推荐产品
表单
lyophilized powder
标记范围
18-31 μmol per mL
基质活性基团
hydroxypropyl 2-pyridyl disulfide
溶胀
1 g swells to 4-5 mL gel
储存温度
2-8°C
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应用
Thiopropyl Sepharose™ 6B is used in protein chromatography, affinity chromatography and hydrophobic interactions. Thiopropyl Sepharose™ 6B has been used for the removal of inhibitors from PCR extracts from evidence collected for law enforcement murder investigations. Thiopropyl Sepharose™ 6B has also been used to describe a method for the investigation of functional properties of distinct domains of viral thiol proteins, including the influenza virus membrane M1 protein.
外形
Lyophilized powder stabilized with lactose and dextran
法律信息
Sepharose is a trademark of Cytiva
储存分类代码
13 - Non Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
Z Glatz et al.
Journal of chromatography. B, Biomedical sciences and applications, 688(2), 239-243 (1997-01-24)
Thiopropyl Sepharose 6B in the 2-thiopyridyl-activated form was used for the reversible immobilisation of reduced glutathione (GSH). The resulting affinity matrix was successfully tested as a sorbent for the partial purification of glutathione S-transferase (GST) from pig kidney. The specific
I Tabuchi et al.
FEBS letters, 508(3), 309-312 (2001-12-01)
In vitro virus is a molecular construct for in vitro protein evolution, which requires some mechanism to link phenotype to genotype. The first in vitro virus was realized by bonding a nascent protein with its coding mRNA via puromycin in
Covalent chromatography of influenza virus membrane M1 protein on activated thiopropyl Sepharose-6B.
N V Fedorova et al.
Journal of chromatography. B, Biomedical sciences and applications, 706(1), 83-89 (1998-04-17)
The M1 protein of influenza virus is a highly hydrophobic polypeptide that is resistant to enzyme cleavage during incubation in water solutions. We show here that the M1 protein that is immobilized on an insoluble activated support (thiopropyl Sepharose-6B) by
G Williamson et al.
Biochimica et biophysica acta, 706(2), 245-248 (1982-09-07)
The commercially available gel, 2-pyridyl disulphide hydroxypropyl ether-Sepharose (thiopropyl-Sepharose 6B), can be used to remove bound ligand completely from butyryl-CoA dehydrogenase (EC 1.399.2) in two simple operations. The resultant enzyme forms normal complexes with acetoacetyl-CoA and CoA persulphide, contains no
F Desarnaud et al.
Journal of chromatography, 603(1-2), 95-104 (1992-06-19)
The major problem usually encountered in the application of the (strept)avidin-biotin system to the purification of proteins (or other biological molecules) lies in the difficult reversion of the interaction between immobilized (strept)avidin and the adsorbed biotinylated protein. Among the proposed
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