21-3280
Nonne-Apelt′s reagent
Synonyme(s) :
Ammonium sulfate solution
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About This Item
Forme:
liquid
Produits recommandés
Forme
liquid
Disponibilité
available only in Japan
Température de stockage
15-25°C
Chaîne SMILES
N.N.OS(O)(=O)=O
InChI
1S/2H3N.H2O4S/c;;1-5(2,3)4/h2*1H3;(H2,1,2,3,4)
Clé InChI
BFNBIHQBYMNNAN-UHFFFAOYSA-N
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Autres remarques
Aqueous ammonium sulfate solution equivalent to indicated ammonia levels
Code de la classe de stockage
12 - Non Combustible Liquids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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N A Nidialkova et al.
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
Stefan Tenzer et al.
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
Soo Chan Lee et al.
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
Urh Černigoj et al.
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
S Ishwarya et al.
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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