An interferon-inducible, RNA-dependent protein serine/threonine kinase (PKR) has been described. PKR in earlier literature is variously known as DAI, dsJ, PI kinase, p65, p67 or TIK for the mouse kinase; and p68 or p69 for the human kinase. The PKR kinase substrate is the α subunit of protein synthesis initiation factor eIF-2. Phosphorylation of eIF-2α on serine-51 results in inhibition of translation. The serine/threonine kinase catalytic domains map to the carboxy terminal half of the protein while the RNA-binding domains are located in the amino terminal region. PERK is a type I transmembrane protein located in the endoplasmic reticulum that contains a kinase domain similar to the kinase domain of PKR. PERK is activated in response to ER stress and phosphorylates eIF-2α, thus inhibiting the translation of mRNA.
Clone
B5
Isotype
IgG1k
Host species
Mouse
Species Reactivity
Human, mouse, rat
Cellular Localization
cytoplasm
Positive Control
breast, colon carcinoma, stomach, kidney
Applications
IHC, ELISA, IF, IP, WB
Intended Use
Research Use Only
Research Use Only