PKC? (human, recombinant)

PKC? (human, recombinant)

CAT N°: 32563
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PKC? is an ?-type conventional isoform of the PKC family of serine/threonine protein kinases, which includes the conventional isoforms PKC?, -?, and -?, the novel isoforms PKC?, -?, -?, and -?, and the atypical isoforms PKC? and -?/?.{54650} PKC? is composed of an N-terminal regulatory domain containing a pseudosubstrate binding site, a C1 domain that binds the cofactor diacylglycerol (DAG), a C2 domain that binds the cofactor calcium, and a C-terminal domain containing an ATP-binding domain, substrate binding site, and catalytic domain. PKC? is ubiquitously expressed and localized to the cytoplasm in an auto-inhibited conformation until activated by calcium and DAG, which are both required for activation of the conventional PKC isoforms.{54650,54651} Activation of PKC? occurs via an allosteric and temporal mechanism during which it is translocated primarily to the plasma membrane where it phosphorylates a wide variety of substrates.{54650} PKC? is involved in the regulation of cell survival with anti- or pro-apoptotic effects and an increase or decrease in cell proliferation depending on the cellular context and cell type. It is also involved in cell differentiation and motility.{54651} Protein levels of PKC? are either increased or decreased in cancer cells, indicating a complex role in oncogenesis.{54652} Tumor levels of PKC? correlate positively to tumor grade and negatively to survival in patients with breast cancer.{54653} A SNP in PRKCA, which encodes PKC?, is associated with an increased risk of post-traumatic stress disorder (PTSD) in survivors of genocide.{54654} Cayman’s PKC? (human, recombinant) protein can be used for enzyme assay applications. This protein consists of 672 amino acids and has a calculated molecular weight of 102 kDa.

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