Recombinant Human PKCe protein

Protein kinase C epsilon (PKCε), a member of the protein kinase C (PKC) family, is a calcium-independent, phospholipid-dependent serine/threonine kinase classified under the novel PKC subfamily (nPKC). It plays critical roles in diverse cellular processes, including cell proliferation, apoptosis, differentiation, and stress responses. PKCε is distinct from other PKC isoforms due to its unique regulatory domain structure and activation mechanisms, primarily mediated by lipid second messengers like diacylglycerol (DAG) and phosphatidylserine. Its dysregulation has been implicated in cancer, neurodegenerative disorders, cardiovascular diseases, and metabolic syndromes, making it a key therapeutic target.

Recombinant PKCε proteins are engineered using heterologous expression systems (e.g., *E. coli*, insect cells, or mammalian cells*) to produce highly purified, functional kinase domains or full-length proteins for *in vitro* studies. These recombinant forms retain catalytic activity and substrate specificity, enabling researchers to investigate PKCε's signaling mechanisms, substrate interactions, and regulatory pathways. Tagged versions (e.g., His-tag, GST-tag) facilitate purification, detection, and protein-protein interaction assays.

Research applications include kinase activity assays, structural studies (e.g., X-ray crystallography), inhibitor screening for drug development, and elucidating its role in disease models. For instance, PKCε overexpression in cancer correlates with tumor invasiveness and chemoresistance, while its cardioprotective effects in ischemia-reperfusion injury highlight context-dependent functions. Recombinant PKCε tools have advanced the understanding of its dual roles in cell survival and stress adaptation, offering potential for targeted therapies. However, challenges remain in achieving post-translational modifications (e.g., phosphorylation) in certain expression systems, necessitating system-specific optimization.