Phenyl Sepharose™ is used in protein chromatography, affinity chromatography, hydrophobic interaction media, resins and separation media. Phenyl Sepharose™ has been used in studies that contributed to improving industrial applications in additives in detergents and feed industries. Phenyl Sepharose™ has also been used to study microbial communities inhabiting hypersaline environments.
Journal of biotechnology, 83(3), 177-187 (2000-10-29)
Cellulases produced by two Bacillus strains, CH43 and HR68, isolated from hot springs in Zimbabwe, were purified to homogeneity from culture supernatants. Both enzymes had molecular mass of 40 kDa and isoelectric point of 5.4. The enzymes also resembled each
Development of a downstream process for the isolation of <I>Staphylococcus aureus</I> arsenate reductase overproduced in <I>Escherichia coli</I>.
Messens, J., et al.
Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences, 737, 167-178 (2000)
The Biochemical journal, 363(Pt 2), 377-386 (2002-04-05)
The faeB gene encoding a second feruloyl esterase from Aspergillus niger has been cloned and characterized. It consists of an open reading frame of 1644 bp containing one intron. The gene encodes a protein of 521 amino acids that has
The Journal of biological chemistry, 271(8), 4243-4250 (1996-02-23)
The effect of sphingomyelin (SPM) on the structure and function of discoidal and spherical reconstituted high density lipoproteins (rHDL) has been studied. Three preparations of discoidal rHDL with 1-palmitoyl-2-oleoyl phosphatidylcholine (POPC)/SPM/unesterified cholesterol (UC)/apolipoprotein (apo)A-I molar ratios of 99.6/0. 0/10.2/1.0, 86.0/13.6/10.8/1.0
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.