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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.
Phosphorylated PKCalpha is elevated in epidermis genetically deleted of DLX3 (show DLX3 Proteins) and the hyperproliferative response to TPA (show PLAT Proteins) is increased, suggesting that the homeobox protein indirectly regulates the activity in the pathway, possibly through an effect on reduced phosphatase expression
Results show that PKCalpha expression is under the regulation of miR (show MLXIP Proteins)-142-3p contributing to reduced osteoclasts survival.
Molecular Determinants for the Binding Mode of Alkylphosphocholines in the C2 Domain of PKCalpha.
Studies suggest that rare deleterious variants of PARD3 (show PARD3 Proteins) in the aPKC-binding region contribute to human cranial neural tube defect (NTD).
study identified PKCalpha as hepatitis E virus HEV in host defense
ADP inhibits mesothelioma cell proliferation via PKC-alpha/ERK (show EPHB2 Proteins)/p53 (show TP53 Proteins) signaling.
This study provides evidences of a new PKCalpha/GAP-43 (show GAP43 Proteins) nuclear signalling pathway that controls neuronal differentiation in Human Periodontal Ligament Stem Cells.
protein kinase (show CDK7 Proteins) Calpha (show PRKACA Proteins) (PKCalpha) gain of function mutations may promote synaptic defects in Alzheimer's disease
Some polyphenols exert their antioxidant properties by regulating the transcription of the antioxidant enzyme genes through PKC signaling. Regulation of PKC by polyphenols is isoform dependent
Data suggest that phosphorylation activity of PRKCA stems from conformational flexibility in region C-terminal to phosphorylated Ser (show SIGLEC1 Proteins)/Thr (show TRH Proteins) residues; flexibility of substrate-kinase interaction enables an Arg/Lys (show LYZ Proteins) two to three amino acids C-terminal to phosphorylated Ser (show SIGLEC1 Proteins)/Thr (show TRH Proteins) to prime a catalytically active conformation, facilitating phosphoryl transfer to substrate.
However, the mechanism that induces release of IL-6 (show IL6 Proteins) from skeletal muscle cells remains unknown. Here we show that heat increases IL-6 (show IL6 Proteins) in skeletal muscle cells through the transient receptor potential vannilloid 1, PKC, and cAMP response element-binding protein signal transduction pathway.
Erk5 MAP kinase is activated in response to PDGF-BB in the smooth muscle cell line MOVAS in a manner dependent on Mekk2, Mek1/2, Mek5, PI3-kinase and protein kinase C (PKC).
PKC-alpha plays a crucial role in the pathophysiology of peritoneal membrane dysfunction induced by peritoneal dialysis fluids, and its therapeutic inhibition might be a valuable treatment option for peritoneal dialysis patients.
these results identify PKCalpha and HMGB1 as important co-regulators involved in hydrogen peroxide-induced poly-ADP-ribose formation.
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.
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