type i human ifn α2a Search Results


k-562  (ATCC)
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ATCC k-562
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R&D Systems type i human ifn α2a
Type I Human Ifn α2a, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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R&D Systems human type ifn-α2a
Unbiased hierarchical clustered heat map showing the log 2 fold changes of <t>IFN-induced</t> proteins (GO <t>type-I</t> IFN) identified from capsids-host protein sediments from cytosol of resting Mφ, or IFN-induced Mφ IFN macrophages. For each protein, the fold change was calculated based on their abundance (iBAQs) in V 1 , V 0.5 and V 0.1 capsids as compared to their abundance in D capsids, using a linear scale from violet being the lowest to dark green being the highest. (*) and (**) design the proteins with an FDR corrected p-value < 0.05 and < 0.01, respectively.
Human Type Ifn α2a, supplied by R&D Systems, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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R&D Systems human type i interferons
Unbiased hierarchical clustered heat map showing the log 2 fold changes of <t>IFN-induced</t> proteins (GO <t>type-I</t> IFN) identified from capsids-host protein sediments from cytosol of resting Mφ, or IFN-induced Mφ IFN macrophages. For each protein, the fold change was calculated based on their abundance (iBAQs) in V 1 , V 0.5 and V 0.1 capsids as compared to their abundance in D capsids, using a linear scale from violet being the lowest to dark green being the highest. (*) and (**) design the proteins with an FDR corrected p-value < 0.05 and < 0.01, respectively.
Human Type I Interferons, supplied by R&D Systems, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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ImmunoTools rhifn-α2a
Unbiased hierarchical clustered heat map showing the log 2 fold changes of <t>IFN-induced</t> proteins (GO <t>type-I</t> IFN) identified from capsids-host protein sediments from cytosol of resting Mφ, or IFN-induced Mφ IFN macrophages. For each protein, the fold change was calculated based on their abundance (iBAQs) in V 1 , V 0.5 and V 0.1 capsids as compared to their abundance in D capsids, using a linear scale from violet being the lowest to dark green being the highest. (*) and (**) design the proteins with an FDR corrected p-value < 0.05 and < 0.01, respectively.
Rhifn α2a, supplied by ImmunoTools, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Bio-Techne corporation recombinant human il-28a/ifn-lambda 2 protein, cf
Unbiased hierarchical clustered heat map showing the log 2 fold changes of <t>IFN-induced</t> proteins (GO <t>type-I</t> IFN) identified from capsids-host protein sediments from cytosol of resting Mφ, or IFN-induced Mφ IFN macrophages. For each protein, the fold change was calculated based on their abundance (iBAQs) in V 1 , V 0.5 and V 0.1 capsids as compared to their abundance in D capsids, using a linear scale from violet being the lowest to dark green being the highest. (*) and (**) design the proteins with an FDR corrected p-value < 0.05 and < 0.01, respectively.
Recombinant Human Il 28a/Ifn Lambda 2 Protein, Cf, supplied by Bio-Techne corporation, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Bio-Techne corporation recombinant human il-28b/ifn-lambda 3 protein, cf
Unbiased hierarchical clustered heat map showing the log 2 fold changes of <t>IFN-induced</t> proteins (GO <t>type-I</t> IFN) identified from capsids-host protein sediments from cytosol of resting Mφ, or IFN-induced Mφ IFN macrophages. For each protein, the fold change was calculated based on their abundance (iBAQs) in V 1 , V 0.5 and V 0.1 capsids as compared to their abundance in D capsids, using a linear scale from violet being the lowest to dark green being the highest. (*) and (**) design the proteins with an FDR corrected p-value < 0.05 and < 0.01, respectively.
Recombinant Human Il 28b/Ifn Lambda 3 Protein, Cf, supplied by Bio-Techne corporation, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Bio-Techne corporation recombinant human il-28a/ifn-lambda 2 protein
