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In human ovarian cancers, high PRKCI expression correlates with high expression (show TNF Proteins) of TNFalpha and YAP1 and low infiltration of cytotoxic T cells
promotes epithelial-mesenchymal transition and induces immunosuppression through the aPKC-iota/P-Sp1 (show PSG1 Proteins)/Snail (show SNAI1 Proteins) signaling pathway in cholangiocarcinoma
Polarity signaling via CDC42 (show CDC42 Proteins)/atypical protein kinase C (show PRKCZ Proteins) can affect the dynamic turnover of the intermediate filament network to promote the polarization of the network itself.
a PI3K (show PIK3CA Proteins)/PKCiota/cyclin E (show CCNE1 Proteins) signaling pathway as a therapeutic target during ovarian tumorigenesis
results identify a novel role of PHLPP in regulating aPKC and cell polarity.
the polarity function of PRKCI during cavitation
14-3-3zeta (show YWHAZ Proteins)-mediated invasion of cancer cells was found to upregulate Snail (show SNAI1 Proteins) through the activation of atypical protein kinase C (show PRKCZ Proteins) (aPKC).
Upregulated expression of PRKCI and interaction with CDK7 (show CDK7 Proteins) is associated with esophageal squamous cell carcinoma.
the results revealed that PRKCI rs546950 variant decreased the risk of prostate cancer in an Iranian population
effects. Further studies indicated that PRKCI knockdown-mediated autophagy was associated with the inactivation of phosphatidylinositol 3-kinase alpha/AKT (show AKT1 Proteins)-mammalian target of rapamycin (show FRAP1 Proteins) (PIK3CA (show PIK3CA Proteins)/AKT (show AKT1 Proteins)-MTOR (show FRAP1 Proteins)) signaling.
the aPKC-CBP (show CREBBP Proteins) pathway is a homeostatic compensatory mechanism that modulates hippocampal neurogenesis and memory in an age-dependent manner in response to reduced CREB (show CREB1 Proteins) activity.
he oncogenic activity of PRKCI relates in part to the up-regulation of TNFalpha (show TNF Proteins) to promote an immune-suppressive tumor microenvironment characterized by an abundance of myeloid-derived suppressor cells and inhibition of cytotoxic T-cell infiltration
Selective deletion of the aPKC isoform Pkc-lambda in proopiomelanocortin (POMC (show POMC Proteins)) neurons disrupts leptin (show LEP Proteins) action, reduces melanocortin content in the paraventricular nucleus, and markedly increases susceptibility to obesity, glucose intolerance, and insulin (show INS Proteins) resistance specifically in HFD-fed male mice.
Prkci and its downstream partners direct polarized cell division of luminal myocardial cells to drive trabeculation in the nascent heart.
Prkci regulates expansion of various stem cells via Notch (show NOTCH1 Proteins)-dependent pathway.
PKClambda/iota could be a crucial regulator of mitochondrial function and energy metabolism in stem cells and other cellular contexts
Asymmetric division and CD8+ T lymphocyte fate specification is regulated by protein kinase Czeta and protein kinase Clambda.
adenoviral-mediated supplementation of hepatic PKC-lambda induced a diabetic state in heterozygous PKC-lambda knockout mice.
Data indicate that pseudosubstrate arginine residues are key regulators of atypical protein kinase C (show PRKCZ Proteins)-lambda and atypical protein kinase C-zeta (show PRKCZ Proteins).
Zebrafish pronephros tubulogenesis and epithelial identity maintenance are reliant on the polarity proteins Prkc iota and zeta.
a loss of zBves affects the proteins involved in the pathway of the PAR (show AFG3L2 Proteins) junctional complex, especially aPKC, and both aPKC and Bves (show BVES Proteins) are indispensable to claudin expression.
Heart and soul/PRKCi and nagie oko/Mpp5 regulate myocardial coherence and remodeling during cardiac morphogenesis.
PrkCi function and planar divisions are necessary for asymmetric, self-renewing division of spinal cord precursors.
These data identify atypical PKC isozymes as STAT and ERK activators that mediate c-fos and collagenase expression.
This gene encodes a member of the protein kinase C (PKC) family of serine/threonine protein kinases. The PKC family comprises at least eight members, which are differentially expressed and are involved in a wide variety of cellular processes. 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 direct 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. This kinase is found to be necessary for BCL-ABL-mediated resistance to drug-induced apoptosis and therefore protects leukemia cells against drug-induced apoptosis. There is a single exon pseudogene mapped on chromosome X.
protein kinase C, iota
, protein kinase C iota
, protein kinase C iota type
, 17 kDa inhibitor of protein kinase C
, adenosine 5'-monophosphoramidase
, histidine triad nucleotide-binding protein 1
, protein kinase C inhibitor 1
, protein kinase C-interacting protein 1
, atypical protein kinase C-lambda/iota
, protein kinase C, lambda
, heart and soul protein