T8387
Thiopropyl–Sepharose™ 6B
lyophilized powder
Synonym(s):
Thiopropyl−activated–Agarose
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About This Item
Recommended Products
form
lyophilized powder
extent of labeling
18-31 μmol per mL
matrix active group
hydroxypropyl 2-pyridyl disulfide
swelling
1 g swells to 4-5 mL gel
storage temp.
2-8°C
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Application
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.
Physical form
Lyophilized powder stabilized with lactose and dextran
Legal Information
Sepharose is a trademark of Cytiva
Storage Class Code
13 - Non Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Michael T Forrester et al.
Journal of lipid research, 52(2), 393-398 (2010-11-04)
Protein S-acylation is a major posttranslational modification whereby a cysteine thiol is converted to a thioester. A prototype is S-palmitoylation (fatty acylation), in which a protein undergoes acylation with a hydrophobic 16 carbon lipid chain. Although this modification is a
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
Markandeswar Panda et al.
Journal of chromatography. A, 1202(1), 75-82 (2008-07-08)
Green fluorescent protein (GFP) fused to the C-terminal 100 amino acids of CAAT enhancer binding protein (C/EBP) also containing an N-terminal (His)(6) tag (GFP-C/EBP) was used as a transcription factor model to test whether thiol-disulfide exchange reactions could be used
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
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