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  • 95
    Millipore hrp conjugated streptavidin
    Proximity Utilizing Biotinylation (PUB) allows for detection of nuclear envelope-proximal regions on mitotic chromosomes. ( A ) The Proximity Utilizing Biotinylation principle. The PUB approach is based on coexpression of protein X fused to biotin ligase (BirA) and protein Y fused to biotin acceptor peptide (BAP). When the proteins are in sufficient proximity or interact with each other in cells harboring the corresponding plasmids, in the presence of biotin (pink), BirA specifically biotinylates the BAP peptide, resulting in a persistent label on the BAP-carrying protein. ( B ) Emerin is localized at the NE. 293T cells were transfected with emerin-GFP (green) and stained with DAPI (blue). Scale bar: 10 μm. ( C ) Biotinylation of NE proximal chromatin using BirA-emerin fusion. 293T cells were transfected with BirA-emerin and BAP-H2A or BAP-H3.1, followed by biotin pulse labeling and counterstaining with <t>streptavidin-Cy3</t> (red) and DAPI (blue). Scale bar: 10 μm. ( D ) The biotin label depends on BAP-histone biotinylation. Western blot analysis was performed on nuclei from control (untransfected) and transfected 293T cells using <t>anti-His-HRP</t> (left) or streptavidin-HRP (right). The bands corresponding to BAP-histones, biotinylated BAP-histones, the ubiquitinated form of BAP-H2A (Ub-BAP-H2A) and non-specific signals (NS) are indicated. ( E ) PUB pulse and chase principle. BirA is fused to a nuclear envelope (NE) protein and BAP to a histone resulting in biotin labeling of chromatin proximal to the NE during interphase. The resulting biotin signals appear as bands on mitotic chromosomes. ( F ) PUB pulse and chase experiment. Interphase 293T cells coexpressing BirA-emerin and BAP-H2A are biotin pulse labeled followed by streptavidin-Cy3 (red) and DAPI (blue) staining (top). After 4 h chase, biotin signal was revealed on mitotic chromosomes using the same staining dies as previously described (bottom). Scale bar: 10 μm.
    Hrp Conjugated Streptavidin, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 490 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Vector Laboratories streptavidin hrp
    Western blot results of Avi-Tag SH2 domain proteins using an <t>streptavidin-HRP</t> conjugate to detect the presence of biotin. DOI: http://dx.doi.org/10.7554/eLife.24903.005
    Streptavidin Hrp, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 95/100, based on 756 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Cusabio horseradish streptavidin
    Western blot results of Avi-Tag SH2 domain proteins using an <t>streptavidin-HRP</t> conjugate to detect the presence of biotin. DOI: http://dx.doi.org/10.7554/eLife.24903.005
    Horseradish Streptavidin, supplied by Cusabio, used in various techniques. Bioz Stars score: 88/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    77
    Santa Cruz Biotechnology horseradish streptavidin
    Western blot results of Avi-Tag SH2 domain proteins using an <t>streptavidin-HRP</t> conjugate to detect the presence of biotin. DOI: http://dx.doi.org/10.7554/eLife.24903.005
    Horseradish Streptavidin, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 77/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Thermo Fisher streptavidin horseradish conjugate
    Western blot results of Avi-Tag SH2 domain proteins using an <t>streptavidin-HRP</t> conjugate to detect the presence of biotin. DOI: http://dx.doi.org/10.7554/eLife.24903.005
    Streptavidin Horseradish Conjugate, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 79/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore streptavidin horseradish conjugate
    Western blot results of Avi-Tag SH2 domain proteins using an <t>streptavidin-HRP</t> conjugate to detect the presence of biotin. DOI: http://dx.doi.org/10.7554/eLife.24903.005
    Streptavidin Horseradish Conjugate, supplied by Millipore, used in various techniques. Bioz Stars score: 79/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Agilent technologies horseradish conjugated streptavidin
    Western blot results of Avi-Tag SH2 domain proteins using an <t>streptavidin-HRP</t> conjugate to detect the presence of biotin. DOI: http://dx.doi.org/10.7554/eLife.24903.005
    Horseradish Conjugated Streptavidin, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 93/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Becton Dickinson horseradish conjugated streptavidin
    Western blot results of Avi-Tag SH2 domain proteins using an <t>streptavidin-HRP</t> conjugate to detect the presence of biotin. DOI: http://dx.doi.org/10.7554/eLife.24903.005
    Horseradish Conjugated Streptavidin, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 78/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology horseradish labeled streptavidin
