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apically localized serine/threonine kinase aPKC directly phosphorylates an N-terminal site of the cell-cycle inhibitor p27Xic1 and reduces its ability to inhibit the cyclin-dependent kinase 2 (show CDK2 Proteins), leading to shortening of G1 and S phases
Neural induction by Syn4 (show SNTG1 Proteins) through the PKC pathway requires inhibition of PKCdelta (show PKCd Proteins) and activation of PKCalpha.
The depletion of membrane PIP(2) underlies receptor-mediated inhibition of IKs and that phosphorylation by PKC of the KCNE1 (show KCNE1 Proteins) subunit underlies the GqPCR-mediated channel activation.
Our data demonstrate isoform-specific regulation of closed-state inactivation by protein kinase C in Kv4.3 (show KCND3 Proteins)
Data show that PKC staining colocalizes with monkey retina expresses a retina-specific slice variant of PCP2.
Protein kinase C enhances the swelling-induced chloride current in human atrial myocytes.
these results confirm the correlation between AXL (show AXL Proteins) and PKCalpha, and suggest PKCalpha-AXL (show AXL Proteins) signaling may be a treatment target, particularly in malignant cancer cells.
After inhibition of the PKC/ERK signalling pathway, the effects of DOR on breast cancer were significantly attenuated in vivo and in vitro. In summary, DOR is highly expressed in breast cancer and is closely related to its progression. These results suggest that DOR may serve as a potential biomarker for the early diagnosis of breast cancer and may be a viable molecular target for therapeutic intervention.
authors found significant interactions among PRKCA, NOS3 (show NANOS3 Proteins) and BDKRB2 (show BDKRB2 Proteins) genotypes associated with enalapril responses.
Protein kinase C alpha (PKCalpha) is able to phosphorylate CK1delta at its C-terminally located residues S328, T329, and S370.
PKCalpha activity was effectively suppressed by the PKC inhibitor.
this study shows that the mTOR inhibitors suppression of invasion and migration of glioblastoma cells is mediated by reduction of PKC-alpha activity and downregulation of NFkappaB
PKCalpha controls HIF-1alpha (show HIF1A Proteins) translation via AKT (show AKT1 Proteins)-mTOR (show FRAP1 Proteins) under hypoxic conditions.
Our results provide compelling evidence that glucose-induced PKCalpha/PKCbeta-mediated inhibition of Kv current in vascular smooth muscle causes an enhanced constrictor response. Inhibition of Kv current causes a significant depolarization of vascular myocytes leading to marked vasoconstriction
Data suggest that targeted manipulation of protein kinase C isoforms PKCalpha, PKCbeta, and PKCeta might be beneficial in certain proteinuric kidney diseases with altered transient receptor potential cation channel subfamily C member 6 (show TRPC6 Proteins) protein (TRPC6 (show TRPC6 Proteins)) functions.
the present study demonstrates that nNOS-derived NO signaling modulated by spinal Sig-1R activation increases Nox2 activity and concomitant ROS production, which leads to a ROS-induced increase in PKC-dependent pGluN1 expression in the spinal cord dorsal horn and the development of pain hypersensitivity
We conclude that synaptotagmin-1 (show SYT1 Proteins) phosphorylation is an essential step in PKC-dependent potentiation of synaptic transmission, acting downstream of the two other essential DAG/PKC substrates, Munc13-1 and Munc18-1 (show STXBP1 Proteins).
These data indicate that LPA increases CCN2 (show CTGF Proteins) expression through the activation of PKC and PKA. Thus, the regulatory functions of the PKC and PKA pathways are implicated in the LPA-induced increase in CCN2 (show CTGF Proteins) expression
Kinocilium is essential for proper localization of Lgn, as well as Gai and aPKC, suggesting that cilium function plays a role in positioning of apical proteins critical for hearing.
We conclude that melatonin, via modulation of PKC and Ca(2 (show CA2 Proteins)+) signaling, could potentially stimulate the Nrf2 (show NFE2L2 Proteins)-mediated antioxidant response in mouse pancreatic acinar cells.
PKCalpha deficiency leads to pulmonary vascular hyperresponsiveness to TXA2 (show TBXA2R Proteins), possibly via increased pulmonary arterial TP receptor (show TBXA2R Proteins) expression.
at the functionally mature calyx of Held synapse the Ca(2+)-dependent protein kinase C isoforms alpha and beta are necessary for post-tetanic potentiation, a form of plasticity thought to underlie short-term memory
PKC gene deletion is responsible for hair loss.
