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Santa Cruz Biotechnology
eif2bα  Eif2bα, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more https://www.bioz.com/product/eif2b%CE%B1/eIF2B%CE%B1+Antibody/pmc07360930-156-31-33 Average 91 stars, based on 1 article reviews
eif2bα - by Bioz Stars,
2026-09
91/100 stars
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GenScript corporation
nucleotide sequence of eif2bα  Nucleotide Sequence Of Eif2bα, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more https://www.bioz.com/product/eif2b%CE%B1/nucleotide+sequence+of+eif2b%CE%B1/pmc08187479-248-4-11 Average 90 stars, based on 1 article reviews
nucleotide sequence of eif2bα - by Bioz Stars,
2026-09
90/100 stars
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CRISPR/Cas9 KO Plasmids consists of eIF2Bα-specific 20 nt guide RNA sequences derived from the GeCKO (v2) library. For CRISPR gene knockout, gRNA sequences direct the Cas9 protein to induce a site-specific double strand break (DSB)
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Gene Silencers generally consist of pools of three to five target-specific 19-25 nucleotide sequences in length. For independent verification of eIF2Bα gene silencing results, individual duplex components or plasmids are also available upon request.
|
Buy from Supplier |
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CRISPR/Cas9 KO Plasmids consists of eIF2Bα-specific 20 nt guide RNA sequences derived from the GeCKO (v2) library. For CRISPR gene knockout, gRNA sequences direct the Cas9 protein to induce a site-specific double strand break (DSB)
|
Buy from Supplier |
|
Gene Silencers generally consist of pools of three to five target-specific 19-25 nucleotide sequences in length. For independent verification of eIF2Bα gene silencing results, individual duplex components or plasmids are also available upon request. Suitable
|
Buy from Supplier |
|
CRISPR/Cas9 KO Plasmids consists of eIF2Bα-specific 20 nt guide RNA sequences derived from the GeCKO (v2) library. For CRISPR gene knockout, gRNA sequences direct the Cas9 protein to induce a site-specific double strand break (DSB)
|
Buy from Supplier |
|
Gene Silencers generally consist of pools of three to five target-specific 19-25 nucleotide sequences in length. For independent verification of eIF2Bα gene silencing results, individual duplex components or plasmids are also available upon request. Suitable
|
Buy from Supplier |
|
Gene Silencers generally consist of pools of three to five target-specific 19-25 nucleotide sequences in length. For independent verification of eIF2Bα gene silencing results, individual duplex components or plasmids are also available upon request. Suitable
|
Buy from Supplier |
|
Gene Silencers generally consist of pools of three to five target-specific 19-25 nucleotide sequences in length. For independent verification of eIF2Bα gene silencing results, individual duplex components or plasmids are also available upon request.
|
Buy from Supplier |
|
Gene Silencers generally consist of pools of three to five target-specific 19-25 nucleotide sequences in length. For independent verification of eIF2Bα gene silencing results, individual duplex components or plasmids are also available upon request. Suitable
|
Buy from Supplier |
|
CRISPR/Cas9 KO Plasmids consists of eIF2Bα-specific 20 nt guide RNA sequences derived from the GeCKO (v2) library. For CRISPR gene knockout, gRNA sequences direct the Cas9 protein to induce a site-specific double strand break (DSB)
|
Buy from Supplier |
Image Search Results
Journal: mBio
Article Title: eIF2B as a Target for Viral Evasion of PKR-Mediated Translation Inhibition
doi: 10.1128/mBio.00976-20
Figure Lengend Snippet: Interaction of SFSV NSs with the eIF2B complex. Coimmunoprecipitation experiments. HEK293 cells were transiently transfected with expression plasmids for all eIF2B subunits as well as 3×FLAG-tagged SFSV NSs variants or the unrelated control 3×FLAG-ΔMx. Proteins in the cell lysates were precipitated via specific tags and analyzed by immunoblotting with the indicated antibodies. (a) Overexpression of eIF2B subunits along with C-terminally 3×FLAG-tagged NSs (SFSV NSs-3×FLAG). Immunoprecipitation was performed with anti-FLAG antibody. (b) mCitrine-HA-tagged eIF2Bε (eIF2Bε-mCitrine-HA) was expressed along with eIF2B subunits α, β, γ, and δ as well as SFSV NSs-3×FLAG. Untagged eIF2Bε served as control for unspecific binding. The eIF2B complex was precipitated using an mCitrine-binding matrix. (c) Overexpression of untagged eIF2B subunits along with C- or N-terminally 3×FLAG-tagged NSs (SFSV NSs-3×FLAG and 3×FLAG-NSs SFSV, respectively). Immunoprecipitation was performed with anti-FLAG antibody. (d) Immunoprecipitated proteins from the experiment shown in panel c after prolonged exposure. Shown data are representatives of 3 (a, c, and d) or 5 (b) experiments. *, light chain of the IP antibody.
