Western blotting in may cases is a combination of techniques. Process samples (proteins), run samples on a PAGE gel (SDS or Native) and transfer to a membrane (PVDF or Nitrocellulose). This transfers the proteins separated by size/charge or both ot the membrane. The unbound portions (i.e. any part of the membrane that doesn't have protein bound to it) of the membrane are blocked with any number of substances (skim milk/BSA/Casein/etc) and the blot probed with an antibody of interest. The bound antibody is labeled, usually by using a second antibody that labels the FC portion of the first antibody (and depends also on the species from which the first antibody is derived) that is tagged with some sort of molecule that will react with your substrate of choice to show the signal.
EX. Antigen of interest detected by an antibody made in mouse to the antigen, the bound mouse antibody is labeled by a goat anti-mouse antibody labeled with HRP (horseradish peroxidase). The substrate is added and the HRP cleaves the substrate to give a signal (visible/chemiluminescent) that is detected by an appropriate instrument.
"Western" refers to the detection of a protein with an antibody, as opposed to "Northern" or "Southern" blotting which are used for RNA and DNA detection respectively.
I would suggest searching on line for a manual on PAGE and western blotting rather than in a specific journal. It will explain the techniques in a bit more detail.....