C0626
N-Z-Amine® A Casein Peptone
Enzymatically Digested, for Biotechnology and Microbiology
Sinónimos:
Peptone from casein, N-Z-Case® A
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Servicio técnico
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Permítanos ayudarlebiological source
bovine milk
form
powder
packaging
poly bottle of 250, 500 g, poly bottle of 1 kg, poly drum of 5 kg
nitrogen analysis
≥6% amino, ≥11.0% total
loss
≤11% loss on drying
pH
5.8-7.8
application(s)
food and beverages
microbiology
Quality Level
Categorías relacionadas
General description
N-Z-Amine® A is an enzyme digest of casein 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® has been used:
- to homogenize leaves for the isolation of plasma membranes
- as a supplement in Murashige and Skoog (MS) medium for optimization of alfalfa regeneration system
- to prepare MOPS low phosphate minimal medium and M9 minimal medium
Preparation Note
Recommended concentration: 25 g/L
Legal Information
N-Z-Amine is a registered trademark of Kerry Group
N-Z-Case is a registered trademark of Kerry Group
Clase de almacenamiento
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Fusicoccin activates the plasma membrane H+-ATPase by a mechanism involving the C-terminal inhibitory domain
Johansson F, et al.
Plant Cell, 5(3), 321- 327 (1993)
Development of alfalfa (Medicago sativa L.) regeneration system and Agrobacterium-mediated genetic transformation
Zhang H, et al.
Agricultural sciences in China, 9(2), 170-178 (2010)
Batu K Sharma-Kuinkel et al.
Journal of bacteriology, 191(15), 4767-4775 (2009-06-09)
Studies of the Staphylococcus aureus LytSR two-component regulatory system have led to the identification of the cid and lrg operons, which affect murein hydrolase activity, stationary-phase survival, antibiotic tolerance, and biofilm formation. The cid gene products enhance murein hydrolase activity
Laboratory evolution of Escherichia coli thioredoxin for enhanced catalysis of protein oxidation in the periplasm reveals a phylogenetically conserved substrate specificity determinant.
Masip L
The Journal of Biological Chemistry, 283(2), 840-848 (2008)
F R Blattner et al.
Science (New York, N.Y.), 196(4286), 161-169 (1977-04-08)
The Charon lambda bacteriophages have been developed as vectors for cloning. Their construction incorporates mutations that make them simple to use and also greatly increases their safety for the biological containment of cloned recombinant DNA. Three of the Charon vector
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