T8512
Activated Thiol–Sepharose™ 4B
lyophilized powder
form
lyophilized powder
extent of labeling
1 μmol per mL
matrix
Sepharose 4B
matrix activation
cyanogen bromide
matrix active group
glutathione 2-pyridyl disulfide
matrix attachment
N-terminal amino group
matrix spacer
10 atoms (when ligands are coupled through the disulfide groups)
swelling
1 g swells to 4-5 mL
storage temp.
2-8°C
Quality Level
Application
Activated thiol Sepharose™ 4B is used in protein chromatography, affinity chromatography and activated/functionalized matrices. Activated thiol Sepharose™ 4B has been used to provide the first report of the isolation of aminopeptidase H from a reptile. Activated thiol Sepharose™ 4B has also been used to purify and characterize a neuropeptide-inactivating peptidase.
Physical form
Lyophilized powder stabilized with lactose and dextran
Legal Information
Sepharose is a trademark of Cytiva
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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G Oshima et al.
Biological & pharmaceutical bulletin, 23(5), 532-536 (2000-05-24)
Glutathione peroxidase (GPx) activity was detected in the ascite fluid of rats injected intraperitoneally with 2.5% heat-denatured casein solution. Activity in the ascite fluid increased with time after the injection of casein, and reached a maximum at 24 h. The
S Al-Jassabi
Biochemistry. Biokhimiia, 64(2), 217-222 (1999-04-03)
Aminopeptidase H was isolated and purified from fresh skeletal muscle of the lizard Agama stellio stellio by ammonium sulfate fractionation and successive chromatographies on DEAE-cellulose, Ultrogel AcA-34, activated thiol-Sepharose 4B, phenyl-Sepharose CL-4B, and DEAE-cellulose again. This is the first report
N Iwatsuki et al.
Biochemistry, 19(6), 1172-1176 (1980-03-18)
DNA photolyase purified from baker's yeast by affinity chromatography on UV-irradiated DNA noncovalently bound to cellulose and by chromatography on activated thiol-Sepharose 4B yields a single protein band having a molecular weight of 51 000 when analyzed by sodium dodecyl
Abdullah Ozer et al.
Nucleic acids research, 41(14), 7167-7175 (2013-06-06)
The non-specific binding of undesired ligands to a target is the primary factor limiting the enrichment of tight-binding ligands in affinity selection. Solution-phase non-specific affinity is determined by the free-energy of ligand binding to a single target. However, the solid-phase
H A Khalfan
Cell biochemistry and function, 9(1), 55-62 (1991-01-01)
The protease activity of cultured normal human skin fibroblasts was studied using the synthetic fluorigenic peptides, the modified protein 4-methylumbelliferyl-casein, the thiol inhibitors and the affinity for concanavalin A-Sepharose. The majority of the activity to N-benzyloxycarbonyl-L-phenylalanyl-L-arginyl-7-amido-4-methyl-coumarin and N-a-benzyloxycarbonyl-L-arginyl-arginyl-7-amido-4-methylcoumarin had a
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