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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. Zusätzlich bieten wir Ihnen Protein Kinase D3 Antikörper (117) und viele weitere Produktgruppen zu diesem Protein an.
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None of the Polymorphous low-grade adenocarcinoma (PLGA) lacking PRKD1 (zeige PRKD1 Proteine) somatic mutations or PRKD gene family rearrangements harboured somatic mutations in the kinase domains of the PRKD2 (zeige PKD2 Proteine) or PRKD3 genes.
This study discovered and characterized a novel, highly conserved N-terminal domain, comprising 92 amino acids, which mediates dimerization of Protein Kinase D (PKD) isoforms, PKD1 (zeige PKD1 Proteine), PKD2 (zeige PKD2 Proteine), and PKD3 monomers.
Studies indicate that the loss of protein kinase D PKD1 is thought to promote invasion and metastasis, while PKD2 (zeige PKD2 Proteine) and upregulated PKD3 to be positive regulators of proliferation.
Loss of PKD2 (zeige PKD2 Proteine) 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 (zeige PRKCE Proteine)/PKD3/NF-kappaB (zeige NFKB1 Proteine) signaling pathway.
Activation of PKD2 (zeige PKD2 Proteine) and further increase of PKD3 activity leads to additional phosphorylation and inhibition of endogenous phosphatase slingshot 1L (zeige SSH1 Proteine).
PKD3 in TNBC cells provides a molecular connection between the Golgi and endolysosomal compartments to enhance proliferative mTORC1-S6K1 (zeige RPS6KB1 Proteine) signaling.
PKD3 negatively regulates human airway epithelial barrier formation and integrity through down-regulation of claudin-1 (zeige CLDN7 Proteine), 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 (zeige MMP7 Proteine) expression.
PKD3 contributes to the proliferation and malignant growth of androgen-dependent prostate cancer cells in part by upregulating PSA expression.
These data provide new insights of a specific PKD3 signaling pathway by identifying a new function, which has not been identified before.
Erythropoietin (zeige EPO Proteine) regulates GATA1 (zeige GATA1 Proteine) through protein kinase D (zeige PRKD1 Proteine) activation, promoting histone deacetylase 5 (zeige HDAC5 Proteine) dissociation from GATA1 (zeige GATA1 Proteine), and subsequent GATA1 (zeige GATA1 Proteine) 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 (zeige AMY Proteine) 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 C nu type
, protein kinase C, nu
, protein kinase EPK2
, protein-serine/threonine kinase
, serine/threonine-protein kinase D3
, protein kinase D3
, serine/threonine-protein kinase D3-like