For research use only. Not for human or veterinary use. Sold strictly for in-vitro laboratory research; not for diagnosis or treatment.
Every research compound in the catalogue belongs to one research area. Most areas are defined by molecular class: how a sequence is built, how it is modified and which structural family it sits in. The mitochondrial compounds are grouped by research field instead. Choose an area to see its compounds and their identifiers.
4 compounds
Synthetic lipidated peptide analogues of roughly thirty to forty residues, listed with formula and molecular weight.
4 compounds
Linear synthetic peptides such as the fifteen-residue BPC-157, listed with sequence and formula, and co-lyophilised blends of them.
3 compounds
Synthetic and recombinant analogues grouped by receptor class, from the pentapeptide ipamorelin to the eighty-three-residue IGF-1 LR3.
3 compounds
Lactam-bridged cyclic heptapeptides and GHK-Cu, the copper(II) complex of the tripeptide Gly-His-Lys, listed with formulas.
3 compounds
MOTS-c, the aromatic-cationic tetrapeptide SS-31 and the dinucleotide NAD+, catalogued together for mitochondrial research.
2 compounds
Two synthetic heptapeptides, Semax and Selank, each a short sequence extended at the C-terminus by the tripeptide Pro-Gly-Pro.
| Research area | Defining structure | Compounds | Examples | Residue range |
|---|---|---|---|---|
| Incretin & Amylin Analogues | Lipidated chains of about thirty to forty residues | 4 | GLP-3, Tirzepatide, Cagrilintide | 31–39 |
| Peptide Fragments | Linear chains without cyclisation or lipidation, and their blends | 4 | TB-500, BPC-157, BPC-157 / TB-500 Mix | 15–43 |
| GHRH, GHS-R & IGF-1 Analogues | Analogues grouped by the receptor class of their parent peptide | 3 | Tesamorelin, IGF-1 LR3, Ipamorelin | 5–83 |
| Melanocortin & Copper Peptides | Lactam-bridged cyclic heptapeptides and a copper(II) tripeptide complex | 3 | GHK-Cu, MT2, PT-141 | 3–7 |
| Mitochondrial Compounds | Two peptides and a dinucleotide, grouped by research field | 3 | NAD+, SS-31, MOTS-c | 4–16 |
| Neuropeptides | Heptapeptides extended by a C-terminal Pro-Gly-Pro | 2 | Semax, Selank | 7 |
A research area here is a molecular class: a group of compounds that share a way of being built. The grouping follows the chemistry of each molecule, meaning its chain length, its modifications and the structural family its sequence comes from, so the compounds in one area are read with the same set of identifiers and analysed with similar methods. Each label names that class directly, such as Peptide Fragments for linear chains without cyclisation or lipidation, or Neuropeptides for two heptapeptides that end in the same Pro-Gly-Pro tripeptide.
Every compound in the catalogue sits in exactly one area, placed by its defining structural feature, and each hub names that feature in its opening paragraph. The mitochondrial compounds are the one group organised by research field instead of by class. Every hub lists its compounds with CAS number, molecular formula, molecular weight, residue count and the lowest price per milligram, then sets out the structural features, the analytical points and further reading for the class.
Residue count is the quickest way to place a compound. The catalogue runs from the three residues of GHK-Cu to the eighty-three of IGF-1 LR3. Short chains of up to about ten residues, such as the heptapeptides and the tetrapeptide SS-31, give simple mass spectra dominated by singly and doubly charged ions, while chains of thirty residues or more appear as a series of multiply charged ions that are deconvoluted to a neutral mass. The residue range column above shows where each area sits on that scale.
A ring changes how a sequence is written and how it is checked. In the lactam-bridged heptapeptides, an amide bond between the side chains of an aspartic acid and a lysine closes a ring of six residues, written with the cyclo[…] bracket, and the cyclised molecule is 18 Da lighter than its open-chain precursor. Cagrilintide holds a short ring of its own, closed by a disulfide bridge between its two cysteines. The chains in Peptide Fragments and Neuropeptides are linear, with free termini at both ends.
A covalently attached lipid group is the signature of the Incretin & Amylin Analogues area. A long-chain dicarboxylic acid, joined to the peptide through a linker such as a γ-glutamic acid residue, adds a hydrocarbon chain to an otherwise polar peptide. That lengthens retention in reversed-phase HPLC, so these compounds run on steeper organic gradients, and it adds the mass of the diacid and linker to the chain. Their formulas and molecular weights always describe the whole conjugate.
A bound metal ion makes a compound a coordination complex as well as a peptide. GHK-Cu is the copper(II) complex of the tripeptide Gly-His-Lys, and its formula, C14H22CuN6O4, includes the copper. Analysis covers both parts: the peptide by chromatography and mass spectrometry, the copper content separately, and the characteristic copper-63 and copper-65 isotope pattern in a mass spectrum shows that the metal is present in the ion being measured.
Several compounds carry residues outside the twenty standard L-amino acids: α-aminoisobutyric acid (Aib) in semaglutide and ipamorelin, D-2-naphthylalanine and D-phenylalanine in ipamorelin, norleucine in the cyclic heptapeptides and 2′,6′-dimethyltyrosine in SS-31. A D-configured residue leaves the formula and the mass unchanged, so a diastereomer is told apart by chromatography rather than by mass, and each product page writes these residues out in its sequence.