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.
Application
Sepharose™ 2B has been used for the preparation of virosomes and platelets.[1][2][3]
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
Biochimica et biophysica acta, 970(1), 61-67 (1988-06-08)
Experiments were performed to elucidate the role of adenosine 3': 5'-cyclic monophosphate (cAMP) in the control of platelet protein kinase C (PKC) activation. Platelet aggregation and secretion in response to 4 beta-phorbol 12-myristate 13-acetate (PMA) or 1-oleoyl-2-acetylglycerol (OAG) were inhibited
A low molecular weight (LMW) protein phosphokinase enzyme that binds to actin has been isolated from murine sarcoma virions; this kinase activity is not present in nontransforming murine leukemia viruses. Sephadex G-75 gel filtration and affinity chromatography on actin-Sepharose conjugates
Depletion of glycoprotein gp85 from virosomes made with Epstein-Barr virus proteins abolishes their ability to fuse with virus receptor-bearing cells.
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
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