Unbiased hierarchical clustered heat map showing the log 2 fold changes of <t>IFN-induced</t> proteins (GO <t>type-I</t> IFN) identified from capsids-host protein sediments from cytosol of resting Mφ, or IFN-induced Mφ IFN macrophages. For each protein, the fold change was calculated based on their abundance (iBAQs) in V 1 , V 0.5 and V 0.1 capsids as compared to their abundance in D capsids, using a linear scale from violet being the lowest to dark green being the highest. (*) and (**) design the proteins with an FDR corrected p-value < 0.05 and < 0.01, respectively.
Recombinant Human Il 28a/Ifn Lambda 2 Protein, supplied by Bio-Techne corporation, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Bio-Techne corporation recombinant human il-29/ifn-lambda 1 protein, cf
Unbiased hierarchical clustered heat map showing the log 2 fold changes of <t>IFN-induced</t> proteins (GO <t>type-I</t> IFN) identified from capsids-host protein sediments from cytosol of resting Mφ, or IFN-induced Mφ IFN macrophages. For each protein, the fold change was calculated based on their abundance (iBAQs) in V 1 , V 0.5 and V 0.1 capsids as compared to their abundance in D capsids, using a linear scale from violet being the lowest to dark green being the highest. (*) and (**) design the proteins with an FDR corrected p-value < 0.05 and < 0.01, respectively.
Recombinant Human Il 29/Ifn Lambda 1 Protein, Cf, supplied by Bio-Techne corporation, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Bio-Techne corporation recombinant human il-28b/ifn-lambda 3 protein
Unbiased hierarchical clustered heat map showing the log 2 fold changes of <t>IFN-induced</t> proteins (GO <t>type-I</t> IFN) identified from capsids-host protein sediments from cytosol of resting Mφ, or IFN-induced Mφ IFN macrophages. For each protein, the fold change was calculated based on their abundance (iBAQs) in V 1 , V 0.5 and V 0.1 capsids as compared to their abundance in D capsids, using a linear scale from violet being the lowest to dark green being the highest. (*) and (**) design the proteins with an FDR corrected p-value < 0.05 and < 0.01, respectively.
Recombinant Human Il 28b/Ifn Lambda 3 Protein, supplied by Bio-Techne corporation, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Unbiased hierarchical clustered heat map showing the log 2 fold changes of <t>IFN-induced</t> proteins (GO <t>type-I</t> IFN) identified from capsids-host protein sediments from cytosol of resting Mφ, or IFN-induced Mφ IFN macrophages. For each protein, the fold change was calculated based on their abundance (iBAQs) in V 1 , V 0.5 and V 0.1 capsids as compared to their abundance in D capsids, using a linear scale from violet being the lowest to dark green being the highest. (*) and (**) design the proteins with an FDR corrected p-value < 0.05 and < 0.01, respectively.
Recombinant Human Il 29/Ifn Lambda 1 Protein, supplied by Bio-Techne corporation, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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PBL Assay universal type ifn (hifn-αa/d
(A) Gel mobility shift assay was performed using the wild-type (WT) probe (the −434∼−401 region of the IFNLR1 promoter) and the mutant (MUT) probe ( CCAAT motif substituted with AACCG ), incubated with U87 cell nuclear extracts, poly (dA∶dT), 100-fold excess of cold probe, and the indicated antibodies. (B) ChIP analysis was performed on the IFNLR1 promoter in Huh7 and U87 cells with NF-YC and control IgG antibodies. (C–D) NF-YA and IFNLR1 expression was examined by RT-qPCR in Huh7 cells transfected with scrambled or NF-YA-specific siRNAs. (E, G) Expression of NF-YA and receptor subunits of type I, II, and III <t>IFNs</t> was examined by RT-qPCR in Huh7 cells stably expressing scrambled or NF-YA-specific shRNAs. (F) Lysates from Huh7 stable cell lines were harvested and used for WB using the indicated antibodies. Lamin B serves as loading control for nuclear proteins. (H–I) NF-YA and IFNLR1 expression was measured by RT-qPCR in PHHs infected with lentiviruses encoding scrambled or NF-YA-specific shRNAs. In all panels, data represent the mean and SEM of at least three experiments.
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Image Search Results


