptidase-4 (DPP-4), the enzyme primarily responsible for the rapid degradation of native GLP-1. At the lysine position corresponding to residue 26, a C18 fatty-diacid side chain is attached through a linker built from gamma-glutamic acid and two discrete PEG-based spacer units, giving the molecule a hydrophobic "arm" that is central to its research-relevant binding behavior. At position 34, arginine replaces the native lysine, a substitution primarily used to control the site of chemical conjugation during synthesis of the fatty-diacid chain. Collectively, these modifications make semaglutide roughly 94% homologous to human GLP-1(7-37) rather than identical to it — close enough to retain receptor recognition, but chemically distinct enough that data generated on native GLP-1 cannot be assumed to transfer directly to this synthetic analog, or vice versa. This distinction matters for anyone using the product in structure-activity relationship (SAR) work or comparative binding studies. The 10 mg designation refers to the total mass of lyophilized peptide contained in the vial, a standard research-supply format across the peptide industry. Peptides in dry, lyophilized form are substantially more chemically stable than in solution: once reconstituted, exposure to water, light, and ambient temperature accelerates degradation pathways such as deamidation, oxidation of susceptible residues, and aggregation, which is why the lyophilized vial is shipped and stored frozen and protected from light until a researcher is ready to prepare a working solution under their own laboratory protocols. The CAS number 910463-68-2 is the unique registry identifier assigned to semaglutide by the Chemical Abstracts Service, a standardized reference used across scientific literature, regulatory filings, and vendor documentation to unambiguously identify the exact compound independent of trade name or supplier. The molecular formula C₁₈₇H₂₉₁N₄₅O₅₉ describes the total atomic composition of the modified peptide — 187 carbon, 291 hydrogen, 45 nitrogen, and 59 oxygen atoms — reflecting both the 31-residue peptide backbone and the C18 fatty-diacid/spacer modification attached at position 26. Researchers cross-referencing semaglutide across different literature sources or supplier documentation can use the CAS number and molecular formula together to confirm they are comparing data on the same compound, regardless of how a given source names or brands it.

Semaglutide is a long-acting GLP-1 receptor agonist studied extensively for its effects on glucose-dependent insulin secretion, gastric emptying, and satiety signaling in metabolic research models. As a synthetic analog of human GLP-1, semaglutide binds the GLP-1 receptor (GLP-1R), a class B G protein-coupled receptor, and activates downstream cAMP signaling — the basis for its use in receptor-binding assays, incretin-signaling studies, and in vitro metabolic models. This scientific identity is separate from the clinical evidence associated with FDA-approved semaglutide medicines such as Ozempic, Wegovy, and Rybelsus; that evidence describes those approved drug products and does not extend to this or any other research-use material. GLP-1R is expressed on pancreatic beta cells and in other tissues studied in incretin research, including regions of the gastrointestinal tract and central nervous system relevant to appetite and gastric-emptying signaling. Ligand binding at GLP-1R triggers a conformational shift in the receptor that couples to the Gαs subunit, activating adenylate cyclase and raising intracellular cAMP. The resulting cAMP signal engages both protein kinase A (PKA) and the exchange protein Epac2, two parallel effector pathways that researchers study for their respective roles in glucose-dependent insulin secretion from beta cells. Because this activation is glucose-dependent, in vitro models often examine how GLP-1R agonism behaves differently under varying glucose concentrations — a common experimental variable in incretin pharmacology research. The C18 fatty-diacid side chain described in the Product Details section is itself a subject of structural research interest: this modification promotes reversible, non-covalent binding to serum albumin, a property studied for its influence on a molecule's apparent half-life and receptor exposure profile in in vitro and ex vivo systems. Researchers examining long-acting incretin analogs frequently compare albumin-binding fatty-acid or fatty-diacid modifications across different GLP-1 receptor agonists to understand how side-chain chemistry affects receptor residence time and clearance behavior at the molecular level — independent of any human dosing consideration. Common research applications built around this scientific profile include GLP-1 receptor binding and displacement assays, cAMP reporter-gene assays in receptor-transfected cell lines, in vitro incretin and glucose-signaling models, comparative SAR studies against native GLP-1 and other GLP-1 receptor agonists, and stability or degradation studies examining how the Aib substitution and fatty-diacid modification affect resistance to enzymatic and chemical breakdown relative to unmodified GLP-1. Extensive clinical trial evidence exists for GLP-1 receptor agonism in FDA-approved pharmaceutical products, including data on glycemic control and body-weight effects in human populations. That evidence was generated using specific approved formulations, manufacturing processes, and regulatory oversight applicable to those drug products. It does not establish safety, purity, potency, or efficacy for this or any other research-use-only material, and should not be read as characterizing this product. GLP-1 belongs to a small class of gut-derived hormones known as incretins, alongside glucose-dependent insulinotropic polypeptide (GIP). Incretins are released from intestinal cells in response to nutrient intake and act on pancreatic beta cells to potentiate insulin secretion beyond what elevated blood glucose alone would trigger — a phenomenon researchers refer to as the incretin effect. Native GLP-1 has a circulating half-life of only a few minutes because it is rapidly cleaved by DPP-4, which limits its usefulness as a stable reagent for extended in vitro experiments. Synthetic analogs such as semaglutide were designed specifically to resist this degradation pathway, making them more practical tools for researchers studying sustained GLP-1 receptor activation, receptor desensitization kinetics, or downstream signaling over timeframes that native GLP-1 could not support in solution. This is one of the reasons semaglutide and related long-acting GLP-1 receptor agonists are frequently selected for in vitro incretin research over native GLP-1 itself.

