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ADP inhibits mesothelioma cell proliferation via PKC-delta/JNK (show MAPK8 Proteins)/p21 (show CDKN1A Proteins)/p27 (show PAK2 Proteins) signaling.
PKCdelta, via MAPK (show MAPK1 Proteins) pathway, is involved in the glycodelin (show PAEP Proteins)-driven cell differentiation.
PKCdelta is a critical regulator of signaling mechanisms of neutrophil-endothelium interaction in acute inflammation. Inhibition of PKCdelta in human endothelial cells and neutrophils reduced chemoattractant-induced neutrophil migration across TNF-alpha (show TNF Proteins)-activated endothelium, and reduced expression of E-selectin (show SELE Proteins) and ICAM-1 (show ICAM1 Proteins). Shear rate and vascular geometry regulate the impact of PKCdelta inhibition of neutrophil-endot...
Lysophosphatidylcholines prime polymorphonuclear neutrophil through Hck (show HCK Proteins)-dependent activation of PKCdelta, which stimulates PKCgamma (show PRKCG Proteins), resulting in translocation of phosphorylated p47(phox).
The interplay between intracellular progesterone receptor (show PGR Proteins) and PRKCA (show PKCa Proteins)-PRKCD plays a key role in migration and invasion of human glioblastoma cells.
Amphiregulin (show AREG Proteins) enhances VEGF-A (show VEGFA Proteins) production in human chondrosarcoma cells and promotes angiogenesis by inhibiting miR (show MLXIP Proteins)-206 via FAK (show PTK2 Proteins)/c-Src (show SRC Proteins)/PKCdelta pathway.
In the present investigation, we demonstrated that miR486 is negatively associated with the expression of PKC-delta and could regulate the development of osteosarcoma. miR (show MLXIP Proteins)-486 may be a potential target for the treatment of osteosarcoma
PKCdelta and PKCepsilon (show PRKCE Proteins) work as a functional couple with opposite roles on thrombopoiesis, and the modulation of their balance strongly impacts platelet production.
These findings suggest that targeting Wnt (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) or Akt (show AKT1 Proteins) pathways may increase the efficacy of taxane chemotherapy in advanced human prostate cancers that have lost PKCdelta expression.
description of a rare monogenic form of juvenile systemic lupus erythematosus caused by a novel but damaging homozygous mutation affecting the active region of PRKCD.
HIF1a (show HIF1A Proteins) transcriptional activity is stimulated by Protein kinase A-dependent phosphorylation
Generation of the Dnajb1 (show DNAJB1 Proteins)-Prkaca (show PRKACA Proteins) fusion gene in wild-type mice to be sufficient to initiate formation of tumors that have many features of human fibrolamellar hepatocellular carcinonma.
Data indicate a subpopulation of the CaV1.2 (show CACNA1C Proteins) channel pore-forming subunit (alpha1C) within nanometer proximity of protein kinase A (PKA) at the sarcolemma of murine and human arterial myocytes.
S1928A KI mice failed to induce long-term potentiation in response to prolonged theta-tetanus (PTT-LTP (show SCP2 Proteins)), a form of synaptic plasticity that requires Cav1.2 (show CACNA1C Proteins) and enhancement of its activity by the beta2-adrenergic receptor (show ADRB2 Proteins) (beta2AR (show ADRB2 Proteins))-cAMP-PKA cascade.
Data show that laminin alpha2beta1gamma1 (Lm211) can inhibit neuregulin 1 (show NRG1 Proteins) type III (Nrg1III) by limiting protein kinase A (PKA) activation, which is required to initiate myelination.
spinal PKCdelta has a role in the development of chronic pain in SCD (show SCD Proteins), which may become a potential target for pharmacological interventions
study identifies a new role of Dual-AKAP1 (show AKAP1 Proteins) in regulating mitochondrial trafficking through Miro-2 (show RHOT2 Proteins), and supports a model in which PINK1 (show PINK1 Proteins) and mitochondrial PKA participate in a similar neuroprotective signaling pathway to maintain dendrite connectivity
Data suggest that enzyme activation by cAMP involves highly stable conformation of Prkar1a as it binds to Prkaca; glycine residue, G235, appears to function as hinge in B/C helix conserved in Prkar1a; this "Flipback" conformation plays role in cAMP association to A domain of Prkar1a. (Prkar1a = cyclic AMP-dependent protein kinase RIalpha subunit; Prkaca = cyclic AMP-dependent protein kinase catalytic subunit)
K8/K18 (show KRT18 Proteins)-dependent PKCdelta- and ASMase (show SMPD1 Proteins)-mediated modulation of lipid raft size can explain the more prominent FasR-mediated signaling resulting from K8/K18 (show KRT18 Proteins) loss.
MALAT1 recruits splice factor serine-arginine-rich splice factor 2 (SRSF2 (show SRSF2 Proteins)) to promote alternative splicing of PKCdeltaII.
Report PRKCD-dependent regulation of bovine embryonic development, gene expression and post-hatching events.
investigation of signaling mechanism used by fibroblast growth factor-2 (FGF2 (show FGF2 Proteins)) to regulate interferon-tau (IFNT) production in trophoblasts: several lines of evidence suggest that FGF2 (show FGF2 Proteins) regulates IFNT production in trophoblasts by acting through PRKCD
deltaPKC inhibition or varepsilonPKC activation repairs endothelial vascular dysfunction by regulating eNOS (show NOS3 Proteins) post-translational modification
stimulation of bovine theca cells with lysophosphatidic acid leads to redistribution of protein kinase C delta from the cytosol to the perinuclear area and in the presence of LH, complete nuclear translocation of protein kinase C delta is induced
Protein kinase (show CDK7 Proteins) Cdelta-dependent phosphorylation of syndecan-4 (show SDC4 Proteins) regulates cell migration.
Activation of PKC induces the translocation of Nrf2 (show NFE2L2 Proteins) and the enhancement of endogenous antioxidant defenses in ischemic preconditioned rabbit heart.
PKC-delta (show PRKCG Proteins) mediates the apoptotic processes through ROS (show ROS1 Proteins)-dependent caspase-3 (show CASP3 Proteins) activation
Here, substitution studies on peptides correlating to the C1B domain in PKC gamma (show PRKCG Proteins) show that a flexible structure and ability to be phosphorylated on serine 109 are critical for this purpose.
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 distinct roles in cells. The protein encoded by this gene is one of the PKC family members. Studies both in human and mice demonstrate that this kinase is involved in B cell signaling and in the regulation of growth, apoptosis, and differentiation of a variety of cell types. Alternatively spliced transcript variants encoding the same protein have been observed.
protein kinase C delta VIII
, protein kinase C delta type
, tyrosine-protein kinase PRKCD
, protein kinase C delta variant IX
, protein kinase C, delta IV
, protein kinase C, delta V
, protein kinase C[d]
, protein kinase-delta2
, protein kinase C, delta
, protein kinase C delta type-like
, PKA C-alpha
, cAMP-dependent protein kinase catalytic subunit alpha
, sperm cAMP-dependent protein kinase catalytic subunit
, protein kinase C delta
, protein kinase C gamma type