|
|
|
|
|
|
|
|
|||||
| Home Help Feedback Subscriptions Archive Search Table of Contents | |||||
|
Fig. 4. Induction of p38
phosphorylation by NP60. (A) Flag-p38 was co-transfected with myc-NP60 in 293T cells. Cell extracts were prepared 24 hours after transfection. Total proteins were analyzed by immunoblotting with anti-phospho-p38 (*P-p38) antibody. Equal loading was confirmed by immunoblotting with anti-p38 antibody as indicated. (B) Cell extracts were prepared from NP60-transfected 293T cells. Total proteins were analyzed by immunoblotting with anti-phospho-p38 antibody. Equal loading was confirmed by immunoblotting with anti-p38 antibody as indicated. (C) Cell extracts of truncated NP60 mutants co-transfected with p38. Total proteins were analyzed by immunoblotting with anti-phospho-p38 antibody. (D) 293T cells were co-transfected with myc-NP60 and Flag-JNK1. Cell extracts were prepared after transfection. Total proteins were analyzed by immunoblotting with anti-phospho-JNK antibody. (E) 293T cells were co-transfected with myc-NP60 and Flag-ERK2. Total proteins were analyzed by immunoblotting with anti-phospho-ERK antibody. (F) 293T cells were transfected with interference plasmid mu6, or the plasmid containing interference sequence of NP60 at two concentrations. Total RNA was extracted after transfection for 48 hours and used for RT-RCR analysis with NP60 primers. (G) 293T cells were transfected with interference plasmid mu6 and the plasmid containing interference sequence of NP60. Cells were treated with sorbitol for 30 minutes after transfection for 48 hours. Total proteins were extracted and subjected to western blot assay using anti-phospho-p38, or anti-phospho-JNK or anti-phospho-ERK as indicated. Normalization of loading was assessed using p38 antibody.
|
