N4517
N-Z-Amine® AS
Casein enzymatic hydrolysate, suitable for microbiology
Synonym(s):
Peptone from casein
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About This Item
Recommended Products
biological source
bovine milk
Quality Level
form
powder
packaging
pkg of 1 kg
nitrogen analysis
≥6% amino, ≥11% total
color
yellow
pH
5.8-7.8
application(s)
microbiology
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General description
N-Z-Amine® AS is an enzyme digest of casein prepared from Bovine milk, processed to a high degree of hydrolysis. It is a refined hydrolysate with high solubility and is used as a microbiological nutrient in laboratory media and fermentations. It is a high-quality source of amino acids, vitamins, peptides, and growth promoting substances, produced by the enzymatic digestion of casein.
Application
N-Z-Amine® AS is used as a nutrient for laboratory and fermentation media and in the production of antibiotics and enzymes.
Linkage
A form of N-Z-Amine A with much greater solubility. Concentrated solutions are clear, but contain some filterable solids.
Reconstitution
Recommended concentration: 210 g/L
Legal Information
N-Z-Amine is a registered trademark of Kerry Group
N-Z-Case is a registered trademark of Kerry Group
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Andrew R Ednie et al.
The Journal of biological chemistry, 290(5), 2769-2783 (2014-12-20)
Voltage-gated K(+) channels (Kv) are responsible for repolarizing excitable cells and can be heavily glycosylated. Cardiac Kv activity is indispensable where even minimal reductions in function can extend action potential duration, prolong QT intervals, and ultimately contribute to life-threatening arrhythmias.
P Askerlund et al.
Plant physiology, 100(4), 1670-1681 (1992-12-01)
Purification and functional reconstitution of a calmodulin-stimulated Ca(2+)-ATPase from cauliflower (Brassica oleracea L.) is described. Activity was purified about 120-fold from a microsomal fraction using calmodulin-affinity chromatography. The purified fraction showed a polypeptide at 115 kD, which formed a phosphorylated
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