C7013
Coenzyme A–Agarose
Sinônimo(s):
coa-agarose
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About This Item
Produtos recomendados
forma
lyophilized powder
Extensão da rotulagem
2-6 μmol per mL gel
matriz
cross-linked 4% beaded agarose
ativação da matriz
cyanogen bromide
ligação da matriz
amino
espaçador de matriz
1 atom
inchaço
1 g swells to 5-10 mL
temperatura de armazenamento
−20°C
Aplicação
Coenzyme A-agarose is an agarose conjugate, in physical form stabilized with lactose and is used in affinity chromatography, protein chromatography and nucleotide/coenzyme resins. Coenzyme A has been used in studies assessing age-related hearing loss as well as to assess organisms that survive in environments subject to changing oxygen concentrations.
forma física
Stabilized with lactose
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Equipamento de proteção individual
Eyeshields, Gloves, type N95 (US)
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Biochemistry, 47(39), 10407-10419 (2008-09-06)
Serotonin N-acetyltransferase [arylalkylamine N-acetyltransferase (AANAT)] is a key circadian rhythm enzyme that drives the nocturnal production of melatonin in the pineal. Prior studies have suggested that its light and diurnal regulation involves phosphorylation on key AANAT Ser and Thr residues
Expression pattern of oxidative stress and antioxidant defense-related genes in the aging Fischer 344/NHsd rat cochlea.
Neurobiology of Aging (2012)
The Journal of biological chemistry, 287(13), 10494-10508 (2012-02-04)
We have studied for the first time the transcriptional regulatory circuit that controls the expression of the box genes encoding the aerobic hybrid pathway used to assimilate benzoate via coenzyme A (CoA) derivatives in bacteria. The promoters responsible for the
The Journal of biological chemistry, 282(15), 11446-11455 (2007-02-03)
GAT is an N-acetyltransferase from Bacillus licheniformis that was optimized by gene shuffling for acetylation of the broad spectrum herbicide, glyphosate, forming the basis of a novel mechanism of glyphosate tolerance in transgenic plants (Castle, L. A., Siehl, D. L.
Journal of lipid research, 36(5), 986-997 (1995-05-01)
To understand the possible role of phytanoyl-CoA ligase, present in the membrane, in the oxidation of phytanic acid in the matrix of peroxisomes (Pahan, K. and I. Singh. 1993. FEBS Lett. 333: 154-158) we examined the transport of phytanic acid/phytanoyl-CoA
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