Gene Researcher at the Taubert Lab: Day 3

18 03 2012

Today, I learned about Western blot also known as the immuno blot. Just as PCR detects and amplify specific DNA sequences, the western blot detects specific proteins in a sample. I once again used gel electrophoresis to separate proteins by 3-D structure or denatured proteins by the length of the polypeptide. This time I used SDS- Page as in most proteins, the binding of SDS to the polypeptide chain gives an even distribution of charge per unit. I also heated the sample to 60 degrees Celsius to promote protein denaturation and thus, help SDS bind. A tracking dye was added to the protein solution so we could track the progress of the protein solution through the gel during the run. Afterwards, the proteins are transferred to a membrane where they are searched using antibodies specific to the target protein. Since it was my second time making gel electrophoresis, I found easy to pipette the solution into the holes.


Although reading about Western blotting does not take that long, the actual process actually took the whole day. And in the end, only one of the two samples worked. I was a bit disappointed, but I guess that is what happens in science: experiments don’t always turn out the way you want them to turn out.


– Alice Yip




2 responses

19 03 2012

Wow the whole day? I guess scientists have to be pretty positive and look at the bright side… ! What can you use the separated proteins for?

28 03 2012

One of two samples worked? That’s the “glamour” of doing science for real! That is, it’s a lot harder work than it looks like on TV. 🙂 I remember days during my graduate degree where I was further behind at the end of the day than at the beginning. At beginning of the day I had a sample that I’d spent the entire previous day preparing and was ready to test. At the end of the day….well, something had gone wrong, the sample was damaged, and I had to start making a new one. It’s just the nature of experimental science. You have to be persistent.

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