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Merck
모든 사진(3)

주요 문서

T8512

Sigma-Aldrich

Activated Thiol–Sepharose 4B

lyophilized powder

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About This Item

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

형태

lyophilized powder

Quality Level

라벨링 범위

1 μmol per mL

기질

Sepharose 4B

기질 활성

cyanogen bromide

기질 활성군

glutathione 2-pyridyl disulfide

기질 부착

N-terminal amino group

기질 스페이서

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

팽창

1 g swells to 4-5 mL

저장 온도

2-8°C

애플리케이션

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.

물리적 형태

Lyophilized powder stabilized with lactose and dextran

법적 정보

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

개인 보호 장비

Eyeshields, Gloves, type N95 (US)


시험 성적서(COA)

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문서 라이브러리 방문

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
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
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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