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anti-Human PKC theta Antikörper:
anti-Mouse (Murine) PKC theta Antikörper:
anti-Rat (Rattus) PKC theta Antikörper:
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Human Polyclonal PKC theta Primary Antibody für IHC (p), ELISA - ABIN545471
Sun, Mao, Rao et al.: Association of CBFA2 mutation with decreased platelet PKC-theta and impaired receptor-mediated activation of GPIIb-IIIa and pleckstrin phosphorylation: proteins regulated by CBFA2 play a role in ... in Blood 2004
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Human Polyclonal PKC theta Primary Antibody für IHC - ABIN966842
Xu, Chaudhary, Olland, Wolfrom, Czerwinski, Malakian, Lin, Stahl, Joseph-McCarthy, Benander, Fitz, Greco, Somers, Mosyak: Catalytic domain crystal structure of protein kinase C-theta (PKCtheta). in The Journal of biological chemistry 2004
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Human Polyclonal PKC theta Primary Antibody für WB - ABIN6713928
Xu, Song, Gao, Xu, Xu, Xia, Dai: Paeoniflorin attenuates lipopolysaccharide-induced permeability of endothelial cells: involvements of F-actin expression and phosphorylations of PI3K/Akt and PKC. in Inflammation 2013
Human Monoclonal PKC theta Primary Antibody für ELISA, WB - ABIN533164
Kawakami, Kitaura, Yao, McHenry, Kawakami, Newton, Kang, Kato, Leitges, Rawlings, Kawakami: A Ras activation pathway dependent on Syk phosphorylation of protein kinase C. in Proceedings of the National Academy of Sciences of the United States of America 2003
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Human PKC theta Primary Antibody für IHC - ABIN966839
Bonny, Nicod, Waeber: IB1, a JIP-1-related nuclear protein present in insulin-secreting cells. in The Journal of biological chemistry 1998
Human Polyclonal PKC theta Primary Antibody für IF (p), IHC (p) - ABIN711746
van Rees, Lago, Cox, Tomasik, Rustogi, Weigelt, Ozcan, Cooper, Drexhage, Leweke, Bahn: Evidence of microglial activation following exposure to serum from first-onset drug-naïve schizophrenia patients. in Brain, behavior, and immunity 2017
Human Monoclonal PKC theta Primary Antibody für ICS - ABIN1176929
Parker, Murray-Rust: PKC at a glance. in Journal of cell science 2003
The results indicate that PKC could be the final target and an integrator molecule of different signaling pathways triggered by angiotensin II (Ang II), which could explain the sustained activation of Na(+)-ATPase by Ang II.
Phorbol 12-myristate 13-acetate activation of ERK and JNK signaling is relevant in the regulation of gene expression during follicular development, ovulation, and luteinization.
The Pro(168) residue in the C1a domain of full length PKCtheta; plays a critical role in the ligand and membrane binding, while exchanging the residue (Lys(240)) at the same position in C1b domain of full length PKCtheta; only modestly reduced the membrane interaction.
PKC-theta; is strongly and exclusively expressed in GISTs and interacts with intracellular mutant KIT to promote its stabilization by increased retention in the Golgi complex. PKC-theta; plays critical roles in the sustained activation of MT-KITs. Overexpression of PKC-theta; significantly correlates with several clinicopathological parameters
PCR and transcriptome analysis suggest that the genes CD3D and PKRCQ together can be used as a model for differentiating between B-cell and T-cell acute lymphoblastic leukemia.
PKC-theta; is a critical factor for type 2 innate lymphoid cells activation that contributes to TH2 cell differentiation, which is associated with IRF4 and NFAT1 expression in allergic lung inflammation.
Enhanced PRKCQ/PKCtheta; expression can promote growth-factor-independent growth, anoikis resistance, and migration. PRKCQ critically regulates growth and survival of a subset of TNBC.
Data suggest that, in T-lymphocytes, nitric oxide generated by eNOS S-nitrosylates Cys374 on ACTB and thus regulates activation/recruitment of PRKCQ at immune synapse; S-nitrosylation of beta-actin impairs actin binding to PFN1 and regulates protein transport in lamellipodia. (eNOS = nitric oxide synthase 3; ACTB = beta-actin; PRKCQ = protein kinase C-theta; PFN1 = profilin-1)
PKCtheta;-induced phosphorylations control the ability of Fra-1 to stimulate gene expression and breast cancer cell migration.
Within the nucleus, PKC-theta; catalytic activity maintains the Ser536 phosphorylation on the p65 subunit of NF-kappaB (also known as RelA) and can directly influence chromatin accessibility at transcriptional memory genes by regulating H2B deposition.
Data show that tonantzitlolone (TZL) was able to induce protein kinase c theta (PKCtheta;)-dependent heat shock transcription factor 1 (HSF1)phosphorylation.
The PRKCQ polymorphism is not associated with Behcet's Disease.