Semaglutide 10 mg is manufactured under strict quality controls and independently verified via HPLC and mass spectrometry before release, ensuring each vial matches its published purity and identity profile. Purity is determined by reverse-phase high-performance liquid chromatography (RP-HPLC) with UV detection. The peptide sample is separated on a chromatographic column, and the resulting chromatogram is integrated to calculate the percentage of total peak area attributable to the target compound relative to all detected peaks, including any process-related impurities or truncated synthesis by-products. A result of 99.5%+ purity means the semaglutide peak accounts for that proportion of the total integrated area under the conditions used for that specific analysis. Mass spectrometry is used separately to confirm molecular identity rather than purity. Techniques such as electrospray ionization mass spectrometry (ESI-MS) measure the mass-to-charge ratio of ionized peptide fragments, and the observed mass is compared against the theoretical molecular weight of approximately 4,113.6 Da calculated from the intended sequence and modifications. A match within acceptable tolerance confirms that the synthesized molecule corresponds to the intended structure — including the Aib substitution, fatty-diacid attachment, and Arg substitution described above — and helps rule out common synthesis errors such as truncated sequences, missing modifications, or incorrect residue incorporation. The Certificate of Analysis (COA) provided with each batch ties these results to a specific, physical lot of product rather than a generic specification sheet. The batch number on the COA is matched to the lot number printed on the vial label, allowing a researcher to confirm that the documentation in hand corresponds to the exact vial being used. The purity percentage and analysis date reported on the COA reflect the testing performed on that particular batch at that point in time, rather than a standing claim applied uniformly across all production runs. Retaining and cross-checking this batch-specific documentation supports reproducibility when reporting materials and methods in research contexts. Third-party testing means the analytical work — HPLC purity and mass spectrometry identity — is performed by a laboratory independent of the manufacturer, rather than solely through in-house quality control. This distinction matters for research reproducibility: results generated by an independent lab are not subject to the same potential conflict of interest as testing conducted and reported exclusively by the seller of the material. When citing a source's identity or purity in a lab notebook, methods section, or internal research log, noting that the result comes from independent third-party analysis — along with the specific batch number and analysis date from the COA — gives other researchers a clearer basis for evaluating and reproducing the reported findings. It is worth stating plainly what these analytical methods do and do not establish. HPLC purity and mass spectrometry identity testing characterize the chemical composition of the material — they confirm what the compound is and how pure the sample is by chromatographic and mass measures. They do not test for sterility, endotoxin content, or biological activity, and they do not establish that the material is safe, effective, or appropriate for use in humans or animals. A high purity result and a matching mass spectrum describe a well-characterized research chemical; they do not describe a clinically evaluated product.

This product is intended for in-vitro laboratory research only. Semaglutide 10 mg is not approved for human or veterinary use, has not been reviewed by the FDA, and must not be used as a food, drug, or cosmetic. It is not the same as, equivalent to, or a substitute for any FDA-approved semaglutide medicine, including Ozempic, Wegovy, or Rybelsus. It is not intended for human or animal consumption, diagnostic use, or therapeutic use of any kind, and must be handled only by qualified researchers in an appropriate laboratory setting. Purchasing this product constitutes an acknowledgment that it is intended solely for qualified laboratory and in-vitro research use, that it will not be administered to humans or animals, and that it will not be represented, resold, or used as a treatment, supplement, or consumer health product of any kind.