Separopore® 6B-CL

Applications

Separopore® 6B-CL is crosslinked high gel strength bioagarose matrix for gel filtration and coupling of affinity ligands. It is ideal for both analytical and preparative protein purifications. Separopore® 6B-CL is a proven base matrix for coupling affinity ligands. Separopore® 6B-CL provides good separation over a wide molecular weight range. Larger volumes available at discounted prices (enquire).

Note: Separopore® is a cost-effective equivalent to Sepharose® in all of its physical properties and binding characteristics.

References

References:
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Quantitative assessment of comparative potencies of cholesterol-crystal-promoting factors: relation to mechanistic characterization. Biochem J. (1998) 332: 343-50.
Fermentation Enzymes in Strictly Aerobic Bacteria: Comparative Studies on Strains of the Genus Alcaligenes and on Nocardia opaca and Xanthobacter autotrophicus. Microbiology, (1983) 129: 2825-2835.
Immobilization of trypsin on chitosan gels: use of different activation protocols and comparison with other supports. Int J Biol Macromol. (2008) 43: 54-61.
Elevated serum levels in human pregnancy of a molecule immunochemically similar to eosinophil granule major basic protein. J Exp Med. (1983) 158: 1211-26.
Penicillin G acylase catalyzed acylation of 7-ACA in aqueous two-phase systems using kinetically and thermodynamically controlled strategies: improved enzymatic synthesis of 7-[(1-hydroxy-1-phenyl)-acetamido]-3-acetoxymethyl-Δ3-cephem-4-carboxylic acid. Enzyme and Microbial Technology, (2005) 36: 672-679.
Immobilization of the acylase from Escherichia coli on glyoxyl-agarose gives efficient catalyst for the synthesis of cephalosporins. Enzyme and Microbial Technology,(2008) 42: 121-129.