Anti-PKC iota/PRKCI Antibody Picoband® Fluoro647 Conjugated

Protein kinase C iota type, also called PKCI, is an enzyme that in humans is encoded by the PRKCI gene. This gene encodes a member of the protein kinase C (PKC) family of serine/threonine protein kinases. This protein kinase is calcium-independent and phospholipid-dependent. It is not activated by phorbolesters or diacylglycerol. This kinase can be recruited to vesicle tubular clusters (VTCs) by interaction with the small GTPase RAB2, where this kinase phosphorylates glyceraldehyde-3-phosphate dehydrogenase (GAPD/GAPDH) and plays a role in microtubule dynamics in the early secretory pathway. PRKCI is found to be necessary for BCL-ABL-mediated resistance to drug-induced apoptosis and therefore protects leukemia cells against drug-induced apoptosis. PRKCI is also a hedgehog target gene that forms a positive feedback loop with GLI and exists at increased levels in basal cell carcinomas.

E.coli-derived human PKC iota recombinant protein (Position: D21-Q214) . Human PKC iota shares 96% and 97% amino acid (aa) sequence identity with mouse and rat PKC iota, respectively.

Predominantly expressed in lung and brain, but also expressed at lower levels in many tissues including pancreatic islets. Highly expressed in non-small cell lung cancers. .

Calcium- and diacylglycerol-independent serine/ threonine-protein kinase that plays a general protective role against apoptotic stimuli, is involved in NF-kappa-B activation, cell survival, differentiation and polarity, and contributes to the regulation of microtubule dynamics in the early secretory pathway. Is necessary for BCR-ABL oncogene-mediated resistance to apoptotic drug in leukemia cells, protecting leukemia cells against drug-induced apoptosis. In cultured neurons, prevents amyloid beta protein-induced apoptosis by interrupting cell death process at a very early step. In glioblastoma cells, may function downstream of phosphatidylinositol 3-kinase (PI (3) K) and PDPK1 in the promotion of cell survival by phosphorylating and inhibiting the pro-apoptotic factor BAD. Can form a protein complex in non- small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and regulate ECT2 oncogenic activity by phosphorylation, which in turn promotes transformed growth and invasion. In response to nerve growth factor (NGF), acts downstream of SRC to phosphorylate and activate IRAK1, allowing the subsequent activation of NF-kappa-B and neuronal cell survival. Functions in the organization of the apical domain in epithelial cells by phosphorylating EZR. This step is crucial for activation and normal distribution of EZR at the early stages of intestinal epithelial cell differentiation. Forms a protein complex with LLGL1 and PARD6B independently of PARD3 to regulate epithelial cell polarity. Plays a role in microtubule dynamics in the early secretory pathway through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs) . In human coronary artery endothelial cells (HCAEC), is activated by saturated fatty acids and mediates lipid-induced apoptosis. .

1. Atwood, S. X., Li, M., Lee, A., Tang, J. Y., Oro, A. E. GLI activation by atypical protein kinase C lambda/iota regulates the growth of basal cell carcinomas. Nature 494: 484-488, 2013. 2. De Donato, M., Gallagher Jr., D. S., Davis, S. K, Stelly, D. M., Taylor, J.F. The assignment ofPRKCI to bovine chromosome 1q34-q36 by FISH suggests a new assignment to human chromosome 3. Cytogenet. Cell Genet. 95: 79-81, 2001. 3. Mazzarella R, Ciccodicola A, Esposito T, Arcucci A, Migliaccio C, Jones C, Schlessinger D, D'Urso M, D'Esposito M (August 1995) . Human protein kinase C Iota gene (PRKCI) is closely linked to the BTK gene in Xq21.3. Genomics 26 (3) : 629–31.

Cytoplasm. Membrane. Endosome. Nucleus. Transported into the endosome through interaction with SQSTM1/p62. After phosphorylation by SRC, transported into the nucleus through interaction with KPNB1. Colocalizes with CDK7 in the cytoplasm and nucleus. Transported to vesicular tubular clusters (VTCs) through interaction with RAB2A.