SP Sepharose™ is used in protein chromatography, ion exchange chromatography and cation exchange media. SP Sepharose™ has been used to study inhibitory proteins and peptides from the rhizomes of zingiberaceae plants as well as to study the subunit heterogeneity and molecular evolution of soybean basic 7S globulin. SP Sepharose™ has also assisted with advancing industrial applications of preparation of chitosan oligosaccharides.
Physical form
Suspension in 0.2 M sodium acetate and 20% ethanol
Journal of Alzheimer's disease : JAD, 21(2), 585-596 (2010-06-24)
Alzheimer's disease (AD) is a progressive neurodegenerative disorder where definite diagnosis can only be made postmortem, and for which the most promising peripheral markers of disease state and severity have been found in the cerebrospinal fluid. However, recent results suggest
Bioscience, biotechnology, and biochemistry, 74(8), 1631-1634 (2010-08-12)
Basic 7S globulin, a cysteine-rich protein from soybean seeds, consists of subunits containing 27 kD and 16 kD chains linked by disulfide bonding. Three differently sized subunits of the basic 7S globulin were detected and partially separated by SP Sepharose
Applied biochemistry and biotechnology, 166(8), 2037-2050 (2012-03-07)
Ammonium sulphate cut protein extracts, and their pepsin hydrolysates, from the rhizomes of 15 plants in the Zingiberaceae family were screened for their in vitro angiotensin I-converting enzyme inhibitory (ACEI) activity. The protein extract from Zingiber ottensii had the highest
The Journal of biological chemistry, 282(50), 36341-36353 (2007-10-18)
The central pathogenic event of prion disease is the conformational conversion of a host protein, PrPC, into a pathogenic isoform, PrPSc. We previously showed that the protein misfolding cyclic amplification (PMCA) technique can be used to form infectious prion molecules
Methods in molecular biology (Clifton, N.J.), 459, 117-130 (2008-06-26)
The infectious agents of prion diseases are unorthodox, and they seem to be composed primarily of a misfolded glycoprotein called the prion protein (PrP). Replication of prion infectivity is associated with the conversion of PrP from its normal, cellular form
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.