21-3280
Nonne-Apelt′s reagent
Synonym(s):
Ammonium sulfate solution
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About This Item
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form
liquid
availability
available only in Japan
storage temp.
15-25°C
SMILES string
N.N.OS(O)(=O)=O
InChI
1S/2H3N.H2O4S/c;;1-5(2,3)4/h2*1H3;(H2,1,2,3,4)
InChI key
BFNBIHQBYMNNAN-UHFFFAOYSA-N
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Other Notes
Aqueous ammonium sulfate solution equivalent to indicated ammonia levels
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Methods in molecular biology (Clifton, N.J.), 960, 1-14 (2013-01-19)
Proteasomes are the main cytosolic proteases responsible for generating peptides for antigen processing and presentation in the MHC (major histocompatibility complex) class-I pathway. Purified 20S and 26S proteasomes have been widely used to study both specificity and efficiency of antigen
Mikrobiolohichnyi zhurnal (Kiev, Ukraine : 1993), 74(5), 9-15 (2012-11-06)
Fibrinolytic peptidase of Bacillus thuringiensis IMV B-7324 was isolated by ammonium sulfate fractionation, gel-filtration and ion exchange chromatography on TSK-gels--Toyopearl HW-55 and DEAE 650 (M). Fibrinolytic activity of the purified enzyme was 87.9 U/mg of protein that was 19.9 times
Eukaryotic cell, 11(11), 1391-1398 (2012-09-25)
Cryptococcus neoformans is a human-pathogenic basidiomycete that commonly infects HIV/AIDS patients to cause meningoencephalitis (7, 19). C. neoformans grows as a budding yeast during vegetative growth or as hyphae during sexual reproduction. Pseudohyphal growth of C. neoformans has been observed
Journal of chromatography. A, 1281, 87-93 (2013-02-13)
To exploit different chromatographic modes for efficient plasmid DNA (pDNA) purification a novel monolithic chromatographic support bearing multimodal histamine (HISA) groups was developed and characterized. Electrostatic charge of HISA groups depends on the pH of the mobile phase, being neutral
Preparative biochemistry & biotechnology, 43(1), 95-107 (2012-12-12)
A serine protease was purified 6.9-fold from the leaves of Thespesia populnea using ammonium sulfate fractionation followed by CM-cellulose and Sephadex G-100 chromatography. The purified enzyme was named populnein and was characterized. It was made up of a single polypeptide
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