More February 2015 News

Our immunocytochemical images continue to be used in books, journals and news articles, usually without any attribution, since we did not bother to copyright or watermark any of them. Many have been sent freely to our OEM partners and in some cases to Wikipedia. Scroll down in this very recent high profile on line article entitled “An Inflammatory Theory of Brain Disease” to see one of our images. The article is an interesting PBS NOVA write up of some progress (and also lack thereof) in the search for effective therapies to treat human brain diseases. The image in the article is of our mixed neural cells grown in tissue culture stained with our microglial cell marker Coronin 1a in green and the neuronal marker α-internexin in red. This particular image was in fact provided to Wikipedia Commons for unfettered use as shown here.

New Antibodies and New Data

We release several new antibodies. These are a new mouse antibody to muscleblind like protein 1, MCA-1H1, and several to Calbindin, made in both mouse MCA-5A9, MCA-4H7 and chicken CPCA-Calb (page in preparation). We also continue to develop a better understanding of all of our current reagents. For example, we previously made antibodies to the abundant cytoplasmic enzyme Aldolase C, both monoclonal and polyclonal. A potential problem with antibodies to this protein is cross-reactivity with the Aldolase A and B molecules which are very similar in amino acid sequence. Each Aldolase is 70-80% identical to the other two and the molecules have very similar molecular sizes on SDS-PAGE gels so one cannot distinguish which protein is being detected using western blotting. So we went to the trouble of expressing both human Aldolase A and B in order to test our panel of Aldolase C antibodies. We found that two of our monoclonals MCA-1A1 and MCA-4A9 were absolutely specific for Aldolase C, while a third MCA-E9 recognized all three Aldolases. We suspected that this might be the case since MCA-1A1 and MCA-4A9 were made against the C and N-terminal peptides respectively, which are the least conserved parts of the three Aldolases. In contrast, MCA-E9 was made against the intact human recombinant protein, and we now know that the epitope does not include either the N or C terminal sequences. Our rabbit polyclonal antibody to Aldolase C, RPCA-AldC, (page in preparation) not surprisingly, also recognizes all three Aldolase enzymes. Since Aldolases are abundant enzymes found in many tissues, we believe that using antibodies such as MCA-E9 and RPCA-AldC, which recognize all three, might be particularly useful as a western blotting standard, similar to our pan-specific actin antibody MCA-5J11.