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E7655
Anti-phospho-eIF2Bε (pSer539) antibody produced in rabbit
affinity isolated antibody, buffered aqueous glycerol solution
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About This Item
pochodzenie biologiczne
rabbit
Poziom jakości
białko sprzężone
unconjugated
forma przeciwciała
affinity isolated antibody
rodzaj przeciwciała
primary antibodies
klon
polyclonal
Formularz
buffered aqueous glycerol solution
masa cząsteczkowa
antigen 82 kDa
reaktywność gatunkowa
rat, human
metody
western blot: 1:1,000 using recombinant eIF2Bε treated with GSK-3β or CHO-T cells transfected with human insulin receptor.
numer dostępu UniProt
Warunki transportu
wet ice
temp. przechowywania
−20°C
informacje o genach
human ... EIF2B5(8893)
rat ... Eif2b5(192234)
Immunogen
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.
Zastosowanie
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.
Działania biochem./fizjol.
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.
Postać fizyczna
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.
Oświadczenie o zrzeczeniu się odpowiedzialności
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
Thomas C Vary et al.
American journal of physiology. Endocrinology and metabolism, 283(5), E1032-E1039 (2002-10-12)
We reported that the inhibition of protein synthesis in skeletal muscle during sepsis correlated with reduced eukaryotic initiation factor eIF2B activity. The present studies define changes in eIF2Bepsilon phosphorylation in gastrocnemius of septic animals. eIF2B kinase activity was significantly elevated
Xuerong Leng et al.
Journal of human genetics, 56(4), 300-305 (2011-02-11)
Vanishing white matter disease (VWM) is the first human hereditary disease known to be caused by defects in initiation of protein synthesis. Gene defects in each of the five subunits of eukaryotic translation initiation factor 2B (eIF2B α-ɛ) are responsible
Jia Wei et al.
Protein & cell, 1(6), 595-603 (2011-01-05)
Eukaryotic translation initiation factor eIF2B, the guanine nucleotide exchange factor (GEF) for eIF2, catalyzes conversion of eIF2·GDP to eIF2·GTP. The eIF2B is composed of five subunits, α, β, γ, δ and ɛ, within which the ɛ subunit is responsible for
H D W van der Lei et al.
Neurology, 75(17), 1555-1559 (2010-10-27)
Vanishing white matter (VWM) is an autosomal recessive leukoencephalopathy characterized by slowly progressive ataxia and spasticity with additional stress-provoked episodes of rapid and major deterioration. The disease is caused by mutations in the genes encoding the subunits of eukaryotic initiation
X Wang et al.
The EMBO journal, 20(16), 4349-4359 (2001-08-14)
Eukaryotic initiation factor (eIF) 2B is a heteromeric guanine nucleotide exchange factor that plays an important role in regulating mRNA translation. Here we identify multiple phosphorylation sites in the largest, catalytic, subunit (epsilon) of mammalian eIF2B. These sites are phosphorylated
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