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Fibrinogen-Binding Peptide Sale

目录号 : GC66420

Fibrinogen-Binding Peptide 是一种通过抗完全性假说设计的纤维蛋白原受体上玻连蛋白结合位点的假定肽模拟物。Fibrinogen-Binding Peptide 结合纤维蛋白原,抑制血小板对纤维蛋白原的粘附和血小板聚集,也抑制血小板对氟噻嗪的粘附。

Fibrinogen-Binding Peptide Chemical Structure

Cas No.:137235-80-4

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5mg
¥756.00
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10mg
¥1,166.00
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Sample solution is provided at 25 µL, 10mM.

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产品描述

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].

Chemical Properties

Cas No. 137235-80-4 SDF Download SDF
分子式 C25H39N7O8 分子量 565.62
溶解度 DMSO : 125 mg/mL (221.00 mM; Need ultrasonic) 储存条件 Store at -20°C
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溶解性数据

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1 mg 5 mg 10 mg
1 mM 1.768 mL 8.8399 mL 17.6797 mL
5 mM 0.3536 mL 1.768 mL 3.5359 mL
10 mM 0.1768 mL 0.884 mL 1.768 mL
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Research Update

Promotion of phagocytosis of Streptococcus pyogenes in human blood by a Fibrinogen-Binding Peptide

Microbes Infect 2011 Apr;13(4):413-8.PMID:21241819DOI:10.1016/j.micinf.2010.12.008.

The binding of fibrinogen to M-related protein (Mrp) is known to contribute to the ability of Streptococcus pyogenes to evade phagocytosis by preventing the deposition of complement on the streptococcal surface. The objectives of this investigation were to map the common fibrinogen-binding domain of Mrp and to determine if this domain has a therapeutic potential to enhance phagocytosis of S. pyogenes in human blood. Using a series of recombinant, truncated proteins of Mrp, two fibrinogen-binding domains (FBD) were mapped. FBD1 was contained within amino acid residues 1-55 of Mrp and FBD2 within residues 81-138. FBD2 is found in all Mrp sequenced to date whereas FBD1 is not. Both FBD1 and FBD2 peptides but not a control peptide blocked the binding of fibrinogen to S. pyogenes and promoted phagocytosis of the streptococci in human blood. The data support the hypothesis that the binding of fibrinogen by S. pyogenes is centrally involved in their resistance to phagocytosis in human blood and suggest that treatments that interfere with the binding of fibrinogen to S. pyogenes may help in fighting infections by these organisms.