83263
BICINE buffer Solution
BioUltra, for molecular biology, 1 M in H2O
Sinónimos:
N,N-Bis(2-hydroxyethyl)glycine
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About This Item
Fórmula empírica (notación de Hill):
C6H13NO4
Número de CAS:
Peso molecular:
163.17
Beilstein/REAXYS Number:
1769362
MDL number:
UNSPSC Code:
12161700
eCl@ss:
32129211
PubChem Substance ID:
grade
for molecular biology
product line
BioUltra
concentration
1 M in H2O
impurities
DNases, none detected
RNases, none detected
phosphatases, none detected
proteases, none detected
pH
5.0±0.2
density
1.05 g/mL at 20 °C
λ
neat
UV absorption
λ: 260 nm Amax: <0.07
λ: 280 nm Amax: <0.04
suitability
in accordance for filter test
SMILES string
OCCN(CCO)CC(O)=O
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves
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S Ito et al.
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
Raewyn M Town et al.
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
Dominik Koszel et al.
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.
D Parkinson et al.
Radiation research, 90(2), 252-259 (1982-05-01)
A Hausladen et al.
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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