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EIF2A antibody review
EIF2A antibodies
This is a review about EIF2A antibodies, based on 5 published articles using EIF2A antibodies in western blot, immunohistochemistry, immunoprecipitation, immunocytochemistry, and other immunological technologies. It is aimed to help ExactAntigen visitors find the most suited EIF2A antibody. Information in this review (with links to publications) can be searched freely.
CELL SIGNALING TECHNOLOGY    search Cell Signaling Technology EIF2A products
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wb    Cell Signaling Technology rabbit polyclonal anti-eIF2alpha antibody was used in human fibrosarcoma HT1080 cells and in western blot to study the role for tyrosine phosphorylation in full-scale activation of the eIF2alpha RNA-dependent protein kinase.
wb    Cell Signaling Technology antibody against eukaryotic initiation factor 2a (eIF2a) was used in western blot to study the interaction of ADAR1 with NF90 through double-stranded RNA and its regulation on NF90-mediated gene expression, independent of RNA editing.
wb    Cell Signaling Technology rabbit polyclonal antibody against the phospho-eIF2 (anti-Pser51) and rabbit polyclonal antibody recognizing both phosphorylated and unphosphorylated eIF2a were used in western blot to study the phosphorylation of eIF2a.
SANTA CRUZ BIOTECHNOLOGY    search Santa Cruz Biotechnology EIF2A products
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wb    Santa Cruz Biotechnology Inc. polyclonal anti-eIF2α antibody was used in western blot to study the effect of inhibitor-1 C terminus on hormonal regulation of cellular protein phosphatase-1.
wb    Santa Cruz polyclonal anti-eIF2a antibody was used in western blot to study the role of PACT in the activation of double-stranded-RNA-dependent protein kinase (PKR).
INVITROGEN    search Invitrogen EIF2A products
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wb    BIOSOURCE anti-phospho-Ser51 eIF2α antibody was used in western blot to study the effect of inhibitor-1 C terminus on hormonal regulation of cellular protein phosphatase-1.


Articles Reviewed
1. Xu Huang et al. The C-terminal, third conserved motif of the protein activator PACT plays an essential role in the activation of double-stranded-RNA-dependent protein kinase (PKR). 2002
2. Constantinos Koumenis et al. Regulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase PERK and phosphorylation of the translation initiation factor eIF2alpha. 2002
3. Douglas C Weiser et al. The inhibitor-1 C terminus facilitates hormonal regulation of cellular protein phosphatase-1: functional implications for inhibitor-1 isoforms. 2004
4. Yongzhan Nie et al. ADAR1 interacts with NF90 through double-stranded RNA and regulates NF90-mediated gene expression independently of RNA editing. 2005
5. Qiaozhu Su et al. Tyrosine phosphorylation acts as a molecular switch to full-scale activation of the eIF2alpha RNA-dependent protein kinase. 2006


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