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Merck
CN

F9145

Fibrinogen-binding Inhibitor Peptide

≥97% (HPLC)

Synonym(s):

Fibrinogen-γ Fragment 400-411

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About This Item

Empirical Formula (Hill Notation):
C50H80N18O16
CAS Number:
Molecular Weight:
1189.28
UNSPSC Code:
12352200
MDL number:
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SMILES string

CC(C)C[C@H](NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@@H](N)Cc2c[nH]cn2)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C(C)C)C(O)=O

assay

≥97% (HPLC)

composition

Peptide content, ~70%

UniProt accession no.

storage temp.

−20°C

Gene Information

human ... FGG(2266)

Biochem/physiol Actions

Fibrinogen γ 400-411, a non-RGD containing sequence, is derived from plasmin digestion. If platelet activation is blocked with prostaglandin E1 blockade, it is required for the establishment of initial contact and support spreading but not firm adhesion on immobilized substrate. However, in activated platelets, single γ 400-411 sequence is no longer required for initiation of adhesion but becomes sufficient for firm adhesion. In contrast to the binding of whole fibrinogen, binding of fragment 400-411 does not lead to tyrosine phosphorylation for platelet proteins.

Storage Class

13 - Non Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Regulatory Information

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B Savage et al.
The Journal of biological chemistry, 270(48), 28812-28817 (1995-12-01)
We have investigated how modulation of integrin alpha IIb beta 3 function influences the mechanisms that initiate platelet thrombus formation onto surface-bound fibrinogen and isolated fibrinogen domains. Under stationary conditions and with full activation of platelets blocked by prostaglandin E1
M M Huang et al.
The Journal of cell biology, 122(2), 473-483 (1993-07-01)
Tyrosine phosphorylation of multiple platelet proteins is stimulated by thrombin and other agonists that cause platelet aggregation and secretion. The phosphorylation of a subset of these proteins, including a protein tyrosine kinase, pp125FAK, is dependent on the platelet aggregation that

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