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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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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
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 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
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
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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