The protein encoded by the Platelet-Derived Growth Factor Receptor Alpha (PDGFRA) gene is a cell surface tyrosine kinase receptor that can bind with members of the platelet-derived growth factor family. These receptors have intracellular tyrosine kinase activity and are catalytic receptors. They play a regulatory role in multiple biological processes such as embryonic development, angiogenesis, tumor progression, and cell proliferation and differentiation, and have a proliferative effect on cells of mesenchymal origin. After the platelet-derived growth factor protein ligand binds with PDGFRA, it can trigger receptor dimerization and autophosphorylation, thereby activating several downstream signaling pathways. This signal transduction encoded by the receptor plays an important role in gastrulation and the development of almost all organ systems.

This strain was constructed by integrating the Cre recombinase gene expression element into the mouse endogenous Pdgfra gene using gene editing technology. Heterozygous Pdgfra-Cre mice are viable and fertile. In this strain, the expression of Cre recombinase is driven by the mouse endogenous Pdgfra gene expression regulatory elements, but the normal expression and function of the mouse Pdgfra gene are disrupted. Research shows that when Pdgfra-Cre mice are bred with mice containing loxP-flanked sequence, the expected Cre recombinase-mediated recombination will result in the deletion of the floxed sequences in the inner nuclear layer (INL) of the retina of the offspring, and some Cre recombinase activity can also be detected in the outer nuclear layer (ONL) and ganglion cell layer (GCL). Internal detection results show that there is obvious Cre recombinase expression in the retina, uvea, lens, cornea, and other eye tissues of Pdgfra-Cre mice, and a small amount of Cre recombinase activity also exists in tissues such as the skin, brain, and spinal cord.