Octyl Separopore® 4B-CL

Applications:

Octyl-Separopore® 4B-CL is a hydrophobic chromatorgraphy matrix used to separate proteins on the basis of relative hydrophobicity. This is particularly useful for the purification from high ionic strength biological extracts since binding is performed in the presence of salt and the elution is carried out in the absence of salt.

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

References

References:

Biosynthesis and transcriptional analysis of thurincin H, a tandem repeated bacteriocin genetic locus, produced by Bacillus thuringiensis SF361. FEMS Microbiol Lett. (2009) 299: 205-13.
Two step purification of Acinetobacter sp. lipase and its evaluation as a detergent additive at low temperatures. Appl Biochem Biotechnol. (2008) 150: 139-56.
Purification and structural characterization of bacillomycin F produced by a bacterial honey isolate active against Byssochlamys fulva H25. J Appl Microbiol. (2008) 105: 663-73.
Screening and immobilization Burkholderia sp. GXU56 lipase for enantioselective resolution of (R,S)-methyl mandelate. Appl Biochem Biotechnol. (2008) 149: 79-88.
The surface physicochemistry and adhesiveness of Shewanella are affected by their surface polysaccharides. Microbiology. (2007) 153: 1872-83.
Isolation and characterisation of a novel bacteriocin produced by Bacillus thuringiensis strain B439. FEMS Microbiol Lett. (2003) 220: 127-31.
Purification and localization of a 10 kDa calcareous corpuscle binding protein of Spirometra mansoni plerocercoid. Parasitol Res. (2003) 89: 235-7.
Characterization of virus adsorption by using DEAE-sepharose and octyl-sepharose. Appl Environ Microbiol. (2002) 68: 3965-8.
Characterization of an extracellular medium-chain-length poly(3-hydroxyalkanoate) depolymerase from Pseudomonas alcaligenes LB19. Biomacromolecules. (2002) 3: 291-6.
Single-step method for purification of Shiga toxin-1 B subunit using receptor-mediated affinity chromatography by globotriaosylceramide-conjugated octyl sepharose CL-4B. Protein Expr Purif. (2001) 22: 267-75.
Purification and characterization of an extracellular lipase from Penicillium candidum. Lipids. (2001) 36: 283-9.
Overexpression and purification of the membrane-bound cytochrome P450 2B4. Protein Expr Purif. (2001) 21: 303-9.
Characterization of O-acetyl-L-serine sulfhydrylase purified from an alkaliphilic bacterium. Biosci Biotechnol Biochem. (2000) 64: 2352-9.
Partial purification and characterization of dolichol phosphate mannose synthase from Entamoeba histolytica. Glycobiology. (2000) 10: 1311-6.
Gel chromatographic characterization of the hydrophobic interaction of glycosylphosphatidylinositol-alkaline phosphatase with detergents. Biol Chem. (2000) 381: 161-72.
Purification and characterization of a monoacylglycerol lipase from the moderately thermophilic Bacillus sp. H-257. J Biochem. (2000) 127: 419-25.
Purification and characterization of D-glucosaminitol dehydrogenase from Agrobacterium radiobacter. Biosci Biotechnol Biochem. (1999) 63: 785-91.
Amphiphilic properties of acetylcholinesterase monomers in mouse plasma. Neurosci Lett. (1999) 265: 211-4.
Purification and characterization of adenosine diphosphate ribose pyrophosphatase from human erythrocytes. Int J Biochem Cell Biol. (1998) 30: 629-38.