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T8512

Sigma-Aldrich

Activated Thiol–Sepharose 4B

lyophilized powder

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MDL number:

form

lyophilized powder

Quality Level

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

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This Item
C91424B200GE17-0569-01
Activated Thiol–Sepharose™ 4B lyophilized powder

T8512

Activated Thiol–Sepharose 4B

Sepharose™ 4B 45-165 μm bead diameter

4B200

Sepharose 4B

EAH-Sepharose™ 4B Cytiva 17-0569-01, pack of 50 mL

GE17-0569-01

EAH-Sepharose 4B

matrix

Sepharose 4B

matrix

Sepharose 4B

matrix

-

matrix

4% agarose

form

lyophilized powder

form

lyophilized powder

form

suspension

form

-

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

-

extent of labeling

1 μmol per mL

extent of labeling

-

extent of labeling

-

extent of labeling

-

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_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Customers Also Viewed

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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
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
N Agell et al.
The Biochemical journal, 273 ( Pt 3), 615-620 (1991-02-01)
A ubiquitin hydrolase that removes ubiquitin from a multi-ubiquitinated protein has been purified 600-fold from Saccharomyces cerevisiae. Four different ubiquitin-protein conjugates were assayed as substrates during the purification procedure. Enzymic activities that removed ubiquitin from ubiquitinated histone H2A, a ubiquitin-ubiquitin
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

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