Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.

Protein kinase N (PKN) is a fatty acid- and Rho-activated serine/threonine protein kinase involved in the regulation of cell motility by association with cytoskeletal components such as neurofilament and alpha-actinin (1). Serine/threonine-protein kinase N1 (PKN1) belongs to the protein kinase C superfamily. It is activated by Rho family of small G proteins and may mediate the Rho-dependent signaling pathway. This kinase can be activated by phospholipids and by limited proteolysis. The phosphorylation of PKN1 by PDK1 may mediate insulin signals to the actin cytoskeleton. The proteolytic activation of this kinase by caspase-3 or related proteases during apoptosis suggests its role in signal transduction related to apoptosis (2).

A synthetic peptide corresponding to residues near the C-terminus of human PKN1 was used as an immunogen.

Rabbit

50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.

1. Bartsch JW, et al. Genomics 49(1):129-32, 1998 2. NCBI Reference Sequence (RefSeq): a curated non- redundant sequence database of genomes, transcripts and proteins. Pruitt KD, Tatusova, T, Maglott DR. Nucleic Acids Res 2007 Jan 1;35(Database issue):D61-5

Human, Mouse, Rat

Serine/threonine-protein kinase N1, Protease-activated kinase 1, PAK-1, Protein kinase C-like 1, Protein kinase C-like PKN, Protein kinase PKN-alpha, Protein-kinase C-related kinase 1, Serine-threonine protein kinase N, PKN1, PAK1, PKN, PRK1, PRKCL1

WB~~1:1000~10000 FC~~1:10~100

Function PKC-related serine/threonine-protein kinase involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation. Regulates the cytoskeletal network by phosphorylating proteins such as VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser- 159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro. Cellular_Location Cytoplasm. Nucleus. Endosome. Cell membrane; Peripheral membrane protein. Cleavage furrow. Midbody Note=Associates with chromatin in a ligand-dependent manner Localization to endosomes is mediated via its interaction with RHOB. Association to the cell membrane is dependent on Ser-374 phosphorylation. Accumulates during telophase at the cleavage furrow and finally concentrates around the midbody in cytokinesis Tissue_Location Found ubiquitously. Expressed in heart, brain, placenta, lung, skeletal muscle, kidney and pancreas. Expressed in numerous tumor cell lines, especially in breast tumor cells