Recombinant PKN1 protein (His tag)

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Recombinant human Serine/threonine-protein kinase N1 (PKN1) fragment (residues 608-942), encompassing the complete Protein kinase and AGC-kinase C-terminal domains. This high-purity fragment serves as an essential tool for investigating kinase activity, substrate interactions, and domain-specific functions in cytoskeletal regulation, transcriptional activation, and cell signaling pathways.

Serine/threonine-protein kinase N1 (PKN1) is a multifunctional kinase involved in critical cellular processes including cytoskeletal organization through phosphorylation of vimentin and neurofilament proteins, cell migration, tumor invasion, and transcription regulation. The kinase functions as a key coactivator of androgen receptor-dependent transcription by mediating histone H3 phosphorylation at Thr-11, promoting epigenetic activation. PKN1 localizes to multiple cellular compartments including cytoplasm, nucleus, endosomes, and cell membranes, with dynamic redistribution during cell division where it accumulates at the cleavage furrow and midbody. The full-length protein participates in adrenergic receptor signaling cascades leading to MAPK14 activation and regulates histone deacetylase nuclear import through phosphorylation. The 608-942 fragment retains the complete catalytic and regulatory domains necessary for studying these fundamental biological mechanisms.