Sumoylation of PKC-theta; was essential for T cell activation. Desumoylation did not affect the catalytic activity of PKC-theta; but inhibited the association of CD28 with PKC-theta; and filamin A and impaired the assembly of a mature immunological synapse.
Together, these findings both in Jurkat T cells as well as in primary T cells indicate a regulatory role of Coro1A on PKCtheta; recruitment and function downstream of the TCR leading to NF-kappaB transactivation.
PKCtheta; acts through the activation of p38 MAPK and autophagy induction. PKCtheta; acts through the activation of p38 MAPK and autophagy induction to induce the Epstein-Barr virus (EBV) lytic cycle.
Data suggest that protein kinase C theta (PKCtheta;) inhibition alone may be sufficient to drive efficacy in chronic autoimmune and inflammatory diseases.
responsive to chemokine induced migration and are defective in migration to lymph nodes. Our results reveal a novel role for PKCtheta; in regulating T cell migration
protein kinase C-theta promotes Epithelial to mesenchymal transition by acting as a critical chromatin-anchored switch for inducible genes via transforming growth factor beta and the key inflammatory regulatory protein NF-kappaB.
Diacylglycerol activation of protein kinase Ctheta; and subsequent impairment of insulin signaling plays a major role in the pathogenesis of muscle insulin resistance in humans.
The results show that PKC-theta; has important diagnostic significance in gastrointestinal stromal tumors.
Results show that T allele of rs500766 in PRKCQ was associated with a reduced risk of ACE inhibitor-associated angioedema in the Nashville/Marshfield sample and ONTARGET.
This is the first study that shows that the activity of PKC-theta; is regulated by the intracellular redox state, and that PKC-theta; is recruited to the plasma membrane in an inactive form in naive T cells.
The authors established that OX40L/OX40 interaction was required and sufficient to induce regulatory T-cell proliferation in vivo independent of PKC- status. Although PKC- is dispensable for T-cell receptor-independent regulatory T-cell proliferation per se, it is essential for optimum IL-2 production by effector T-cells.
PKC-theta; is a regulator of lipid-induced insulin resistance in skeletal muscle.
Comparison with expanded cord blood-derived CD4(+)CD25(hi) tTreg and expanded Teffs from the same donors indicate that iTreg are intermediate between expanded CD4(+)CD25(hi) tTregs and Teffs, whereas modulation of suppressive activities by PKC-theta; and Dlgh1 signaling pathways are shared.
PKCtheta; selectively inactivates the negative regulator of F-actin generation, Coronin 1A, at the center of the T cell interface with the antigen presenting cell (APC). This allows for effective generation of the large actin-based lamellum required for recruitment of the Notch-processing membrane metalloproteinase ADAM10.
Results suggest that while PKCtheta; is involved in Treg cell differentiation in vivo, it is dispensable for Treg-mediated suppression.
Data show that pharmacological inhibition of Protein Kinase C theta (PKCtheta;) in Duchenne Muscular Dystrophy (DMD) can be considered an attractive strategy to modulate immune response and prevent the progression of the disease.
Knockdown of PKCtheta suppresses phosphorylation of IKK and JNK and consequently attenuates the HOCl-impaired insulin signaling pathway.
Data indicate that Protein kinase C theta; (PKCtheta;) is critical for stabilizing Th17 cell phenotype.
Data suggest that protein kinase Ctheta (PKCtheta;) inhibition alone is insufficient for complete efficacy in rodent arthritis model.
Inhibition of PKC-theta preserves cardiac function and reduces fibrosis in streptozotocin-induced diabetic cardiomyopathy
DTX1, similar to Cbl-b and Itch, participates in T cell anergy-induced PKC-theta degradation. there is a coupling of DTX1 to Cbl-b in T cell anergy.
Therefore, TCR ligation elicits a caspase cascade involving caspase-8, caspase-9 and caspase-3 which initiates PKC-theta;-dependent pathway leading to NF-kappaB activation.
PKCtheta regulates myogenic and protein synthetic signaling via the modulation of IRS1 and ERK1/ERK2 phosphorylation.
timed activation of PKCtheta;, phosphorylation of EKLF at S68 by P-PKCtheta;(S676), and sumoylation of EKLF at K74 occurs during the Pro-E to Baso-E transition
Our findings indicate that PKCalpha and theta; contribute to T-cell activation with overlapping functions essential for graft-vs-host disease
results demonstrate that PKCtheta; functions as an ER stress sensor in skeletal muscle, required for ER-stress-dependent autophagy activation, and can be proposed as a novel molecular target to maintain muscle homeostasis in response to external stimuli.
PKCtheta;/beta and CYLD are antagonistic partners in the NFkappaB and NFAT transactivation pathways in primary mouse CD3+ T lymphocytes.
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. The protein encoded by this gene is one of the PKC family members. It is a calcium-independent and phospholipid-dependent protein kinase. This kinase is important for T-cell activation. It is required for the activation of the transcription factors NF-kappaB and AP-1, and may link the T cell receptor (TCR) signaling complex to the activation of the transcription factors.
protein kinase C theta type
, PKC theta