F9145
Fibrinogen-binding Inhibitor Peptide
≥97% (HPLC)
别名:
Fibrinogen-γ Fragment 400-411
Amino Acid Sequence
His-His-Leu-Gly-Gly-Ala-Lys-Gln-Ala-Gly-Asp-Val
生化/生理作用
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.
储存分类代码
13 - Non Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
此项目有
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
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
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