Anti-phospho-eIF2Bε (pSer⁵³⁹) antibody produced in rabbit

synthetic phosphopeptide derived from the region of rat eIF2B containing serine 535, which corresponds to serine 539 in the human sequence. Detects human (69% homologous) and rat eIF2Bε.

Anti-phospho-eIF2Bε (pSer⁵³⁹) antibody produced in rabbit is suitable for western blotting at a dilution of 1:1,000 using recombinant eIF2Be treated with GSK-3β or CHO-T cells transfected with human insulin receptor.

Translation initiation factor eIF-2B subunit ε is a protein encoded by the EIF2B5 gene in humans. The eIF2B is composed of five subunits, α, β, γ, δ and ε, within which the ε subunit is responsible for catalyzing the guanine exchange reaction. Defect in any of these 5 subunits leads to diseases. Mutation in the subunit of eIF2B is associated with an autosomal recessive leukoencephalopathy called Vanishing white matter (VWM). eIF-2B is a heteromeric guanine nucleotide exchange factor that plays an important role in regulating mRNA translation. eIF2Bε has multiple phosphorylation sites in the largest catalytic subunit. Increased phosphorylation of eIF2ε by activation of GSK-3 is an important mechanism for the inhibition of skeletal muscle protein synthesis during sepsis.

Solution in Dulbecco′s phosphate buffered saline (without Mg²⁺ and Ca²⁺), pH 7.3, with 50% glycerol, 1.0 mg/mL BSA (IgG and protease free), and 0.05% sodium azide.

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