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ACTN1 was used to correct for loading differences.
ADAMs immunoblots were normalized for loading differences using b-actin.
PKC isoforms immunoblots were normalized for loading differences using β-actin.
The blots were probed with anti-β-actin antibodies (Sigma, A1978, lot 118K4827) to control for loading differences.
Band intensities in the blots were later quantified using ImageJ 1.38× [19] and α-Tubulin or β-Actin bands were used to adjust for loading differences.
Although this sequence associates with Cdc45p as the replication fork moves across, it does so later and was therefore considered to be the best choice in order to control for loading differences.
Similar(42)
Cells were incubated at 25°C for 30 min with 10 μ m CM-H2DCFDA and FACS analysis was performed immediately and every 30 min for 3 h to allow for dye loading differences.
This was followed by normalization to the total spectral count for all bands of one lane to account for possible loading differences.
Each lysate sample was loaded into two adjacent lanes of a 10% polyacrylamide gel for minimizing loading differences if indicated.
To account for protein loading differences in the seven samples, a small fraction (~0.1%) of the supernatant from the tyrosine phosphopeptide immunoprecipitation was analysed by LC-MS/MS, thereby providing quantification for the non-phosphorylated peptides in each sample.
Therefore, subtracting the Ct of the reference genes (or taking the ratio on the exponential scale) would adjust for these RNA loading differences.
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