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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. Additionally we are shipping Protein Kinase D3 Proteins (7) and many more products for this protein.
Showing 10 out of 108 products:
Human Polyclonal PRKD3 Primary Antibody for IF, IHC (p) - ABIN359071
Yeaman, Ayala, Wright, Bard, Bossard, Ang, Maeda, Seufferlein, Mellman, Nelson, Malhotra: Protein kinase D regulates basolateral membrane protein exit from trans-Golgi network. in Nature cell biology 2004
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Human Polyclonal PRKD3 Primary Antibody for IF, IHC (p) - ABIN359072
Rey, Yuan, Young, Rozengurt: Protein kinase C nu/protein kinase D3 nuclear localization, catalytic activation, and intracellular redistribution in response to G protein-coupled receptor agonists. in The Journal of biological chemistry 2003
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Human Polyclonal PRKD3 Primary Antibody for IHC (p), WB - ABIN391014
Matthews, Dayalu, Thompson, Scharenberg: Regulation of protein kinase Cnu by the B-cell antigen receptor. in The Journal of biological chemistry 2003
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Human Polyclonal PRKD3 Primary Antibody for IHC (p), WB - ABIN658062
Ellwanger, Pfizenmaier, Lutz, Hausser: Expression patterns of protein kinase D 3 during mouse development. in BMC developmental biology 2008
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Human Monoclonal PRKD3 Primary Antibody for ELISA, WB - ABIN565151
Borges, Döppler, Perez, Andorfer, Sun, Anastasiadis, Thompson, Geiger, Storz: Pharmacologic reversion of epigenetic silencing of the PRKD1 promoter blocks breast tumor cell invasion and metastasis. in Breast cancer research : BCR 2014
Data show that similar to a knockdown of serine/threonine kinase (show TLK2 Antibodies) protein kinase D3 (PKD3), treatment with this inhibitor targets all tumorigenic processes in vitro and decreases growth of primary tumors and metastasis in vivo
Studies indicate that the loss of protein kinase D PKD1 is thought to promote invasion and metastasis, while PKD2 (show PKD2 Antibodies) and upregulated PKD3 to be positive regulators of proliferation.
Loss of PKD2 (show PKD2 Antibodies) enhanced KC proliferative potential while loss of PKD3 resulted in a progressive proliferation defect, loss of clonogenicity and diminished tissue regenerative ability.
for the first time, PKD3 is implicated in the transcription activation of latent HIV-1 provirus, and our results revealed a molecular mechanism of prostratin-induced HIV-1 transcription via PKCepsilon (show PRKCE Antibodies)/PKD3/NF-kappaB (show NFKB1 Antibodies) signaling pathway.
Activation of PKD2 (show PKD2 Antibodies) and further increase of PKD3 activity leads to additional phosphorylation and inhibition of endogenous phosphatase slingshot 1L (show SSH1 Antibodies).
PKD3 in TNBC cells provides a molecular connection between the Golgi and endolysosomal compartments to enhance proliferative mTORC1-S6K1 (show RPS6KB1 Antibodies) signaling.
PKD3 negatively regulates human airway epithelial barrier formation and integrity through down-regulation of claudin-1 (show CLDN7 Antibodies), which is a key component of tight junctions.
PKD3 may contribute to the malignant progression of prostate cancer cells through negative regulation of MMP-7 (show MMP7 Antibodies) expression.
PKD3 contributes to the proliferation and malignant growth of androgen-dependent prostate cancer cells in part by upregulating PSA (show PLAG1 Antibodies) expression.
these data suggest that PKD2 (show PKD2 Antibodies) and PKD3 coordinate to promote prostate cancer cell invasion through p65 NF-kappaB (show NFkBP65 Antibodies)- and HDAC1 (show HDAC1 Antibodies)-mediated expression and activation of uPA (show PRAP1 Antibodies).
Erythropoietin (show EPO Antibodies) regulates GATA1 (show GATA1 Antibodies) through protein kinase D (show PRKD1 Antibodies) activation, promoting histone deacetylase 5 (show HDAC5 Antibodies) dissociation from GATA1 (show GATA1 Antibodies), and subsequent GATA1 (show GATA1 Antibodies) acetylation.
These data validate PKD3 as a promising therapeutic target in prostate cancer and shed light on the role of secreted tumor-promoting factors in prostate cancer progression.
PKCnu is an important component of signaling pathways downstream from novel PKC enzymes after B-cell receptor engagement
the catalytic activity of PKD3 may regulate its nuclear import through autophosphorylation and/or interaction with another protein
PKD3 is increasingly expressed in neuronal as well as in the supporting connective tissue and in skeletal muscles
reveal a novel distinction between the exocrine and endocrine cells of the pancreas and further identify PKD3 as a signaling molecule that promotes hormone-stimulated amylase (show AMY Antibodies) secretion
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. This kinase can be activated rapidly by the agonists of G protein-coupled receptors. It resides in both cytoplasm and nucleus, and its nuclear accumulation is found to be dramatically enhanced in response to its activation. This kinase can also be activated after B-cell antigen receptor (BCR) engagement, which requires intact phopholipase C gamma and the involvement of other PKC family members.
protein kinase D3
, serine/threonine-protein kinase D3-like
, protein kinase C nu type
, protein kinase C, nu
, protein kinase EPK2
, protein-serine/threonine kinase
, serine/threonine-protein kinase D3