The overall result suggests the cancer preventive activity of quercetin via the induction of apoptosis and modulates PKC signaling with the reduction of oxidative stress in ascite cells of lymphoma-bearing mice.
the ANG II (show AGT Proteins)-dependent upregulation of renin (show REN Proteins) in the collecting duct depends on PKC-alpha, which allows the augmentation of cAMP production and activation of PKA/CREB (show CREB1 Proteins) pathway
PKC activation can enhance hippocampal neurotransmitter release, depending on changes specific to mGluR5 (show GRM5 Proteins) and AMPA (show GRIA3 Proteins)/kainate receptors.
Isoenzymes beta and delta of PKC have been found significantly phosphorylated, although their location was not changed as a consequence of Trichinella spiralis infection.
AngII activates PKD via a mechanism involving Src family kinases and PKC, to underlie increased aldosterone production.
Significant changes in thin filament Ca2 (show CA2 Proteins)+-sensitivity, structure and kinetics are brought about through PKC phosphorylation of cardiac troponin T (show TNNT2 Proteins).
Data indicate the involvement of PKC-alpha in proMMP-2 activation and inhibition of TIMP-2 (show TIMP2 Proteins) expression by NF-kappaB (show NFKB1 Proteins)-MT1-MMP (show MMP14 Proteins)-dependent and -independent pathway.
calcium-dependent phosphorylation of argininosuccinate synthase (show ASS1 Proteins) Ser (show SIGLEC1 Proteins)-328 is mediated by PKCalpha
VDAC phosphorylation is an important determinant of its interaction with dimeric tubulin (show TUBB Proteins).
Using yeast cells co-expressing the human wild-type p53 and a single mammalian PKCalpha, delta, epsilon or zeta, results showed a differential regulation of p53-mediated apoptosis by these PKC isoforms.
degradation of protein kinase C(alpha)in sperm capacitation is mediated by PRKA
Data suggest that ceramide interacts with the calcium-dependent lipid binding C2 domain of protein kinase C alpha and thereby induces translocation of the enzyme to the Golgi compartment.
analysis of amino acid critical for the catalytic competence and function of protein kinase (show CDK7 Proteins) Calpha (show PRKACA Proteins)
By regulating VEGFR2 (show KDR Proteins) expression and activation, PKC-epsilon (show PRKCE Proteins) expression is critical for activation of Akt (show AKT1 Proteins) and eNOS (show NOS3 Proteins) by VEGF (show VEGFA Proteins) and contributes to VEGF (show VEGFA Proteins)-stimulated Erk (show MAPK1 Proteins) activation, whereas PKC-alpha has opposite effects.
We conclude that ouabain, even at low concentrations (0.5-8.0 mum), can increase INaL and reverse INCX , and these effects may contribute to the effect of the glycoside to increase Ca(2 (show CA2 Proteins)+) transients and contractility.
These results suggest a complex antagonistic interplay between G(q)-activated PKC and Gbetagamma in regulation of L-VDCC, in which multiple cytosolic segments of alpha(1C) are involved.
Protein kinase C alpha (PKCalpha) regulates growth and invasion of endometrial cancer cells.
This study examined the protein expression and spatial-temporal distribution of PKCalpha and CPI-17 (show PPP1R14A Proteins) in intact smooth muscle tissues.
Results suggest that the action of genistein on protein kinase A is mediated via adenylate cyclase, but does not appear to involve Gs protein or ICI 182780-sensitive estrogen receptor (show ESR1 Proteins).
The PKCalpha, PKCbeta1, and PKCbeta2 mRNA levels tended to be lower in ischemia-reperfused than in sham-operated eyes in both the retinal arteries and the neuroretina.
protein level of retinal PKC-alpha is increased with maturation
Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and the second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. The protein encoded by this gene is one of the PKC family members. This kinase has been reported to play roles in many different cellular processes, such as cell adhesion, cell transformation, cell cycle checkpoint, and cell volume control. Knockout studies in mice suggest that this kinase may be a fundamental regulator of cardiac contractility and Ca(2+) handling in myocytes.
, protein kinase C alpha type
, protein kinase C, alpha
, protein kinase C alpha type-like
, aging-associated gene 6
, protein kinase c-alpha
, protein kinase, C alpha
, protein kinase C alpha