20152
Chromosorb® W
HP, 60-80 mesh particle size, bottle of 100 g
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About This Item
CAS Number:
EC Number:
MDL number:
UNSPSC Code:
23151817
PubChem Substance ID:
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Quality Level
packaging
bottle of 100 g
technique(s)
gas chromatography (GC): suitable
surface area
0.6-1.3 m2/g
particle size
60-80 mesh
density
0.23 g/mL at 25 °C
0.18 g/cm3 (loose weight)(lit.)
SMILES string
O=[Si]=O
InChI
1S/O2Si/c1-3-2
InChI key
VYPSYNLAJGMNEJ-UHFFFAOYSA-N
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Chromosorb is a registered trademark of Imerys Minerals California, Inc.
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Myroslav Sprynskyy et al.
Journal of hazardous materials, 181(1-3), 700-707 (2010-06-15)
In this work the natural and the surfactant modified diatomite has been tested for ability to remove uranium ions from aqueous solutions. Such controlling factors of the adsorption process as initial uranium concentration, pH, contact time and ionic strength have
Guodong Sheng et al.
Environmental science & technology, 45(18), 7718-7726 (2011-08-23)
Sequestration of Ni(II) on diatomite as a function of time, pH, and temperature was investigated by batch, XPS, and EXAFS techniques. The ionic strength-dependent sorption at pH < 7.0 was consistent with outer-sphere surface complexation, while the ionic strength-independent sorption
Guodong Sheng et al.
Journal of environmental radioactivity, 113, 108-115 (2012-06-09)
Clay minerals have been extensively studied because of their strong sorption and complexation ability. In this work, diatomite was characterized by using acid-base titration. Retention of radionuclide (60)Co(II) from aqueous solution by sorption onto diatomite was investigated by using batch
Junhua Li et al.
Applied microbiology and biotechnology, 97(6), 2541-2549 (2012-08-29)
The ribosomal protein L2, a constituent protein of the 50S large ribosomal subunit, can be used as Si-tag using silica particles for the immobilization and purification of recombinant proteins (Ikeda et al. (Protein Expr Purif 71:91-95, 2010); Taniguchi et al.
Junhua Li et al.
Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 917-918, 30-35 (2013-01-29)
A basic polypeptide L2 (252-273) derived from Escherichia coli ribosomal protein L2 was used as a purification tag. In order to develop faster, less expensive methods for expression and purification of proteins, the L2 (252-273)-small ubiquitin like modifier (SUMO) fusion
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