추천 제품
product name
N-Z-Amine® A, Casein enzymatic hydrolysate, Suitable for microbiology
생물학적 소스
bovine milk
Quality Level
형태
powder
포장
poly bottle of 250, 500 g
poly bottle of 1 kg
poly drum of 5 kg
질소 분석
≥6% amino, ≥11.0% total
손실
≤11% loss on drying
pH
5.8-7.8
응용 분야
food and beverages
microbiology
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일반 설명
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.
애플리케이션
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
재구성
Recommended concentration: 25 g/L
법적 정보
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
Choose from one of the most recent versions:
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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