Recombinant Human PKN2 protein

**Background of PKN2 Recombinant Protein**

PKN2 (Protein Kinase N2), also known as PRKCL2. is a serine/threonine kinase belonging to the protein kinase C (PKC) superfamily. It plays a critical role in regulating diverse cellular processes, including cytoskeletal organization, cell proliferation, apoptosis, and migration. Structurally, PKN2 contains an N-terminal regulatory region with a conserved C2-like domain and three antiparallel coiled-coil motifs, as well as a C-terminal catalytic kinase domain. The N-terminal region mediates interactions with small GTPases like RhoA and Rac1. linking PKN2 to Rho-mediated signaling pathways involved in cell adhesion and motility.

Recombinant PKN2 protein is engineered using expression systems such as *E. coli* or mammalian cells, often fused with tags (e.g., GST, His) for purification and detection. This allows researchers to study its enzymatic activity, substrate specificity, and interactions in vitro. PKN2 is implicated in cancer progression, as it regulates pathways like mTOR and NF-κB, influencing tumor cell survival and invasion. Additionally, PKN2 interacts with components of the Wnt/β-catenin pathway, suggesting roles in development and tissue homeostasis.

Studies using PKN2 recombinant protein have advanced understanding of its phosphorylation targets, including proteins like β-catenin and MYPT1. and its modulation by lipids or kinases like PDK1. Despite its importance, PKN2’s functional overlap with other PKN family members (PKN1 and PKN3) complicates mechanistic studies, necessitating isoform-specific tools. Recombinant PKN2 remains a vital reagent for biochemical assays, inhibitor screening, and structural studies, with potential therapeutic applications in cancer and fibrosis. Ongoing research aims to clarify its context-dependent roles and validate its candidacy as a drug target.