Between 1990 and 2017, the worldwide rate of female infertility has increased by nearly 15% (Sun et al., 2019). The major factor responsible for early pregnancy loss is attributed to the failure of an embryo to implant into the uterus. A number of studies have identified molecules that are necessary for successful implantation, but their function during implantation remains poorly understood (Zhang et al., 2013). Therefore, it is imperative to further investigate the process of embryo implantation to progress the field of reproduction and fertility. The cell surface glycoprotein basigin, is necessary for embryo implantation in the mouse (Li & Nowak, 2020) and plays a significant role in many cellular functions including cell communication and the remodeling of the extracellular matrix (Chen et al., 2009). In vitro studies using human uterine cells grown in culture, demonstrate that basigin regulates the expression and secretion of enzymes called matrix metalloproteinases, (MMPs) which are critical for successful implantation to occur in the mouse (Belton et al., 2008). Recently, our lab purified the anti-basigin-2 monoclonal antibody originally developed by Dr. Belton at the University of Illinois. We hypothesize that this monoclonal antibody (P2D7) will specifically label human basigin proteins in human uterine tissue. To test this hypothesis, we sectioned paraffin-embedded human endometrial tissue samples and performed immunohistochemistry (IHC) using the P2D7 antibody to demonstrate antibody labeling of basigin proteins. Antibody competition assays were also performed using the purified recombinant basigin protein (rBSG) to block antibody binding to the tissues. Our results reveal that the P2D7 antibody specifically and reproducibly labels basigin within the uterine tissue samples. These results will allow us to address the overall research question of “Is basigin-2 involved in cellular migration of human endometrial stromal cells?”

Class Standing

Graduate Student



Faculty Advisor

Dr. Robert Belton

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