Cat. # | Size | Qty. | Price |
---|---|---|---|
26168S | 1 Kit |
|
Product Includes | Quantity | Reactivity | MW(kDa) | Isotype | |
---|---|---|---|---|---|
Phospho-GCN2 (Thr899) (E1V9M) Rabbit mAb 94668 | 100 µl | H | 220 | Rabbit IgG | |
GCN2 (E7G7E) Rabbit mAb 65981 | 100 µl | H | 220 | Rabbit IgG |
Product Information
Phosphorylation of the eukaryotic initiation factor 2 (eIF2) alpha subunit is a well-documented mechanism of downregulating protein synthesis under a variety of stress conditions. Kinases activated by viral infection (PKR), endoplasmic reticulum stress (PERK/PEK), amino acid deprivation (GCN2), and hemin deficiency (HRI) can phosphorylate the eIF2 alpha subunit (1,2). GCN2 is also required for UV light-induced translation inhibition, and in vivo phosphorylation of murine GCN2 at Thr898 is induced by both UV irradiation and by leucine deprivation (3). UV-induced activation of NF-κB also requires GCN2, which may act simply by preventing translation of IκB-alpha to replace pools that have been ubiquitinated and degraded (4). Interestingly, proteasome inhibitors (MG132 and ALLN) activate the GCN2/eIF2alpha pathway, suggesting a pivotal role for this kinase in stress response and ubiquitin-mediated signaling (5). In vitro autophosphorylation of yeast GCN2 within its activation loop at Thr882 and Thr887 (Thr898 and Thr903 in mouse) has also been reported (6).
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