Separopore® 6B

Applications:

Separopore®6B is a 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 is a proven base matrix for coupling affinity ligands. Separopore®6B 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:
The covalent binding of daunomycin and adriamycin to antibodies, with retention of both drug and antibody activities. Cancer Res. (1975) 35: 1175-81.
Purification and properties of filamin, and actin binding protein from chicken gizzard. J Biol Chem. (1976) 251: 6562-7.
Surface topography of histidine residues: a facile probe by immobilized metal ion affinity chromatography. Proc Natl Acad Sci U S A. (1989) 86: 1811-5.
Purification and properties of an 8-hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum. J Biol Chem. (1982) 257: 3385-8.
Purification and characterization of placental heparanase and its expression by cultured cytotrophoblasts. Mol Hum Reprod. (1996) 2: 679-84.
Ferritin and superoxide-dependent lipid peroxidation. J Biol Chem. (1985) 260: 3275-80.
Multiple forms of uridine kinase in normal and neoplastic rat liver. Biochem J. (1971) 124: 943-7.
The calcium release channel of sarcoplasmic reticulum is modulated by FK-506-binding protein. Dissociation and reconstitution of FKBP-12 to the calcium release channel of skeletal muscle sarcoplasmic reticulum. J Biol Chem. (1993) 268: 22992-9.
Purification of the tetrodotoxin-binding component associated with the voltage-sensitive sodium channel from Electrophorus electricus electroplax membranes. Proc Natl Acad Sci U S A. (1978) 75: 2606-10.