추천 제품
양식
lyophilized powder
Quality Level
라벨링 범위
1 μmol per mL
Matrix
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)
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 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
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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