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| Description | RGD Trifluoroacetate (CAS: 2378808-45-6) is the TFA salt of the minimal tripeptide sequence Arg-Gly-Asp recognized by integrins. TFA salt C₁₄H₂₃F₃N₆O₈, MW 460.36 Da; free base C₁₂H₂₂N₆O₆, MW 346.34 Da. The RGD motif is the core integrin-binding site of fibronectin, fibrinogen, and other extracellular-matrix proteins; it inhibits platelet aggregation and fibrinogen binding, and is used in integrin-binding mechanism and biomaterial-surface-functionalization research. |
| Structure type | Linear 3-mer (RGD minimal motif, TFA salt) |
| Solubility | Readily soluble in water, PBS |
| Storage | Powder -20°C, dry, protected from light |
Product Basic Information Table
| Product Standard English Name | Product Abbreviation / Alias | Function Tags (comma-separated) | Core Structure | Molecular Formula | Exact Mass (Da) | Average MW (Da) | Salt Form | Length (aa) |
| Arg-Gly-Asp (RGD), minimal RGD integrin-recognition motif tripeptide, trifluoroacetate (TFA) salt | RGD; Arg-Gly-Asp; minimal integrin-recognition motif; H-Arg-Gly-Asp-OH (TFA salt); CAS 2378808-45-6 | RGD tripeptide, minimal integrin-recognition motif, cell adhesion, TFA salt, integrin-antagonist lead | Linear tripeptide H-Arg-Gly-Asp-OH; the minimal RGD integrin-recognition motif itself, N-terminal Arg and C-terminal Asp; net side-chain charge ~0 (Arg +1 / Asp -1, plus N-term +1 / C-term -1); no Cys/Met/Trp; good water solubility; supplied as a trifluoroacetic-acid (TFA) counterion salt; free-peptide sequence, TFA salt CAS 2378808-45-6 | C12H22N6O6 | 346.16 | 346.34 | TFA salt (trifluoroacetate counterion); the formula/MW above are for the free peptide C12H22N6O6 (exact 346.16 / avg 346.34 Da); the TFA salt form is C14H23F3N6O8 (exact 460.15 / avg 460.37 Da); CAS 2378808-45-6 | 3 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-RGD-TFA-01 | White to off-white powder (TFA salt; more hygroscopic than the free base, requires desiccated sealed storage) | Store at -20°C, sealed, desiccated, protected from light (~2 years). Aliquot to avoid repeated freeze-thaw. No Cys/Met/Trp-low oxidation risk. The TFA salt is hygroscopic: weigh quickly and immediately reseal in a desiccator (or under nitrogen) to prevent moisture uptake. | 2–8°C for up to ~1 month; working aliquots at -20°C; stable for shipping at ambient (protect from moisture). | RGD tripeptide with good water solubility, readily dissolved in aqueous buffers (PBS, pure water) at ≥10 mg/mL. No Cys (no disulfide), no Met (no oxidation), no Trp (no photo-oxidation). Prepare fresh or store working aliquots at -20°C. NOTE: this is the TFA salt containing a trifluoroacetate counterion; for salt-/TFA-sensitive cell or in-vivo studies, use the free-base version, since TFA at low pH can affect some cell-culture systems. | solid stable for ~2 years at -20°C, sealed and desiccated. The TFA salt is more hygroscopic than the free base, so keep the desiccator sealed and weigh quickly in a dry environment. |
Functional Description
| Product Code | Frontend Short Summary | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Pathways |
| PEP-RGD-TFA-01 | The TFA-salt form of the minimal RGD integrin-recognition motif Arg-Gly-Asp. It competitively blocks integrin binding to ECM ligands, inhibits cell-matrix adhesion and platelet aggregation, and is a core tool peptide for integrin-antagonist lead discovery and cell-adhesion control studies. | This is the trifluoroacetic-acid (TFA) salt of the minimal RGD integrin-recognition motif Arg-Gly-Asp (RGD). The RGD tripeptide itself is the smallest functional unit within ECM proteins (fibrinogen, fibronectin, vitronectin, etc.) recognized by integrins, and it directly occupies the ligand-binding pocket of integrin heterodimers (αIIbβ3/GPIIb/IIIa, αvβ3, αvβ5, α5β1, etc.). Because it is small and rapidly penetrating, the RGD tripeptide acts as a competitive inhibitor that blocks cell adhesion, spreading and migration on ECM-coated surfaces and inhibits fibrinogen-bridged platelet aggregation-making it a classic tool for integrin-dependent adhesion, tumor invasion and angiogenesis studies, as well as the lead scaffold for designing cyclic RGD (e.g., cRGDfK) and αvβ3-targeted imaging/drug delivery. Supplied with a TFA counterion, it favors lyophilization and weighing; however, the TFA salt is more hygroscopic than the free base and requires desiccated sealed storage, and TFA-/low-pH-sensitive cell or in-vivo studies should use the free-base version. Containing no Cys/Met/Trp, oxidation and photo-oxidation risks are low, and water solubility is good; the RGD tripeptide serves as an integrin-antagonist lead and a negative control for cell adhesion. | Integrin-antagonist lead, cell-adhesion control, platelet-aggregation inhibition, tumor invasion/metastasis, angiogenesis, αvβ3-targeted imaging and drug-delivery lead, peptide drug design | Integrins αIIbβ3 (GPIIb/IIIa), αvβ3, αvβ5, α5β1; fibrinogen/fibronectin binding sites; focal-adhesion and FAK signaling; cyclic-RGD lead scaffold |
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