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anti-Human PKC iota Anticorps:
anti-Mouse (Murine) PKC iota Anticorps:
anti-Rat (Rattus) PKC iota Anticorps:
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Human Polyclonal PKC iota Primary Antibody pour IHC (p), ELISA - ABIN545464
Roehrl, Hyberts, Sun, Fields, Wagner: Rapid backbone 1H, 13C, and 15N assignment of the V1 domain of human PKC iota using the new program IBIS. dans Journal of biomolecular NMR 2003
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Human Polyclonal PKC iota Primary Antibody pour IHC (p), WB - ABIN391010
Li, Wang, Liu, Xiao, Lu, Zou: Correlation of aPKC-iota and E-cadherin expression with invasion and prognosis of cholangiocarcinoma. dans Hepatobiliary & pancreatic diseases international : HBPD INT 2008
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Study results led to the conclusion that the detection of PKC-iota may be used as a biomarker of prostate carcinogenesis and that PKC-iota inhibition may be an alternative therapy in patients with prostate cancer.
aPKClambda phosphorylates the DNA binding domain of forkhead box O1 (FoxO1) transcription factor, a gatekeeper of endothelial growth.
Results show a correlation was found between the overexpression of aPKClambda/iota and the degree of pathological differentiation in oral squamous cell carcinoma (OSCC). The nuclear localization of aPKClambda/iota was associated with progression-free survival of OSCC. Overall, the expression and localization of aPKClambda/iota may be involved in the degree of malignancy in OSCC, which is related to prognosis.
We also carried out PKC-iota and PKC-zeta directed siRNA treatments to prove the above observations. Immunoprecipitation data suggested an association between PKC-iota and vimentin and PKC-iota siRNA treatments confirmed that PKC-iota activates vimentin by phosphorylation. These results further suggested that PKC-iota is involved in signaling pathways which upregulate EMT and which can be effectively suppressed using A...
These results indicate that PKCiota/lambda is dispensable for Cdc42-triggered processes and for thrombosis and hemostasis in mice.
14-3-3zeta and aPKC-iota synergistically facilitate EMT of CCA via GSK-3beta/Snail signalling pathway.
In human ovarian cancers, high PRKCI expression correlates with high expression of TNFalpha and YAP1 and low infiltration of cytotoxic T cells
promotes epithelial-mesenchymal transition and induces immunosuppression through the aPKC-iota/P-Sp1/Snail signaling pathway in cholangiocarcinoma
Polarity signaling via CDC42/atypical protein kinase C can affect the dynamic turnover of the intermediate filament network to promote the polarization of the network itself.
a PI3K/PKCiota/cyclin E 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-mediated invasion of cancer cells was found to upregulate Snail through the activation of atypical protein kinase C (aPKC).
Upregulated expression of PRKCI and interaction with CDK7 is associated with esophageal squamous cell carcinoma.
This is the first report on the relationship between aPKC[lambda]/[iota] expression patterns and cervical intraepithelial neoplasia progression or regression.
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-mammalian target of rapamycin (PIK3CA/AKT-MTOR) signaling.
the knockdown of aPKC increases and extends TGFbeta-induced p38 MAPK activation, which sensitizes NSCLC cells to undergo apoptosis.
PKCiota binds to Rab14 and that PKCiota requires Rab14 for its correct distribution in cells. As with Rab14, PKCiota protects claudin-2 from lysosomal degradation and, in consequence, modulates epithelial barrier.
Constitutive expression of BAG-1M decreased levels of phosphorylated aPKC.
aPKC regulates apical localization of Lgl1 and Lgl2 to restrict elongation of microridges in developing zebrafish epidermis.
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 junctional complex, especially aPKC, and both aPKC and Bves are indispensable to claudin expression.
These results suggest that the aPKC cell autonomously controls the Golgi localization and thereby regulates the specification of the primary dendrite of Purkinje cells.
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 findings suggest that miR-29c is a negative regulator of axonal growth of dorsal root ganglia neurons by targeting PRKCI under hyperglycemia.
PKClambda/iota emerges as a critical regulator of Th17 differentiation and allergic airway hyperresponsiveness.
This study demonstrated hat under physiological conditions, PKCiota/lambda is essential for hippocampal early-LTP and long-term memory.
the aPKC-CBP pathway is a homeostatic compensatory mechanism that modulates hippocampal neurogenesis and memory in an age-dependent manner in response to reduced CREB activity.
he oncogenic activity of PRKCI relates in part to the up-regulation of TNFalpha 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) neurons disrupts leptin action, reduces melanocortin content in the paraventricular nucleus, and markedly increases susceptibility to obesity, glucose intolerance, and insulin 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-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-lambda and atypical protein kinase C-zeta.
Loss of aPKClambda in differentiated neurons disrupts the polarity complex but does not induce obvious neuronal loss or disorientation in mouse brains.
Down-regulation of aPKC, involved in cell polarity, decreases the number of apical nuclei and doubles the number of asymmetric divisions.
Data demonstrate that PKCiota is required for a tumor-initiating cell phenotype in ovarian cancer.
PKClambda/iota was identified as an important factor for actin cytoskeletal regulation in podocytes and Def-6 as a specific downstream target of PKClambda/iota that regulates the activity of small GTPases and subsequently the actin cytoskeleton of podocytes.
Phosphatidylinositol-3,4,5-triphosphate but not phosphatidylinositol-4,5-biphosphate plays an important role in GLUT4 upregulation and glucose metabolism mediated by AKT/PKCzeta/lambda phosphorylation.
FGF21 inhibits hepatic glucose production by the PI3K-dependent activation of protein kinase c iota.
aPKClambda is critical for PDGF-induced actin cytoskeletal reorganization and cell migration.
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.
, atypical protein kinase C-lambda/iota
, protein kinase C iota type
, heart and soul protein
, protein kinase C, iota
, protein kinase C iota
, protein kinase C, lambda