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  • 86
    Millipore flag
    Flag, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/flag/product/Millipore
    Average 86 stars, based on 1 article reviews
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    flag - by Bioz Stars, 2023-01
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    86
    Abnova mouse anti flag
    (a) Western blot analysis demonstrates the efficient amino acid dependant expression of an mCherry-EGFP fusion protein separated by an amber stop codon bearing a C-terminal HA-tag (mCh-TAG-EGFP-HA) in HEK293T cells. <t>Anti-FLAG</t> detected tagged PylRS (b) Specific labelling of mCh-TAG-EGFP-HA (immunoprecipitated from 106 cells) with 4a (20μM in 50μL PBS, 1h, RT) confirms the incorporation of 3 into protein in HEK293 cells. (c) SORT-M labelling of 3 that is statistically incorporated into newly synthesised proteins across the whole proteome of mammalian cells directed by six different PylRS/PyltRNAXXX mutants using 0.5 mM 3. Labeling with 4g (20μM in PBS, 1h, RT, as above). The amino acids in parentheses are the natural amino acids encoded by the endogenous tRNA bearing the corresponding anti-codon.
    Mouse Anti Flag, supplied by Abnova, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mouse anti flag/product/Abnova
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    mouse anti flag - by Bioz Stars, 2023-01
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    86
    Santa Cruz Biotechnology smo
    (a) Western blot analysis demonstrates the efficient amino acid dependant expression of an mCherry-EGFP fusion protein separated by an amber stop codon bearing a C-terminal HA-tag (mCh-TAG-EGFP-HA) in HEK293T cells. <t>Anti-FLAG</t> detected tagged PylRS (b) Specific labelling of mCh-TAG-EGFP-HA (immunoprecipitated from 106 cells) with 4a (20μM in 50μL PBS, 1h, RT) confirms the incorporation of 3 into protein in HEK293 cells. (c) SORT-M labelling of 3 that is statistically incorporated into newly synthesised proteins across the whole proteome of mammalian cells directed by six different PylRS/PyltRNAXXX mutants using 0.5 mM 3. Labeling with 4g (20μM in PBS, 1h, RT, as above). The amino acids in parentheses are the natural amino acids encoded by the endogenous tRNA bearing the corresponding anti-codon.
    Smo, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/smo/product/Santa Cruz Biotechnology
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    smo - by Bioz Stars, 2023-01
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    86
    Applied Biological Materials Inc anti flag
    LPS induces the translocation of CNBP to the nucleus by phosphorylation-mediated dimerization. ( A ) CNBP translocates to the nucleus from the cytosol in LPS-stimulated macrophages. Confocal microscopy of bone marrow-derived macrophages (BMDMs) that were stimulated with 80 ng ml −1 LPS for 0 or 30 min and then stained with DAPI and immunolabeled with anti-p65 antibody or anti-CNBP antibody. Scale bar, 5 μm. ( B ) The NLS of CNBP is important for the targeting of CNBP to the nucleus in response to LPS. Immunoblot analysis of CNBP or CNBP mutant (ΔNLS) in cytosolic and nuclear fractions of RAW macrophages after treatment with LPS (80 ng ml −1 ) for 0 or 2 h. Tubulin and lamin A/C were analyzed as loading controls for cytosolic and nuclear fractions, respectively. ( C ) C-terminal region of CNBP was aligned, and the conservation of residues is highlighted in shades of gray. Darker colors represent more conserved residues. Residues highlighted are Thr 173 and Thr 177 in the mouse. T173A, T177A and T173/177A indicate the point mutation at Thr 173 , Thr 177 and Thr 173 /Thr 177 to alanine of CNBP. ( D ) Both putative phosphorylation sites (Thr 173 and Thr 177 ) are required for the transcriptional activity of il-6 in response to LPS. MEFs were transfected with an empty vector (mock), wild-type GFP-CNBP vector or GFP-CNBP T173/177A vector, along with the il-6 luciferase reporter and Renilla reporter. Cells were then stimulated with LPS (80 ng ml −1 ) for 12 h. * P < 0.05 (Student's t -test). Immunoblot analysis of wild-type GFP-CNBP or GFP-CNBP T173/177A protein expression (right). ( E ) PKC, CK1 or TAK1 is responsible for LPS-mediated CNBP phosphorylation. HEK 293T cells were transfected with <t>FLAG-PKA,</t> FLAG-CK1, Myc-TAK1 or FLAG-PKC, and cell lysates were immunoprecipitated with <t>anti-FLAG</t> or anti-Myc antibodies. Phosphorylated CNBP was resolved by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and analyzed by autoradiography. Coomassie blue stained gels are shown in bottom panels. GST was used as a negative control. ( F ) Dimerization of endogenous CNBP is induced by LPS stimulation. RAW macrophages were treated with LPS (80 ng ml −1 ) for 2 h. GA, glutaraldehyde. ( G ) The formation of CNBP dimers was determined by co-immunoprecipitation (Co-IP). IP of Myc-CNBP from HEK 293T cells transfected with Myc-CNBP and GFP-CNBP, followed by immunoblot analysis (IB) with antibody to Myc or GFP. Asterisks indicate the IgG heavy and light chains. ( H ) The phosphorylation of CNBP is critical for its dimerization. The dimer forms of the total cell lysates (left) or nuclear fraction (right) of CNBP-HA were detected by immunoblot analysis under non-reducing conditions after treatment with LPS (80 ng ml −1 ) for 2 h. Data are representative of three independent experiments and are presented as mean ± s.d. in D.
    Anti Flag, supplied by Applied Biological Materials Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti flag/product/Applied Biological Materials Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti flag - by Bioz Stars, 2023-01
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    Image Search Results


