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A sodium acetate buffer was used at pH 2.0 5.0, a potassium dihydrogen phosphate buffer was used at pH 6.0 8.0, and a carbonate bicarbonate buffer was prepared at pH 9.0 11.0.
Lysis buffer was used at 100 μl per 20 μl of packed cell volume (PCV).
When citrate buffer was used at a concentration of 5 mM, similar results were found (data not shown).
Secondary anti-rabbit-horseradish peroxidase conjugate (Pierce Biotechnology) in blocking buffer was used at 1 10000 for Gapdh, Smad3, and phospho- Smad3 for 1 h.
Secondary anti-goat-horseradish peroxidase conjugate (Pierce Biotechnology) in blocking buffer was used at 1 10000 for Myostatin for 1 h.
Tris buffer was used at a concentration of 50 mM in each reaction, demonstrating the ability of this assay to quantify the products of enzymatic processes in complex biochemical mixtures.
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For this purpose, a small buffer is used at the output of the FEC encoder in order to store l o g 2 q) bits from each one of the two RSC encoder outputs.
Bis-Tris 10% gels with MES SDS running buffer were used at 100 V for 70 min. Staining was performed using a SilverSNAP II stain kit according to the manufacturer's instructions.
To investigate the stability of oxytocin in the presence of a combination of buffer and monovalent metal ions, citrate and acetate buffer were used at a concentration of 10 mM, in combination with the monovalent metal ions, sodium and potassium, added at a concentration of 10 and 20 mM (excluding sodium from the buffer component).
The columns and the buffers were used at the same temperature.
For calibration, Mettler Toledo pH 4.01 ± 0.02 and pH 9.21 ± 0.02 buffers were used at room temperature.
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