Orange Separopore® 4B-CL

Applications

Orange-Separopore® 4B-CL is useful for the isolation of nucleotide enzymes, complement factors, human serum albumin. Immobilized orange dye binds from 5 to 60% of the proteins in various crude cell extracts. The affinity for reactive orange dye to proteins may be due to substrate/cofactor similarities as well as hydrophobic and ion exchange properties. Some proteins have been found to require the addition of divalent cations for binding to orange dye resin.

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

References

References:

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Bovine UDP-N-acetylglucosamine:lysosomal-enzyme N-acetylglucosamine-1-phosphotransferase. I. Purification and subunit structure. J Biol Chem. (1996) 271: 31437-45.
Purification and characterization of threonine dehydrogenase from Clostridium sticklandii. Arch Microbiol. (1995) 163: 286-90.
UDP-rhamnose:flavanone-7-O-glucoside-2\'\'-O-rhamnosyltransferase. Purification and characterization of an enzyme catalyzing the production of bitter compounds in citrus. J Biol Chem. (1991) 266: 20953-9.
Fetuin and alpha-2HS glycoprotein induce alkaline phosphatase in epiphyseal growth plate chondrocytes. J Cell Physiol. (1991) 149: 222-34.
The affinity purification and characterization of a dehydrogenase from Aspergillus parasiticus involved in aflatoxin B1 biosynthesis. Prep Biochem. (1991) 21: 125-40.
Evaluation of assays for detecting alpha-1-protease inhibitor during purification from rat serum. Anal Biochem. (1991) 193: 260-5.