Article Snippet: Primary antibodies were used as follows: β-actin (1:1,000, number [no.] 3700; Cell Signaling); eIF2α (1:1,000, no. 2103; Cell Signaling); phospho (p)-eIF2α (1:500, no. 3597 [Cell Signaling] and 1:1,000, no. 44728G [Invitrogen]);
Techniques: Transfection, Expressing, Control, Western Blot, Over Expression, Immunoprecipitation, Binding Assay
Journal: mBio
Article Title: eIF2B as a Target for Viral Evasion of PKR-Mediated Translation Inhibition
doi: 10.1128/mBio.00976-20
Figure Lengend Snippet: SFSV NSs and established mechanisms of eIF2B regulation. (a and b) Monitoring expression levels of eIF2B subunits in the presence of NSs. A549 cells were either infected with the indicated recombinant viruses (MOI, 1) and lysed 16 hpi (a) or infected with parental viruses SFSV, RVFV MP12, and Cl13 (MOI, 1) and lysed 12 hpi (b) and analyzed by immunoblotting. Staining of viral N proteins served as marker for infection. *, leftover SFSV N signal, for which the blot was probed before detecting eIF2B beta. (c) Monitoring eIF2B decamer formation. HEK293 cells were infected with SFSV or NSs-deficient RVFV strain rRVFVΔNSs::Katushka (rRVFVΔNSs::Kat) or treated with ISRIB. rRVFVΔNSs::Kat served as negative control for infection-induced but NSs-independent effects on eIF2B stoichiometry, whereas ISRIB was included as positive control for eIF2B decamerization. Cell lysates were fractionated via 5% to 20% sucrose gradients, and fractions were analyzed for a shift of eIF2B subunits toward fractions of higher density by immunoblotting. Shown data are representatives of 2 (a) or 3 (b and c) experiments.
Article Snippet: Primary antibodies were used as follows: β-actin (1:1,000, number [no.] 3700; Cell Signaling); eIF2α (1:1,000, no. 2103; Cell Signaling); phospho (p)-eIF2α (1:500, no. 3597 [Cell Signaling] and 1:1,000, no. 44728G [Invitrogen]);
Techniques: Expressing, Infection, Recombinant, Western Blot, Staining, Marker, Negative Control, Positive Control
Fig. S5 in the supplemental material for results with the unstimulated cells). Sucrose gradient ultracentrifugation was performed, and fractions were analyzed by immunoblotting for phospho-eIF2α with eIF2B. *, gel artifact; **, remaining signal for SFSV NSs-3×FLAG (lower band) from previous FLAG antibody staining due to incomplete stripping of the anti-FLAG antibody. (b and c) Coprecipitation experiments. HEK293 cells were transfected with expression plasmids, treated with arsenite to induce eIF2α phosphorylation, and lysed, and protein complexes were precipitated via specific tags and analyzed by immunoblotting. (b) eIF2B pulldown. eIF2Bε-mCitrine, SFSV NSs, and ΔMx were expressed, and eIF2B was precipitated via the mCitrine tag. *, cleavage or partial degradation product of eIF2Bε. (c) NSs pulldown. SFSV NSs-Myc-SBP and eGFP-SBP were expressed, and NSs was precipitated via the SBP tag. Shown data are representatives of 2 (a), 5 (b), or 3 (c) experiments. " width="100%" height="100%">
Journal: mBio
Article Title: eIF2B as a Target for Viral Evasion of PKR-Mediated Translation Inhibition
doi: 10.1128/mBio.00976-20
Figure Lengend Snippet: SFSV NSs allows binding of phospho-eIF2α to eIF2B. (a) Cofractionation experiments. HEK293 cells were transfected with expression plasmids for SFSV NSs-3×FLAG or 3×FLAG-ΔMx (negative control) or left untransfected. Half of the cells was stimulated with arsenite to induce eIF2α phosphorylation prior to lysis (see
Article Snippet: Primary antibodies were used as follows: β-actin (1:1,000, number [no.] 3700; Cell Signaling); eIF2α (1:1,000, no. 2103; Cell Signaling); phospho (p)-eIF2α (1:500, no. 3597 [Cell Signaling] and 1:1,000, no. 44728G [Invitrogen]);
Techniques: Binding Assay, Transfection, Expressing, Negative Control, Phospho-proteomics, Lysis, Western Blot, Staining, Stripping Membranes
