83263
BICINE buffer Solution
BioUltra, for molecular biology, 1 M in H2O
Sinonimo/i:
N,N-Bis(2-hydroxyethyl)glycine
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About This Item
Grado
for molecular biology
Nome Commerciale
BioUltra
Concentrazione
1 M in H2O
Impurezze
DNases, none detected
RNases, none detected
phosphatases, none detected
proteases, none detected
pH
5.0±0.2
Densità
1.05 g/mL at 20 °C
λ
neat
Assorbanza UV
λ: 260 nm Amax: <0.07
λ: 280 nm Amax: <0.04
Compatibilità
in accordance for filter test
Stringa SMILE
OCCN(CCO)CC(O)=O
Codice della classe di stoccaggio
12 - Non Combustible Liquids
Classe di pericolosità dell'acqua (WGK)
WGK 3
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Dispositivi di protezione individuale
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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