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T8512

Sigma-Aldrich

Activated Thiol–Sepharose 4B

lyophilized powder

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About This Item

MDL number:
UNSPSC Code:
41106500
NACRES:
NA.56

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

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 Code

11 - 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

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
G Oshima et al.
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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
B J Blacklock et al.
The Journal of biological chemistry, 267(20), 14033-14037 (1992-07-15)
The mechanism of facilitated lipid transfer by insect or mammalian plasma lipid transfer proteins has not been elucidated. Transfer catalysts may act as carriers of lipid between donor and acceptor lipoproteins or, alternatively, transfer may require formation of a ternary
P M Cummins et al.
The international journal of biochemistry & cell biology, 28(8), 883-893 (1996-08-01)
Pyroglutamyl aminopeptidase type-1 (PAP-I) is reported to be a soluble, broad specificity aminopeptidase, capable of removing the pyroglutamic acid (pGlu) residue from the amino terminus of pGlu-peptides (e.g. TRH, LHRH, neurotensin and bombesin). The central aim of this study was

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