luck

for some unknown reason, I have been really, really lucky with all things science this year. Everything I've tried works, or at least works with minor issues. Yesterday, I managed to get a fairly decent western blot from a new antibody that isn't very homologous to my protein (it's only 70% with the recommended minimum is 75%). To add to all that, the antibody was held up in Australian customs for a week without refrigeration, so I really had no idea if it would work at all. And, it even works when it's really diluted (1:50,000) so I don't have to worry about using it all up. All in all, it was a good day.

Translation: a western blot basically allows you to identify proteins. You grind up tissue in a special buffer with things that keep enzymes from destroying your ptoteins. Spin all the non-protein junk down to the bottom of a tube, figure out how much protein you actually have in your tube using a very cool assay that changed from green to purple when it finds protein. Then you load your proteins onto a gel to separate them according to size, transfer all the proteins on the gel laterally onto a membrane using an electrical current, then apply your antibody to your membrane. Unfortunately, you can't see what your antibody is binding to at this point so you have to apply another antibody, called the secondary, that recognizes a little tag on your first antibody. The secondary has its own little tag that can be made to give off light. So you expose your membrane to film and develop it and you have a western. If an antibody is 70% homologous it means that the chunk of your protein that the antibody binds to has 70% of the same amino acids. The more amino acids that are the same, the better the antibody binds.
Now you can all call ourselves molecular biologists. Funny enough, there's also Southern and northern blots. East was left out of the party, but we can save that lesson for another day.