Journal: mBio
Article Title: eIF2B as a Target for Viral Evasion of PKR-Mediated Translation Inhibition
doi: 10.1128/mBio.00976-20
Figure Lengend Snippet: PKR-mediated shutdown of translation and antagonistic strategies employed by viral proteins. (a) Shutdown of translation initiation mediated by PKR: in response to recognition of double-stranded RNA (dsRNA), PKR phosphorylates eIF2αSer51, resulting in nonproductive binding of the latter to eIF2B and, consequently, global inhibition of translation. Due to limiting concentrations of eIF2B compared to that of eIF2, partial eIF2α phosphorylation is sufficient to shutdown protein synthesis. (b) Previously reported viral strategies for PKR antagonism: viral proteins (blue) sequester viral RNA or affect PKR levels (such as NSs proteins of phleboviruses RVFV and TOSV), PKR activation, or the phosphorylation state of eIF2α. (c) Mechanism used by SFSV NSs: while PKR activation, PKR phosphorylation, and eIF2α phosphorylation occur in response to the virus infection and even the binding of p-eIF2α to eIF2B occurs, SFSV NSs enables cap-dependent translation by targeting eIF2B in a way that somehow neutralizes the nonproductive mode of eIF2B imposed by p-eIF2α binding.
Article Snippet: Primary antibodies were used as follows: β-actin (1:1,000, number [no.] 3700; Cell Signaling); eIF2α (1:1,000, no. 2103; Cell Signaling); phospho (p)-eIF2α (1:500, no. 3597 [Cell Signaling] and 1:1,000, no. 44728G [Invitrogen]);
Techniques: Binding Assay, Inhibition, Phospho-proteomics, Activation Assay, Virus, Infection
Journal: Nature Communications
Article Title: Sugar phosphate activation of the stress sensor eIF2B
doi: 10.1038/s41467-021-23836-z
Figure Lengend Snippet: a Volcano plot of metabolites analyzed in MIDAS, comparing the fold-change between the protein chamber and metabolite chamber. Red indicates metabolites that were significantly enriched in the protein-containing chamber, whereas blue indicates metabolites that were significantly depleted (q < 0.1) based on a two-tailed Wald test. The full data are available as Supplementary Data . b All 16 significant hits from the MIDAS binding screen numbered in a are tabulated. c Differential scanning fluorimetry of eIF2Bα in combination with selected metabolites in dose–response. Metabolite binding increased the T m of eIF2Bα. Bars are mean ± standard deviation of n = 4 independent experiments. Color coding in b , c are as in a . d K d of the eIF2Bα–F6P interaction measured by ITC. The upper subpanel shows the baseline-subtracted thermogram. The bottom subpanel represents the binding isotherm, with the red line indicating the fit curve.
Article Snippet: The nucleotide sequence of
Techniques: Two Tailed Test, Binding Assay, Standard Deviation
Journal: Nature Communications
Article Title: Sugar phosphate activation of the stress sensor eIF2B
doi: 10.1038/s41467-021-23836-z
Figure Lengend Snippet: a Plot of individual metabolites arrayed against GDP release t 1/2 derived from the GEF activity assay. Based on the basal activity of eIF2B under these assay conditions, a t 1/2 cutoff of <10 min was used to define activators (green) and a cutoff of >20 min was used to define inhibitors (orange). b List of the top 10 activators from the screen, ordered by GDP release t 1/2 . The full data are available as Supplementary Data . c Structures of the top 10 activators from the screen, compared to the substrate of archaeal RBPI. The sugar ring and 5′/6′ phosphate moiety are common structural motifs. d GDP release t 1/2 of eIF2B using increasing concentration of F6P or M6P. Only the eIF2B + F6P data could be fit to a dose-response curve with R > 0.9. Each point represents mean ± standard deviation of 3 technical replicates.
