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SEPHADEX G-75 SUPERFINE 100GM |
Sephadex G-75 Superfine Well-proven and widely used in industrial processes.Proven batch-to-batch reproducibility for more than 30 years. Wide selection of separation ranges.Hydrophilic backbone gives low non-specific interactions plus excellent recoverie
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SEPHADEX G-100 100GM |
SEPHADEX G-100 100GM
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SEPHADEX G-100 SUPERFINE 100GM |
SEPHADEX G-100 SUPERFINE 100GM
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CM-SEPHADEX C-25 500GM |
CM Sephadex C-25 High binding capacities for column or batch techniques Proven batch-to-batch reproducibility for more than 30 years Very high capacities even at elevated ionic strengths Hydrophilic backbone gives low non-specific binding and high recover
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CM-SEPHADEX C-50 500GM |
CM Sephadex C-50 500 g
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CNBR-ACTIVATED SEPHARS 4B 15GM |
CNBr-activated Sepharose 4B CNBr-activated Sepharose 4B is an established cyanogen bromide-activated medium used for more than twenty years and documented with many references.Multi-point attachment of protein ligands minimizes leakage of coupled ligand.E
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COLUMN PD-10 EMPTY PK50 |
COLUMN PD-10 EMPTY PK50 Economical and versatile columns for gravity flow applications.Empty PD-10 columns can be packed with a wide range of bulk media. Easy to use.Use PD-10 Columns with LabMate Buffer Reservoir for convenient equilibration sample appl
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CON-A SEPHAROSE 4B 100ML |
Con A Sepharose 4B Immobilized Concanavalin A is useful for isolating mannose- and glucose-containing glycoproteins.To select the optimum lectin for purification screen different lectin media e.g. Con A Sepharose 4B and Lentil Lectin Sepharose 4B.100 ml
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CON-A SEPHAROSE 4B 5ML |
Con A Sepharose 4B Immobilized Concanavalin A is useful for isolating mannose- and glucose-containing glycoproteins.To select the optimum lectin for purification screen different lectin media e.g. Con A Sepharose 4B and Lentil Lectin Sepharose 4B.5 ml
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LENTIL LECTIN-SEPHRO 4 B 25ML |
Lentil Lectin Sepharose 4B Lentil Lectin Sepharose 4B purifies glycoproteins including detergent-solubilized membrane glycoproteins and viral glycoproteinsRetains binding ability in the presence of detergentsTo select the optimum lectin for purification s
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