A2419
ω-Aminohexyl–Sepharose™ 4B
aqueous ethanol suspension
Synonyme(s) :
ψ-Aminohexyl Resin, Aminohexyl Sepharose
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About This Item
Produits recommandés
Forme
aqueous ethanol suspension
Niveau de qualité
Technique(s)
affinity chromatography: suitable
Activation de la matrice
epoxy
Fixation de matrice
amino
Espaceur de matrice
11 atoms
Température de stockage
2-8°C
Application
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.
Forme physique
Suspension in 20% ethanol.
Informations légales
Sepharose is a trademark of Cytiva
Mention d'avertissement
Warning
Mentions de danger
Conseils de prudence
Classification des risques
Flam. Liq. 3
Code de la classe de stockage
3 - Flammable liquids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
95.0 °F
Point d'éclair (°C)
35 °C
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The Journal of biological chemistry, 274(18), 12508-12516 (1999-04-23)
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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
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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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