Article Snippet: The nucleotide sequence of
Techniques: Derivative Assay, Activity Assay, Concentration Assay, Standard Deviation
Journal: Nature Communications
Article Title: Sugar phosphate activation of the stress sensor eIF2B
doi: 10.1038/s41467-021-23836-z
Figure Lengend Snippet: a Overall structure of the eIF2B-F6P complex with eIF2Bα in cartoon representation and eIF2Bβ/δ/γ/ε represented as surfaces (PDB 7KMF). The single F6P molecule bound within each eIF2Bα monomer is shown as space-filling spheres. b Close-up view of the eIF2Bα metabolite binding pocket, with residues contributing to the F6P interaction shown in stick representation. H-bonds are represented by dashed yellow lines. c Overlay of the sugar phosphate binding pockets in the eIF2B-F6P cryo-EM structure (pink) and the eIF2Bα-M6P crystal structure (PDB 7KMA; teal). F6P and M6P are shown as yellow and green sticks, respectively.
Article Snippet: The nucleotide sequence of
Techniques: Binding Assay, Cryo-EM Sample Prep
Journal: Nature Communications
Article Title: Sugar phosphate activation of the stress sensor eIF2B
doi: 10.1038/s41467-021-23836-z
Figure Lengend Snippet: a – d eIF2B complex assembly from WT and eIF2Bα E198K HEK293T lysates treated with ISRIB (blue) or F6P (green) was monitored by sucrose gradient centrifugation. Fractions from the sucrose gradient were subjected to SDS-PAGE followed by immunoblotting with the indicated antibodies. eIF3a was used as an internal control. Western blot data in a , c are quantified in b , d , respectively. Data shown are representative of 2–3 replicates of each experiment. Bands were normalized by the total intensity of each subunit in its respective gradient. Dashed red lines demark the boundary of the decameric eIF2B peak. WT eIF2B forms a decamer in the presence of both ISRIB and F6P. By contrast, eIF2Bα E198K complexes respond to ISRIB but not F6P. e GDP release t 1/2 in a GEF assay using lysates from WT or eIF2Bα E198K cells. WT lysate activity is stimulated by both ISRIB and F6P, whereas eIF2Bα E198K lysate does not respond to F6P. Bars are mean ± standard deviation of n = 3 independent experiments of 3 technical replicates each. Statistical significance was tested by one-way ANOVA with Tukey’s multiple testing correction.
Article Snippet: The nucleotide sequence of
Techniques: Gradient Centrifugation, SDS Page, Western Blot, Control, GEF Assay, Activity Assay, Standard Deviation
Journal: Nature Communications
Article Title: Sugar phosphate activation of the stress sensor eIF2B
doi: 10.1038/s41467-021-23836-z
Figure Lengend Snippet: a Close-up view of a single eIF2Bα monomer showing the positions of residues V183 (green) and N208 (cyan). F6P is shown in stick representation. N208 is within the binding pocket and V183 is positioned at the interface with another eIF2Bα subunit. b GDP release t 1/2 in a GEF assay using recombinant eIF2B reconstituted with either eIF2Bα N208Y or eIF2Bα V183F . N208Y activity is stimulated by ISRIB (blue) but not F6P (green), whereas the reverse is true for V183F. Both mutants are stimulated by the combination of ISRIB and F6P (orange). Bars are mean ± standard deviation of n = 3 independent experiments of 3 technical replicates each. Statistical significance was tested by one-way ANOVA with Tukey’s multiple testing correction. c Size-exclusion chromatography of purified recombinant wild-type or V183F eIF2Bα in the presence of ISRIB and/or F6P. UV absorbance chromatograms as well as Coomassie-stained fractions are shown. Data shown are representative of 3 independent replicates. Wild-type eIF2Bα is a dimer whereas eIF2Bα V183F is a monomer, but is shifted towards a dimeric form by F6P. d Model depicting two distinct pathways to achieve eIF2B decamerization and activation. Arrow thickness indicates the rate of a reaction occurring. The synthetic activator ISRIB bridges the eIF2Bβ/δ interface to form an octamer, which then interacts with eIF2Bα 2 . Sugar phosphates bind to eIF2Bα 2 and promote its interaction with eIF2B(βδγε) to form the holoenzyme.
Article Snippet: The nucleotide sequence of
Techniques: Binding Assay, GEF Assay, Recombinant, Activity Assay, Standard Deviation, Size-exclusion Chromatography, Purification, Staining, Activation Assay