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Unterstützung erhaltenProduktname
Sepharose™ 2B, 60-200 μm bead diameter
form
suspension
bead diameter
60-200 μm
storage temp.
2-8°C
Quality Level
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General description
Sepharose 2B is a well-proven cross-linked agarose gel filtration base matrix and is frequently used for coupling affinity ligands to the matrix. The matrix is not pre-activated and the user performs all steps in coupling.
Legal Information
Sepharose is a trademark of Cytiva
signalword
Danger
hcodes
Hazard Classifications
Flam. Liq. 2
Lagerklasse
3 - Flammable liquids
wgk
WGK 3
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Depletion of glycoprotein gp85 from virosomes made with Epstein-Barr virus proteins abolishes their ability to fuse with virus receptor-bearing cells.
Haddad RS and Hutt-Fletcher LM
Journal of Virology, 63, 4998-4998 (1989)
Regulation of the phosphoinositide cycle by Na+/H+ exchange and intracellular pH in human platelets.
G Luzzatto et al.
Biochimica et biophysica acta, 1084(1), 78-86 (1991-06-19)
We have found that thrombin-induced activation of protein kinase C (PKC) in platelets, measured by phosphorylation of the 47 kDa protein, is synergistically enhanced by the amiloride analogue ethylisopropylamiloride (EIA), a specific inhibitor of Na+/H+ exchange. This EIA effect was
Balakrishnan Sivaraman et al.
Langmuir : the ACS journal of surfaces and colloids, 28(5), 2745-2752 (2011-12-24)
Recent studies have shown that platelets can adhere to adsorbed albumin (Alb) through a receptor-mediated mechanism, but only if the Alb undergoes more than a critical degree of adsorption-induced unfolding. The objectives of this research were to investigate whether Alb
Z Guo et al.
Thrombosis research, 71(1), 77-88 (1993-07-01)
ATA is a novel anticoagulant polymeric anionic aromatic compound that inhibits von Willebrand factor binding to platelet glycoprotein Ib and thereby prevents ristocetin- and shear stress-induced platelet aggregation. To investigate its mechanism of action, ATA fractions of homogeneous M(r) have
The adherence of platelets to adsorbed albumin by receptor-mediated recognition of binding sites exposed by adsorption-induced unfolding.
Sivaraman B and Latour RA
Biomaterials, 31, 1036-1036 (2010)
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