Human CAPN1 adenoviral particles

The CAPN1 gene is located on human chromosome 11q13 and encodes the ubiquitous calcium-dependent cysteine protease Calpain-1, also known as μ-calpain. The enzyme is an important component of the calpain system, a family of proteases that play a key role in mediating intracellular signaling pathways triggered by calcium influx. Calpain-1 functions as a heterodimer and contains a large catalytic subunit (encoded by CAPN1, approximately 80 kDa) and a smaller regulatory subunit (CAPNS1, approximately 28 kDa). Calpain-1 does not act as a degradative protease like proteases in lysosomes, but rather as a highly specific regulator that performs limited proteolysis (“calpain hydrolysis”) of target proteins. This precise cleavage alters the activity, localization, or interactions of its substrates, thereby regulating fundamental cellular processes including cytoskeletal remodeling (cleavage of spectrin, talin, and cytosolic proteins), cell migration, membrane repair, signal transduction (regulation of kinases, phosphatases, and G proteins), apoptosis, synaptic plasticity, and cell cycle progression. Dysregulated CAPN1 expression or activity is implicated in a range of pathological conditions, such as traumatic brain injury, stroke, Alzheimer''s disease, muscular dystrophy, cancer metastasis, and cataracts.

Human CAPN1 adenoviral particles are advanced molecular tools specifically designed for efficient delivery and stable expression of the human CAPN1 gene to a variety of mammalian cell types in vitro and in vivo. These particles are constructed using a replication-defective human adenovirus serotype 5 (Ad5) backbone from which essential viral genes (usually the E1 region and often the E3 region) have been deleted, rendering the virus unable to replicate autonomously in standard host cells. The resulting human CAPN1 adenoviral particles offer significant advantages for research. Their broad tropism enables efficient transduction of a variety of cell types, including primary cells and neurons, which are often difficult to access using other transfection methods. This overexpression is essential for gain-of-function studies, allowing researchers to investigate the effects of elevated Calpain-1 activity on cell signaling, structure, motility, and disease-associated phenotypes. In addition, these particles can be used in animal models to explore the role of Calpain-1 in complex physiological or pathological processes in vivo.