    (a) Western blot analysis demonstrates the efficient amino acid dependant expression of an mCherry-EGFP fusion protein separated by an amber stop codon bearing a C-terminal HA-tag (mCh-TAG-EGFP-HA) in HEK293T cells. Anti-FLAG detected tagged PylRS (b) Specific labelling of mCh-TAG-EGFP-HA (immunoprecipitated from 106 cells) with 4a (20μM in 50μL PBS, 1h, RT) confirms the incorporation of 3 into protein in HEK293 cells. (c) SORT-M labelling of 3 that is statistically incorporated into newly synthesised proteins across the whole proteome of mammalian cells directed by six different PylRS/PyltRNAXXX mutants using 0.5 mM 3. Labeling with 4g (20μM in PBS, 1h, RT, as above). The amino acids in parentheses are the natural amino acids encoded by the endogenous tRNA bearing the corresponding anti-codon.

    Journal: Nature biotechnology

    Article Title: Proteome labelling and protein identification in specific tissues and at specific developmental stages in an animal

    doi: 10.1038/nbt.2860

    Figure Lengend Snippet: (a) Western blot analysis demonstrates the efficient amino acid dependant expression of an mCherry-EGFP fusion protein separated by an amber stop codon bearing a C-terminal HA-tag (mCh-TAG-EGFP-HA) in HEK293T cells. Anti-FLAG detected tagged PylRS (b) Specific labelling of mCh-TAG-EGFP-HA (immunoprecipitated from 106 cells) with 4a (20μM in 50μL PBS, 1h, RT) confirms the incorporation of 3 into protein in HEK293 cells. (c) SORT-M labelling of 3 that is statistically incorporated into newly synthesised proteins across the whole proteome of mammalian cells directed by six different PylRS/PyltRNAXXX mutants using 0.5 mM 3. Labeling with 4g (20μM in PBS, 1h, RT, as above). The amino acids in parentheses are the natural amino acids encoded by the endogenous tRNA bearing the corresponding anti-codon.

