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N4517

Millipore

Casein Peptone

Enzymatic digest of casein from bovine milk, suitable for biotechnology and microbiology

Synonym(s):

Peptone from casein, N-Z-Case® AS

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About This Item

CAS Number:
EC Number:
UNSPSC Code:
41106212
NACRES:
NA.85

product name

N-Z-Amine® AS, Casein enzymatic hydrolysate, suitable for microbiology

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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