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None of the Polymorphous low-grade adenocarcinoma (PLGA) lacking PRKD1 (show PRKD1 ELISA Kits) somatic mutations or PRKD gene family rearrangements harboured somatic mutations in the kinase domains of the PRKD2 or PRKD3 (show PRKD3 ELISA Kits) 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 (show PKD1 ELISA Kits), PKD2, and PKD3 (show PRKD3 ELISA Kits) monomers.
Studies indicate that the loss of protein kinase D PKD1 is thought to promote invasion and metastasis, while PKD2 and upregulated PKD3 (show PRKD3 ELISA Kits) to be positive regulators of proliferation.
the knockdown of PKD2 reduces cell death and promotes polyploidization induced by PMA. PMA/PKD2-mediated necrosis via PARP (show COL11A2 ELISA Kits) cleavage involves both SOD1 (show SOD1 ELISA Kits)-dependent and -independent pathways.
The results implied that PKD2 silencing might inhibit migration of MCF7/DOX cells without affecting chemoresistance significantly
PRKD2 silencing induces glioma cell senescence via p53 (show TP53 ELISA Kits)-dependent and -independent pathways.
Loss of PKD2 enhanced KC proliferative potential while loss of PKD3 (show PRKD3 ELISA Kits) resulted in a progressive proliferation defect, loss of clonogenicity and diminished tissue regenerative ability.
Activation of PKD2 and further increase of PKD3 (show PRKD3 ELISA Kits) activity leads to additional phosphorylation and inhibition of endogenous phosphatase slingshot 1L (show SSH1 ELISA Kits).
Both PKD2 and GOLPH3 (show GOLPH3 ELISA Kits) play important roles in the progression of human gliomas by promoting cell proliferation.
PKD2 controls secretion of MMP7 (show MMP7 ELISA Kits) and 9 in an isoform-specific manner
Our studies demonstrate that PKD1 (show PKD1 ELISA Kits)/2 is a key regulator of MVB maturation and exosome secretion, and constitutes a mediator of the DGK alpha (show DGKA ELISA Kits) effect on MVB secretory traffic.
Results reveal that whereas protein kinase D1 (show PRKD1 ELISA Kits) and protein kinase D2 are essential for neuronal polarity, there exists a functional redundancy between the two proteins.
PKD2 acted as an amplification checkpoint for antigen-stimulated digital cytokine responses and translated the differential strength of TCR signaling to determine the number of naive CD8 (show CD8A ELISA Kits)(+) T cells that became effector cells.
Protein kinase D2 promotes in vitro osteoclast differentiation and fusion
A bioinformatic screen identified the serine-threonine kinase (show CDK4 ELISA Kits) protein kinase D2 (PRKD2) as a potential effector of GABP in hematopoietic stem cells
Transcriptional profiling reveals the full consequences of PKD2 loss and maps in detail the selective, but critical, function for PKD2 in signalling by alpha/beta mature TCR complexes in peripheral T-cells.
PKD2 is a common signaling target downstream of various agonist receptors in platelets and G(q)-mediated signals along with calcium and novel PKC (show PKC ELISA Kits) isoforms, in particular, PKCdelta (show PKCd ELISA Kits) activate PKD2 in platelets.
Data demonstrate that, unlike PKD1 (show PKD1 ELISA Kits), PKD2 catalytic activity is dispensable for normal embryogenesis.
PKD2, like PKD (show PRKD1 ELISA Kits), facilitates mitogenesis in 3T3 cells
The protein encoded by this gene belongs to the protein kinase D (PKD) family of serine/threonine protein kinases. This kinase can be activated by phorbol esters as well as by gastrin via the cholecystokinin B receptor (CCKBR) in gastric cancer cells. It can bind to diacylglycerol (DAG) in the trans-Golgi network (TGN) and may regulate basolateral membrane protein exit from TGN. Alternative splicing results in multiple transcript variants encoding different isoforms.
serine/threonine-protein kinase D2
, protein kinase D2
, serine/threonine-protein kinase D2-like