The atypical protein kinase C isoform, PKCzeta, has been implicated in the control of extracellular signal-regulated kinase (ERK) and nuclear factor (NF)-kappa B pathways. It has been shown that the loss of PKCzeta selectively impairs signaling through the B-cell receptor, resulting in inhibition of cell proliferation and survival, as well as defects in the activation of ERK and the transcription of NF-kappa B-dependent genes (1). The lack of PKCzeta in embryonic fibroblasts (EFs) severely impairs kappaB-dependent transcriptional activity as well as cytokine-induced phosphorylation of p65. Also, a cytokine-inducible interaction of PKCzeta with p65 was detected which requires the previous degradation of IkappaB (2). It has been found that persistent PKCzeta activity maintains potentiated responses, not only of the strongly tetanized pathway, but also of the weakly tetanized pathway. In contrast, an independent, nontetanized pathway was unaffected by the inhibitor, indicating that the function of PKCzeta was specific to the tagged synapses (3).
EGFR1 Signaling Pathway
MAPK signaling pathway
Wnt Signaling Pathway
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