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表单
aqueous ethanol suspension
质量水平
技术
affinity chromatography: suitable
基质活化
epoxy
基质附着
amino
基质隔离区
11 atoms
储存温度
2-8°C
SMILES字符串
[X]NCCCCCCN
应用
ω-Aminohexyl– Sepharose™ 4B is used mainly in affinity chromatography. It has been used in mitochondrial research to purify thioredoxin reductase (TrxR2), which is important in cell signaling and may also be an anticancer drug target.
外形
Suspension in 20% ethanol.
法律信息
Sepharose is a trademark of Cytiva
警示用语：
Warning
危险声明
危险分类
Flam. Liq. 3
储存分类代码
3 - Flammable liquids
WGK
WGK 1
闪点(°F)
95.0 °F
闪点(°C)
35 °C
法规信息
危险化学品
F Pfennig et al.
The Journal of biological chemistry, 274(18), 12508-12516 (1999-04-23)
Actinomycin synthetase I (ACMS I) activates 4-methyl-3-hydroxyanthranilic acid, the precursor of the chromophoric moiety of the actinomycin, as adenylate. The gene acmA of ACMS I was identified upstream of the genes acmB and acmC encoding the two peptide synthetases ACMS
J D Hayes et al.
The Biochemical journal, 207(3), 459-470 (1982-12-01)
Rat liver glutathione S-transferases have previously been defined by their elution behaviour from DEAE-cellulose and CM-cellulose as M, E, D, C, B, A and AA. These enzymes are dimeric proteins which comprise subunits of mol.wt. 22 000 (Ya), 23 500
R Swanson et al.
The Journal of biological chemistry, 260(2), 1287-1289 (1985-01-25)
Bacterial luciferase from Vibrio harveyi, the 77,000-dalton light-emitting enzyme of the marine bacterium, has been crystallized into a two million cubic Angstrom cell with P212121 symmetry. The cell constants are a = 59.6 +/- 0.4 A, b = 112 +/-
Maria Pia Rigobello et al.
Methods in enzymology, 474, 109-122 (2010-07-09)
Mitochondrial thioredoxin reductase (TrxR2) maintains thioredoxin (Trx2) in a reduced state and plays a critical role in mitochondrial and cellular functions. TrxR2 has been identified in many different tissues and can be purified to homogeneity from whole organs and isolated
M Burgos-Trinidad et al.
The Journal of biological chemistry, 267(5), 3498-3505 (1992-02-15)
The chick kidney mitochondrial cytochrome P-450 1,25-dihydroxyvitamin D3 24-hydroxylase was partially purified by sequential polyethylene glycol precipitation, aminohexyl-Sepharose 4B, and hydroxylapatite chromatography. The specific activity of the final preparation, when reconstituted with NADPH, adrenodoxin, and adrenodoxin reductase, was 245 pmol/min/mg
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