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The identity of the ventricular/slow skeletal isoform of the essential light chain band was confirmed using Western blot against MYL3.
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All proteins identified in 1-D BN bands were confirmed using 2-D gel.
The increased expression was confirmed using band densitometry.
However, BOB-3 was more powerful in RhB degradation because larger numbers of superoxide radicals were generated via electron injection from the excited RhB to its more negative conduction band under visible-light irradiation; this was confirmed using active oxygen species measurements and electron spin resonance analysis.
Western blot gave a major band with BCECs at the expected size, which was confirmed using the human calu-3 cells.
More importantly, 4E-BP1 became hyperphosphorylated, as indicated by band shifts at day 3 onwards of ligation, and this was confirmed using anti-phospho-Thr37/46-4E-BP1 antibody.
The purity of the RNA was determined using a spectrophotometer and integrity was confirmed using gel electrophoresis and visualization of ribosomal bands.
This finding was confirmed using GATA-1 antibody, resulting in a supershift of the lower (GATA-1) band (data not shown).
Specificity of the anti-E2F-5 antibody was confirmed using an E2F-5 blocking peptide (SC-999 P, Santa Cruz Biotechnology) and by a single band at 59 kDa detected by immunoblotting.
This was confirmed using TBR1 null mice.
Convergence was confirmed using AWTY [67].
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