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form
lyophilized powder
Quality Level
extent of labeling
2-6 μmol per mL gel
matrix
cross-linked 4% beaded agarose
matrix activation
cyanogen bromide
matrix attachment
amino
matrix spacer
1 atom
swelling
1 g swells to 5-10 mL
storage temp.
−20°C
Application
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.
Physical form
Stabilized with lactose
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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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
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
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
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.
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