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Wichtige Dokumente
83263
BICINE-Pufferlösung
BioUltra, for molecular biology, 1 M in H2O
Synonym(e):
N,N-Bis-(2-hydroxyethyl)-glycin
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About This Item
Qualität
for molecular biology
Produktlinie
BioUltra
Konzentration
1 M in H2O
Verunreinigungen
DNases, none detected
RNases, none detected
phosphatases, none detected
proteases, none detected
pH-Wert
5.0±0.2
Dichte
1.05 g/mL at 20 °C
λ
neat
UV-Absorption
λ: 260 nm Amax: <0.07
λ: 280 nm Amax: <0.04
Eignung
in accordance for filter test
SMILES String
OCCN(CCO)CC(O)=O
Lagerklassenschlüssel
12 - Non Combustible Liquids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Eyeshields, Gloves
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Clinica chimica acta; international journal of clinical chemistry, 115(2), 135-144 (1981-09-10)
Serum guanase activity has been considered as a possible specific indicator of hepatocellular diseases. However, no suitable method is available for routine clinical determination of serum guanase activity. Conventional assay methods are troublesome and inaccurate, since guanine and 8-azaguanine, the
The journal of physical chemistry. A, 112(12), 2563-2571 (2008-03-04)
The impact of ligand protonation on the complexation kinetics of higher-order complexes is quantitatively described. The theory is formulated on the basis of the usual situation for metal complex formation in aqueous systems in which the exchange of water for
Journal of enzyme inhibition and medicinal chemistry, 27(2), 167-173 (2011-06-04)
A series of bis-N,N-(2-hydroxyethyl)glycine (bicine) derivatives, conjugated with an inhibitor of glucosamine-6-phosphate synthase, have been synthesized and their lipophilic and antifungal properties have been tested. The obtained compounds demonstrated higher lipophilicity than free inhibitor (FMDP) and, in consequence, an increased
Irradiation inactivation analysis of acetylcholinesterase and the effect of buffer salts.
Radiation research, 90(2), 252-259 (1982-05-01)
Archives of biochemistry and biophysics, 306(2), 415-419 (1993-11-01)
Xanthine oxidase has long been considered to be subject to inhibition by excess substrate. It is now shown that, although such inhibition can be seen in Tris or N,N-bis(2-hydroxyethyl)glycine buffers, earlier reports in which phosphate, pyrophosphate, or Veronal buffers were
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