    Article Snippet: The samples were run out by SDS-PAGE, transferred to a nitrocellulose membrane and blotted using primary rat anti-HA(clone 3F10, Roche, No. 1 867 423) and mouse anti-FLAG (clone G191, Abnova, cat. MAB8183), the secondary antibodies were anti-rat (Invitrogen, {"type":"entrez-nucleotide","attrs":{"text":"A11077","term_id":"490928","term_text":"A11077"}} A11077 ) and anti-mouse (Cell Signaling Technologies, No. 7076S).

    Techniques: Western Blot, Expressing, Immunoprecipitation, Labeling

    LPS induces the translocation of CNBP to the nucleus by phosphorylation-mediated dimerization. ( A ) CNBP translocates to the nucleus from the cytosol in LPS-stimulated macrophages. Confocal microscopy of bone marrow-derived macrophages (BMDMs) that were stimulated with 80 ng ml −1 LPS for 0 or 30 min and then stained with DAPI and immunolabeled with anti-p65 antibody or anti-CNBP antibody. Scale bar, 5 μm. ( B ) The NLS of CNBP is important for the targeting of CNBP to the nucleus in response to LPS. Immunoblot analysis of CNBP or CNBP mutant (ΔNLS) in cytosolic and nuclear fractions of RAW macrophages after treatment with LPS (80 ng ml −1 ) for 0 or 2 h. Tubulin and lamin A/C were analyzed as loading controls for cytosolic and nuclear fractions, respectively. ( C ) C-terminal region of CNBP was aligned, and the conservation of residues is highlighted in shades of gray. Darker colors represent more conserved residues. Residues highlighted are Thr 173 and Thr 177 in the mouse. T173A, T177A and T173/177A indicate the point mutation at Thr 173 , Thr 177 and Thr 173 /Thr 177 to alanine of CNBP. ( D ) Both putative phosphorylation sites (Thr 173 and Thr 177 ) are required for the transcriptional activity of il-6 in response to LPS. MEFs were transfected with an empty vector (mock), wild-type GFP-CNBP vector or GFP-CNBP T173/177A vector, along with the il-6 luciferase reporter and Renilla reporter. Cells were then stimulated with LPS (80 ng ml −1 ) for 12 h. * P < 0.05 (Student's t -test). Immunoblot analysis of wild-type GFP-CNBP or GFP-CNBP T173/177A protein expression (right). ( E ) PKC, CK1 or TAK1 is responsible for LPS-mediated CNBP phosphorylation. HEK 293T cells were transfected with FLAG-PKA, FLAG-CK1, Myc-TAK1 or FLAG-PKC, and cell lysates were immunoprecipitated with anti-FLAG or anti-Myc antibodies. Phosphorylated CNBP was resolved by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and analyzed by autoradiography. Coomassie blue stained gels are shown in bottom panels. GST was used as a negative control. ( F ) Dimerization of endogenous CNBP is induced by LPS stimulation. RAW macrophages were treated with LPS (80 ng ml −1 ) for 2 h. GA, glutaraldehyde. ( G ) The formation of CNBP dimers was determined by co-immunoprecipitation (Co-IP). IP of Myc-CNBP from HEK 293T cells transfected with Myc-CNBP and GFP-CNBP, followed by immunoblot analysis (IB) with antibody to Myc or GFP. Asterisks indicate the IgG heavy and light chains. ( H ) The phosphorylation of CNBP is critical for its dimerization. The dimer forms of the total cell lysates (left) or nuclear fraction (right) of CNBP-HA were detected by immunoblot analysis under non-reducing conditions after treatment with LPS (80 ng ml −1 ) for 2 h. Data are representative of three independent experiments and are presented as mean ± s.d. in D.

