Brown Separopore® 4B-CL

Applications:

Brown-Separopore® 4B-CL is a dye-ligand affinity matrix consisting of Reactive Brown 10 bound to cross-linked 4% agarose beads. It is used to purify proteins that have distinctive affinity to this dye. Immobilized dyes have been found to bind from 5 to 60 % of the proteins in various crude cell extracts. The affinity for reactive dyes 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 dye resins.

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

References

Purification and characterization of CMP-N-acetylneuraminic acid hydroxylase from pig submandibular glands. Glycobiology. (1994) 4: 675-83.
Purification and characterization of the nuclear cytidine 5\'-monophosphate N-acetylneuraminic acid synthetase from rat liver. J Biol Chem. (1992) 267: 9257-63.
Characterization of sialidase from Entamoaeba hystolitica and possible pathogenic role in amebiasis. Parasitol Res. (2003) 89: 302-7.
Characterisation and immunolocation of an 87 kDa polypeptide associated with UDP-glucuronic acid decarboxylase activity from differentiating tobacco cells (Nicotiana tabacum L.). Phytochemistry. (2002) 61: 771-80.
A 45-kDa midgut glycoprotein from Anopheles albimanus mosquito mediates the killing of trypanosomes. Cell Biochem Funct. (2002) 20: 257-62.
Degradation of aromatics and chloroaromatics by Pseudomonas sp. strain B13: purification and characterization of 3-oxoadipate:succinyl-coenzyme A (CoA) transferase and 3-oxoadipyl-CoA thiolase. J Bacteriol. (2002) 184: 207-15