Butyl Sepharose 4B
Butyl Sepharose 4B structure
|
Common Name | Butyl Sepharose 4B | ||
|---|---|---|---|---|
| CAS Number | 157885-28-4 | Molecular Weight | N/A | |
| Density | N/A | Boiling Point | 78 °C | |
| Molecular Formula | N/A | Melting Point | N/A | |
| MSDS | USA | Flash Point | 38 - 43℃ | |
| Symbol |
GHS02, GHS07 |
Signal Word | Warning | |
|
Isolation of soybean protein P34 from oil bodies using hydrophobic interaction chromatography.
BMC Biotechnol. 8 , 27, (2008) Soybeans play a prominent role in allergologic research due to the high incidence of allergic reactions. For detailed studies on specific proteins it is necessary to have access to a large amount of pure substance.In this contribution, a method for purifying ... |
|
|
High-throughput protein precipitation and hydrophobic interaction chromatography: salt effects and thermodynamic interrelation.
J. Chromatogr. A. 1218 , 8958-8973, (2011) Salt-induced protein precipitation and hydrophobic interaction chromatography (HIC) are two widely used methods for protein purification. In this study, salt effects in protein precipitation and HIC were investigated for a broad combination of proteins, salts... |
|
|
Chemical and chromatographic characterization of a new bioprocess™ medium for hydrophobic interaction chromatogrpahy: Butyl Sepharose® 4 FastFlow. Berggrund, A., et al.
Process. Biochem. 29(6) , 455-463, (1994)
|
|
|
Investigation of protein retention in hydrophobic interaction chromatographic (HIC) systems using the preferential interaction theory and quantitative structure property relationship models. Chen, J., et al.
Reactive funct. Polym. 67(12) , 1561-1569, (2007)
|
|
|
Hydrophobic interaction chromatography selectivity changes among three stable proteins: conformation does not play a major role.
Biotechnol. Bioeng. 87(3) , 388-399, (2004) Interesting retention and selectivity changes have been noted for a number of proteins in hydrophobic interaction chromatography (HIC). In this study, we investigated the degree to which conformational changes may be responsible for selectivity changes of sta... |
|
|
Enolase activates homotypic vacuole fusion and protein transport to the vacuole in yeast.
J. Biol. Chem. 281(20) , 14523-14528, (2006) Membrane fusion and protein trafficking to the vacuole are complex processes involving many proteins and lipids. Cytosol from Saccharomyces cerevisiae contains a high Mr activity, which stimulates the in vitro homotypic fusion of isolated yeast vacuoles. Here... |
|
|
Kinetics of Angiotensin I alteration of conformation on different hydrophobic interaction chromatographic surfaces.
J. Chromatogr. A. 1218 , 8322-8332, (2011) In the present study, Angiotensin I (Ang I) will be used as model peptide to assess on-column alteration of conformation phenomena. Adsorptive behavior of Ang I on various commercial hydrophobic interaction surfaces (Butyl, Octyl and Phenyl - Sepharose), unde... |
|
|
High level expression, purification and activation of human dipeptidyl peptidase I from mammalian cells.
Protein Expr. Purif. 76 , 59-64, (2011) Dipeptidyl peptidase I (DPPI) plays a crucial role in maturation of many regulatory peptides and has been suggested as a pharmaceutical target in several inflammatory diseases. It is also a useful processing enzyme for the generation of authentic protein prod... |