Elastase-1 (ELA1), a member of the serine protease subfamily, is encoded by the Chymotrypsin-Like Elastase Family Member 1 (CELA1) gene and is capable of hydrolyzing elastin and many other proteins. Unlike other elastases, the expression of CELA1 has not been detected in the human pancreas but has been found in keratinocytes, lung epithelial cells, intestinal cells, and immune cells ^[1-4]. Following lung resection, the expression of CELA1 increases in a stretch-dependent manner, and CELA1-positive cells co-localize with elastin remodeling regions during lung development ^[5]. CELA1 plays a role in biological processes such as exocrine pancreatic development, digestive system development, pancreatic morphogenesis, and tissue remodeling. In addition, the CELA1 gene is associated with diseases such as pancreatic steatorrhea and autoimmune pancreatitis.

This strain is constructed by integrating the codon-optimized Cre recombinase (iCre) gene expression element into the 3’ untranslated region (UTR) of the mouse endogenous Cela1 gene using gene editing technology. Compared with traditional Cre recombinase, iCre recombinase has higher recombinase activity. In this strain, the expression of Cre recombinase is driven by the mouse Cela1 gene expression regulatory elements. When Cela1-P2A-iCre mice are bred with mice containing loxP sites, the expected Cre recombinase-mediated recombination will result in the deletion of the floxed sequences in the pericytes in the pancreas and lung tissues of the offspring. Detection results show that there is a high level of Cre recombinase activity in mouse pancreatic acinar cells, bronchial epithelium, and alveolar tissue.