89105-94-2

89105-94-2 structure

Name: Fibrinogen-Binding Inhibitor Peptide
Chemical Name: Fibrinogen Binding Inhibitor Peptide
CAS Number: 89105-94-2
Molecular Formula: C₅₀H₈₀N₁₈O₁₆
Molecular Weight: 1189.28000
Catalog: Peptides
Create Date: 2018-12-26 12:22:25
Modify Date: 2024-01-12 18:50:02
Fibrinogen Binding Inhibitor Peptide is a dodecapeptide (HHLGGAKQAGDV, H12), which is a fibrinogen γ-chain carboxy-terminal sequence (γ400-411). Fibrinogen Binding Inhibitor Peptide is a specific binding site of the ligand for activated glycoprotein (GP) IIb/IIIa.

Name	Fibrinogen Binding Inhibitor Peptide
Synonyms	MFCD00167528 FIBRINOGEN-BINDING INHIBITOR PEPTIDE H-HIS-HIS-LEU-GLY-GLY-ALA-LYS-GLN-ALA-GLY-ASP-VAL-OH Fibrinogen Binding Inhibitory Peptide HHLGGAKQAGDV HIS-HIS-LEU-GLY-GLY-ALA-LYS-GLN-ALA-GLY-ASP-VAL FIBRINOGEN Y-CHAIN DODECAPETIDE FIBRINOGEN-BINDING INHIBITOR PEPTIDE Fibrinogen Binding Inhibitor Peptide

Description	Fibrinogen Binding Inhibitor Peptide is a dodecapeptide (HHLGGAKQAGDV, H12), which is a fibrinogen γ-chain carboxy-terminal sequence (γ400-411). Fibrinogen Binding Inhibitor Peptide is a specific binding site of the ligand for activated glycoprotein (GP) IIb/IIIa.
Related Catalog	Signaling Pathways >> Others >> Others Peptides Research Areas >> Cardiovascular Disease
In Vitro	Glycoprotein (GP) IIb/IIIa, which exists on the membrane of platelets, changes its form from inactive to active when platelets adhere to collagen exposed on sites of vascular injury. In the circulation, platelet aggregation is mediated by fibrinogen by bridging adjacent platelets through GPIIb/IIIa in an activation-dependent manner. A dodecapeptide HHLGGAKQAGDV (H12), corresponding to the fibrinogen γ-chain carboxy-terminal sequence (γ400-411), is a specific binding site of the ligand for activated GPIIb/IIIa[1].
References	[1]. Okamura Y, et al. Release abilities of adenosine diphosphate from phospholipid vesicles with different membraneproperties and their hemostatic effects as a platelet substitute. J Control Release. 2010 Dec 20;148(3):373-9.