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About This Item
NACRES:
SB.52
UNSPSC Code:
23151817
form
liquid
packaging
bottle of 100 g
technique(s)
LPLC: suitable
surface area
~500 m2/g
matrix
styrene-divinylbenzene
matrix active group
polymer
particle size
50-100 μm
pore size
~1.01 mL/g pore volume, 260 Å mean pore size
density
1.30 g/mL at 25 °C (true wet)(lit.)
separation technique
reversed phase
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Application
Polyaromatic adsorbent resin for separation of hydrophobic compounds: small and medium proteins, peptides, amino acids. Excellent for reversed phase applications.
Sepabeads form a polyaromatic adsorbent resin for separation of hydrophobic compounds including small and medium proteins, peptides and amino acids. Sepabeads are excellent for reversed phase applications.
Other Notes
Swelling in toluene = 30%
Legal Information
Sepabeads is a registered trademark of Mitsubishi Chemical Corp.
Storage Class
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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One-step enzymatic synthesis of nucleosides from low water-soluble purine bases in non-conventional media
Fernandez-Lucas, J., et al.
Bioresource Technology (2012)
Karel Hernandez et al.
Enzyme and microbial technology, 49(1), 72-78 (2011-11-25)
Two commercial porous styrene-divinylbenzene beads (Diaion HP20LX and MCI GEL CHP20P) have been evaluated as supports to immobilize lipase B from Candida antarctica (CALB). MCI GEL CHP20P rapidly immobilized the enzyme, permitting a very high loading capacity: around 110mgCALB/wetg of
Karel Hernandez et al.
Enzyme and microbial technology, 48(6-7), 510-517 (2011-11-25)
The effect of the immobilization protocol and some experimental conditions (pH value and presence of acetonitrile) on the regioselective hydrolysis of triacetin to diacetin catalyzed by lipases has been studied. Lipase B from Candida antarctica (CALB) and lipase from Rhizomucor
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