CG&D
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cell Growth & Differentiation

Right arrow Help viewing high resolution images
Right arrow Return to article


Fig. 1. PKC C2 and V5 domain constructs. This figure outlines the structure of classical (PKC{alpha}, PKCßI, and PKCßII) and novel (PKC{delta} and PKC{epsilon}) PKC isoforms and highlights in gray the C2 and V5 regions used in this study. SK-N-BE(2) cells were transfected with expression vectors coding for EGFP alone and for PKC{alpha}, PKC{delta}, and PKC{epsilon} C2 domains and PKC{alpha}, PKCßI, and PKCßII V5 domains fused to EGFP. Cell lysates (60 µg of cellular protein) were subjected to Western blot analysis with polyclonal anti-green fluorescent protein antibody. The positions of molecular weight markers (97, 66, 46, 30, and 21) are indicated (in thousands). Arrowheads indicate the positions of the V5 and C2 domain-EGFP fusion proteins. An unspecific band at approximately Mr 55,000 is also detected with this antibody.





Right arrow Return to article


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cell Growth & Differentiation