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Key Documents

T8512

Sigma-Aldrich

Aktivierte Thiol–Sepharose™ 4B

lyophilized powder

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About This Item

MDL-Nummer:
MFCD00161935
UNSPSC-Code:
41106500

Form

lyophilized powder

Qualitätsniveau

200

Kennzeichnungsgrad

1 μmol per mL

Matrix

Sepharose 4B

Matrixaktivierung

cyanogen bromide

Aktive Matrixgruppe

glutathione 2-pyridyl disulfide

Matrixanbindung

N-terminal amino group

Matrix-Spacer

10 atoms (when ligands are coupled through the disulfide groups)

Quellen

1 g swells to 4-5 mL

Lagertemp.

2-8°C

Anwendung

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.

Physikalische Form

Lyophilisiertes Pulver stabilisiert mit Lactose und Dextran

Rechtliche Hinweise

Sepharose is a trademark of Cytiva

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)

Analysenzertifikate (COA)

Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.

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Cyanogenbromid-aktivierte Agarose lyophilized powder

Sigma-Aldrich

C9210

Cyanogenbromid-aktivierte Agarose

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
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
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
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
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