    Journal: Nucleic Acids Research

    Article Title: CNBP acts as a key transcriptional regulator of sustained expression of interleukin-6

    doi: 10.1093/nar/gkx071

    Figure Lengend Snippet: LPS induces the translocation of CNBP to the nucleus by phosphorylation-mediated dimerization. ( A ) CNBP translocates to the nucleus from the cytosol in LPS-stimulated macrophages. Confocal microscopy of bone marrow-derived macrophages (BMDMs) that were stimulated with 80 ng ml −1 LPS for 0 or 30 min and then stained with DAPI and immunolabeled with anti-p65 antibody or anti-CNBP antibody. Scale bar, 5 μm. ( B ) The NLS of CNBP is important for the targeting of CNBP to the nucleus in response to LPS. Immunoblot analysis of CNBP or CNBP mutant (ΔNLS) in cytosolic and nuclear fractions of RAW macrophages after treatment with LPS (80 ng ml −1 ) for 0 or 2 h. Tubulin and lamin A/C were analyzed as loading controls for cytosolic and nuclear fractions, respectively. ( C ) C-terminal region of CNBP was aligned, and the conservation of residues is highlighted in shades of gray. Darker colors represent more conserved residues. Residues highlighted are Thr 173 and Thr 177 in the mouse. T173A, T177A and T173/177A indicate the point mutation at Thr 173 , Thr 177 and Thr 173 /Thr 177 to alanine of CNBP. ( D ) Both putative phosphorylation sites (Thr 173 and Thr 177 ) are required for the transcriptional activity of il-6 in response to LPS. MEFs were transfected with an empty vector (mock), wild-type GFP-CNBP vector or GFP-CNBP T173/177A vector, along with the il-6 luciferase reporter and Renilla reporter. Cells were then stimulated with LPS (80 ng ml −1 ) for 12 h. * P < 0.05 (Student's t -test). Immunoblot analysis of wild-type GFP-CNBP or GFP-CNBP T173/177A protein expression (right). ( E ) PKC, CK1 or TAK1 is responsible for LPS-mediated CNBP phosphorylation. HEK 293T cells were transfected with FLAG-PKA, FLAG-CK1, Myc-TAK1 or FLAG-PKC, and cell lysates were immunoprecipitated with anti-FLAG or anti-Myc antibodies. Phosphorylated CNBP was resolved by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and analyzed by autoradiography. Coomassie blue stained gels are shown in bottom panels. GST was used as a negative control. ( F ) Dimerization of endogenous CNBP is induced by LPS stimulation. RAW macrophages were treated with LPS (80 ng ml −1 ) for 2 h. GA, glutaraldehyde. ( G ) The formation of CNBP dimers was determined by co-immunoprecipitation (Co-IP). IP of Myc-CNBP from HEK 293T cells transfected with Myc-CNBP and GFP-CNBP, followed by immunoblot analysis (IB) with antibody to Myc or GFP. Asterisks indicate the IgG heavy and light chains. ( H ) The phosphorylation of CNBP is critical for its dimerization. The dimer forms of the total cell lysates (left) or nuclear fraction (right) of CNBP-HA were detected by immunoblot analysis under non-reducing conditions after treatment with LPS (80 ng ml −1 ) for 2 h. Data are representative of three independent experiments and are presented as mean ± s.d. in D.

    Article Snippet: The following antibodies were used: anti-CNBP (ab83038; Abcam, Cambridge, UK or sc-515387; Santa Cruz Biotechnology, Santa Cruz, CA, USA), anti-p65 (sc-8008; Santa Cruz Biotechnology), anti-tubulin (G094; ABM Inc., Richmond, Canada), anti-FLAG (G191; ABM Inc. and M185-3L; MBL International, Woburn, MA, USA), anti-HA (G036; ABM Inc.), anti-Myc (2276; Cell Signaling Technology), anti-GFP (11814460001; Roche, Basel, Switzerland and ab290; Abcam) and anti-Lamin A/C (2032; Cell Signaling Technology).

    Techniques: Translocation Assay, Confocal Microscopy, Derivative Assay, Staining, Immunolabeling, Western Blot, Mutagenesis, Activity Assay, Transfection, Plasmid Preparation, Luciferase, Expressing, Immunoprecipitation, Polyacrylamide Gel Electrophoresis, Autoradiography, Negative Control, Co-Immunoprecipitation Assay