| Bioactivity | Fibrinogen-Binding Peptide TFA (designed by anticomplementarity hypothesis) is a presumptive peptide mimic of the vitronectin binding site on the fibrinogen receptor. Fibrinogen-Binding Peptide TFA binds fibrinogen and inhibits both the adhesion of platelets to fibrinogen and platelet aggregation, and also inhibits the adhesion of platelets to vitronectin[1]. | ||||||
| Name | Fibrinogen-Binding Peptide TFA | ||||||
| Formula | C27H40F3N7O10 | ||||||
| Molar Mass | 679.64 | ||||||
| Appearance | Solid | ||||||
| Transport | Room temperature in continental US; may vary elsewhere. | ||||||
| Storage | Sealed storage, away from moisture and light, under nitrogen
*In solvent : -80°C, 6 months; -20°C, 1 month (sealed storage, away from moisture and light, under nitrogen) |
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| Reference | [1]. Gartner TK, et al. The peptide Glu-His-Ile-Pro-Ala binds fibrinogen and inhibits platelet aggregation and adhesion to fibrinogen and vitronectin. Proc Soc Exp Biol Med. 1991 Oct;198(1):649-55. |
Fibrinogen-Binding Peptide TFA
CAS: F: C27H40F3N7O10 W: 679.64
Fibrinogen-Binding Peptide TFA (designed by anticomplementarity hypothesis) is a presumptive peptide mimic of the vitron
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