| Bioactivity | Fibrinogen-Binding Peptide (designed by anticomplementarity hypothesis) is a presumptive peptide mimic of the vitronectin binding site on the fibrinogen receptor. Fibrinogen-Binding Peptide 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 | ||||||
| CAS | 137235-80-4 | ||||||
| Sequence | Glu-His-Ile-Pro-Ala | ||||||
| Shortening | EHIPA | ||||||
| Formula | C25H39N7O8 | ||||||
| Molar Mass | 565.62 | ||||||
| Transport | Room temperature in continental US; may vary elsewhere. | ||||||
| Storage | Sealed storage, away from moisture
*In solvent : -80°C, 6 months; -20°C, 1 month (sealed storage, away from moisture) |
Fibrinogen-Binding Peptide
CAS: 137235-80-4 F: C25H39N7O8 W: 565.62
Fibrinogen-Binding Peptide (designed by anticomplementarity hypothesis) is a presumptive peptide mimic of the vitronecti
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