Unbiased hierarchical clustered heat map showing the log 2 fold changes of IFN-induced proteins (GO type-I IFN) identified from capsids-host protein sediments from cytosol of resting Mφ, or IFN-induced Mφ IFN macrophages. For each protein, the fold change was calculated based on their abundance (iBAQs) in V 1 , V 0.5 and V 0.1 capsids as compared to their abundance in D capsids, using a linear scale from violet being the lowest to dark green being the highest. (*) and (**) design the proteins with an FDR corrected p-value < 0.05 and < 0.01, respectively.

Journal: bioRxiv

Article Title: The interferon-inducible GTPase MxB promotes capsid disassembly and genome release of herpesviruses

doi: 10.1101/2022.01.25.477704

Figure Lengend Snippet: Unbiased hierarchical clustered heat map showing the log 2 fold changes of IFN-induced proteins (GO type-I IFN) identified from capsids-host protein sediments from cytosol of resting Mφ, or IFN-induced Mφ IFN macrophages. For each protein, the fold change was calculated based on their abundance (iBAQs) in V 1 , V 0.5 and V 0.1 capsids as compared to their abundance in D capsids, using a linear scale from violet being the lowest to dark green being the highest. (*) and (**) design the proteins with an FDR corrected p-value < 0.05 and < 0.01, respectively.

Article Snippet: The cells were cultured with 1000 U/mL human type I IFN-α2a (Mφ IFN ; R&D Systems, Minneapolis, Minnesota, USA) or left untreated for 16 h. A549 cells were cultured in DMEM with 10% FCS.

Techniques:

(A) Gel mobility shift assay was performed using the wild-type (WT) probe (the −434∼−401 region of the IFNLR1 promoter) and the mutant (MUT) probe ( CCAAT motif substituted with AACCG ), incubated with U87 cell nuclear extracts, poly (dA∶dT), 100-fold excess of cold probe, and the indicated antibodies. (B) ChIP analysis was performed on the IFNLR1 promoter in Huh7 and U87 cells with NF-YC and control IgG antibodies. (C–D) NF-YA and IFNLR1 expression was examined by RT-qPCR in Huh7 cells transfected with scrambled or NF-YA-specific siRNAs. (E, G) Expression of NF-YA and receptor subunits of type I, II, and III IFNs was examined by RT-qPCR in Huh7 cells stably expressing scrambled or NF-YA-specific shRNAs. (F) Lysates from Huh7 stable cell lines were harvested and used for WB using the indicated antibodies. Lamin B serves as loading control for nuclear proteins. (H–I) NF-YA and IFNLR1 expression was measured by RT-qPCR in PHHs infected with lentiviruses encoding scrambled or NF-YA-specific shRNAs. In all panels, data represent the mean and SEM of at least three experiments.

Journal: PLoS Biology

Article Title: Epigenetic Reprogramming of the Type III Interferon Response Potentiates Antiviral Activity and Suppresses Tumor Growth

doi: 10.1371/journal.pbio.1001758

Figure Lengend Snippet: (A) Gel mobility shift assay was performed using the wild-type (WT) probe (the −434∼−401 region of the IFNLR1 promoter) and the mutant (MUT) probe ( CCAAT motif substituted with AACCG ), incubated with U87 cell nuclear extracts, poly (dA∶dT), 100-fold excess of cold probe, and the indicated antibodies. (B) ChIP analysis was performed on the IFNLR1 promoter in Huh7 and U87 cells with NF-YC and control IgG antibodies. (C–D) NF-YA and IFNLR1 expression was examined by RT-qPCR in Huh7 cells transfected with scrambled or NF-YA-specific siRNAs. (E, G) Expression of NF-YA and receptor subunits of type I, II, and III IFNs was examined by RT-qPCR in Huh7 cells stably expressing scrambled or NF-YA-specific shRNAs. (F) Lysates from Huh7 stable cell lines were harvested and used for WB using the indicated antibodies. Lamin B serves as loading control for nuclear proteins. (H–I) NF-YA and IFNLR1 expression was measured by RT-qPCR in PHHs infected with lentiviruses encoding scrambled or NF-YA-specific shRNAs. In all panels, data represent the mean and SEM of at least three experiments.

Article Snippet: CD4 + T cells were cultured in complete RPMI 1640 medium supplemented with 100 U/ml IL-2 and 100 ng/ml IL-7 and stimulated with 10 µg/ml PHA every 72 h. Cells were treated with recombinant human IFN-α2a, IFN-β, human IFN-λ1, IFN-λ2, IFN-λ3 (R&D Systems), murine IFN-λ2 (PeproTech), or universal type I IFN (hIFN-αA/D) (PBL Interferon Source).

Techniques: Mobility Shift, Mutagenesis, Incubation, Expressing, Quantitative RT-PCR, Transfection, Stable Transfection, Infection