July 2021 News
You may have noticed that we recently updated our homepage, as our previous version became unstable for some unknown probably computer code related reason. We hope you like the newer version.
We are glad to report that our recent paper, “TNFα increases tyrosine hydroxylase expression in human monocytes”, an early version of which was posted on the BioRΧiv server has been accepted for publication in NPJ Parkinson’s disease and can now be freely downloaded, from the journal here and also from Pubmed here. The Nature partner journals series, abbreviated NPJ, are a series of online-only, open access journals spun off by the journal Nature, one of the most prestigious and respected in science. This high impact journal is associated with the journal Parkinson’s Foundation and so provides a good venue to contact scientists and clinicians engaged in Parkinson’s disease research. The paper makes use of a sensitive and novel tyrosine hydroxylase ELISA developed using EnCor antibodies MCA-4H2 and RPCA-TH which we are now preparing for commercialization. For a write up of this work published on the University of Florida web site see here.
We also release a novel goat polyclonal antibody to neurofilament NF-H GPCA-NF-H. This protein is heavily expressed in axons and is also released into blood and CSF following axonal compromise providing a useful surrogate marker of axonal damage and degeneration.
Finally we continue to characterize the epitopes for our various monoclonal antibodies. An interesting recent finding it the mapping of one of our neurofilament NF-L monoclonals MCA-1B11. We showed that this binds to a highly conserved region of the dimeric α-helical coiled coil region of human NF-L. Much interest has been focused on the use of a neurofilament NF-L ELISA from Uman Diagnostics to monitor axonal loss following CNS compromise. The NF light Uman assay which utilizes two mouse monoclonal antibodies, clone 2.1 for NF-L detection and clone 47.3 for NF-L capture (see Norgren et al. 2002). These two clones are also known as UD1 and UD2 respectively. Interestingly our MCA-1B11 binds to the same epitope as the Uman detection reagent, UD1/clone 2.1. We are currently characterizing the epitope for the other Uman reagent and will shortly submit our findings on this to peer review. This work will lead to a better understanding of exactly how the Uman assay works and may lead to the development of novel second generation NF-L assays.
