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Merck
CN

A5048

Adenosine 5′-diphosphate–Agarose

saline suspension

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UNSPSC Code:
41106500
MDL number:
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form

saline suspension

extent of labeling

1-3 μmol per mL

matrix

4% beaded agarose

matrix activation

cyanogen bromide

matrix attachment

ribose hydroxyls

matrix spacer

11 atoms (adipic acid dihydrazide)

storage temp.

2-8°C

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Application

Adenosine 5′-diphosphate has been used in the research of platelet integrin α(IIb)β3, which is crucial for platelet aggregation. It has been determined that the interaction between Adenosine 5′-diphosphate and the receptor P2Y12 is needed for the maintenance of integrin α(IIb)β3 activation.

Physical form

Suspension in 0.5 M NaCl containing 0.02% thimerosal

存储类别

10 - Combustible liquids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

法规信息

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分析证书(COA)

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C R Tinsley et al.
Infection and immunity, 61(9), 3703-3710 (1993-09-01)
The important human pathogens Neisseria meningitidis and Neisseria gonorrhoeae accumulate phosphate in the form of polyphosphate (A. Noegel and E. C. Gotschlich, J. Exp. Med. 157:2049-2060, 1983), and the localization of more than half of this long-chain polymer on the
Knut Fälker et al.
Thrombosis and haemostasis, 92(1), 114-123 (2004-06-24)
Stimulating human platelets with thrombin induces the activation of the extracellular signal-regulated kinase 2 (ERK2). We demonstrate that this effect is highly dependent on ADP secretion and P2Y12 receptor signalling. AR-C69931MX (10 microM), a specific antagonist of the Gi-coupled P2Y12
T Kamae et al.
Journal of thrombosis and haemostasis : JTH, 4(6), 1379-1387 (2006-05-19)
Platelet integrin alpha(IIb)beta3 plays a crucial role in platelet aggregation, and the affinity of alpha(IIb)beta3 for fibrinogen is dynamically regulated. Employing modified ligand-binding assays, we analyzed the mechanism by which alpha(IIb)beta3 maintains its high-affinity state. Washed platelets adjusted to 50
Francesca Campus et al.
The Journal of biological chemistry, 280(26), 24386-24395 (2005-05-03)
Binding of thrombopoietin (TPO) to the cMpl receptor on human platelets potentiates aggregation induced by a number of agonists, including ADP. In this work, we found that TPO was able to restore ADP-induced platelet aggregation upon blockade of the G(q)-coupled

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