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. Author manuscript; available in PMC: 2012 Jan 1.
Published in final edited form as: J Neuropathol Exp Neurol. 2011 Jan;70(1):36–50. doi: 10.1097/NEN.0b013e318202bfa1

Figure 2.

Figure 2

Western blots of frontal cortex homogenates, and nuclear and cytoplasmic fractions from 6 control (Con), Down syndrome (DS), and Alzheimer disease (AD) subjects. (A-F) Blots were immunostained with mAb 8D9 to detect DYRK1A (A, C, E). In DS, the level of DYRK1A in frontal cortex homogenates, and nuclear and cytoplasmic fractions was 1.68 × (p < 0.0001), 1.67 × (p < 0.0001), and 1.51× (p < 0.01) higher, respectively, than in the control subjects (B, D, F). The differences between AD and controls were not significant. Western blots with mAb SF2/ASF revealed alternative splicing factor (ASF) in the range of 34 kDa (A, C, E), with no significant difference between levels of ASF in homogenates, nuclear and cytoplasmic fractions of control, DS and AD subjects (B, D, F). The loads per lane were 20 μg of homogenates and cytoplasmic fractions protein, and 10 μg of nuclear fraction protein. The protein loading in homogenates and cytoplasmic fractions was verified by β-actin blots (mAb AC-15) and in nuclear fractions by p62 blot (mAb Nup62). The nearly complete absence of cytoplasmic β-actin (C) confirmed the purity of the nuclear fraction, whereas uniform levels of nuclear marker (Nup62) confirmed nuclei preservation.