    Western blot results of Avi-Tag SH2 domain proteins using an <t>streptavidin-HRP</t> conjugate to detect the presence of biotin. DOI: http://dx.doi.org/10.7554/eLife.24903.005
    Horseradish Labeled Streptavidin, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher horseradish conjugated streptavidin
    Western blot results of Avi-Tag SH2 domain proteins using an <t>streptavidin-HRP</t> conjugate to detect the presence of biotin. DOI: http://dx.doi.org/10.7554/eLife.24903.005
    Horseradish Conjugated Streptavidin, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 78/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Thermo Fisher streptavidin hrp conjugate
    Target-selective protein labelling with LDNASA chemistry. a Western blotting analysis of FKBP12 labelling in cell lysates. HeLa cell lysate was mixed with recombinant FKBP12 (1 µM) and incubated with reagent in 50 mM HEPES buffer, pH 7.2, 37 °C, 1 h. <t>SAv-HRP,</t> <t>streptavidin–horseradish</t> peroxidase conjugate; CBB, Coomassie brilliant blue staining. The high background (smear) signals of lane 6 and 7 may suggest unspecific labelling due to a high concentration of reagent (20 µM), whereas such background signals were less in lanes 1–5 (1–5 µM of reagent). b Western blotting analysis of endogenous FKBP12 labelling in live C2C12 cells. The cells were treated with 1 or 5 (1 µM) for 0–120 min at 37 °C in medium. c Time course plot of the endogenous FKBP12 labelling with 1 . d Molecular structures of LDNASA 9 and LDAI 10 for FR labelling. e In-gel fluorescence and western blotting analysis of endogenous FR labelling in KB cells. The cells were treated with 9 or 10 (1 µM) for 0–60 min at 37 °C in medium. FA, Folic acid (competitive inhibitor). f Time profile of the endogenous FR labelling with 9 . I and I 30 min are band intensities of Oregon Green-labelled FR at the indicated time point and at 30 min, respectively. Error bars represent s.d., n = 3
    Streptavidin Hrp Conjugate, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 611 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    77
    Thermo Fisher streptavidin horseradish
    Target-selective protein labelling with LDNASA chemistry. a Western blotting analysis of FKBP12 labelling in cell lysates. HeLa cell lysate was mixed with recombinant FKBP12 (1 µM) and incubated with reagent in 50 mM HEPES buffer, pH 7.2, 37 °C, 1 h. <t>SAv-HRP,</t> <t>streptavidin–horseradish</t> peroxidase conjugate; CBB, Coomassie brilliant blue staining. The high background (smear) signals of lane 6 and 7 may suggest unspecific labelling due to a high concentration of reagent (20 µM), whereas such background signals were less in lanes 1–5 (1–5 µM of reagent). b Western blotting analysis of endogenous FKBP12 labelling in live C2C12 cells. The cells were treated with 1 or 5 (1 µM) for 0–120 min at 37 °C in medium. c Time course plot of the endogenous FKBP12 labelling with 1 . d Molecular structures of LDNASA 9 and LDAI 10 for FR labelling. e In-gel fluorescence and western blotting analysis of endogenous FR labelling in KB cells. The cells were treated with 9 or 10 (1 µM) for 0–60 min at 37 °C in medium. FA, Folic acid (competitive inhibitor). f Time profile of the endogenous FR labelling with 9 . I and I 30 min are band intensities of Oregon Green-labelled FR at the indicated time point and at 30 min, respectively. Error bars represent s.d., n = 3
    Streptavidin Horseradish, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 77/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Thermo Fisher horseradish peroxidase streptavidin
    Expression of protocadherins. GFP was electroporated alone or in combination with protocadherins into K562 cells. a Immunoblotting of cell lysates with anti-GFP shows bands compatible with the expected molecular weights for GFP (27 kDa) and mature PCDHB11-GFP (110 kDa); image representative of three transfections. b Immunoblotting of cell lysates with anti-HA shows bands compatible with the expected molecular weights for mature HA-PCDHB11-GFP (113 kDa) and HA-PCDHGA3 (99 kDa); image representative of two transfections. c Proportion of medium and large clusters was lower in HA-PCDHB11-GFP-transfected than in HA-PCDHGA3-transfected cells, but higher than in control cells ( n = 10-12 images per condition). d Proportion of medium to large cell clusters when normalized by HA-PCDHGA3. For visualization of surface protocadherins, live cells transfected with GFP alone (e) or in combination with HA-PCDHB11-GFP (f) or HA-PCDHGA3 (g) were stained with anti-HA-biotin and <t>streptavidin-Alexa555,</t> then fixed. Blue: DAPI. Green: GFP. Red: surface HA-tagged protocadherins. Scale bar: 10 μm
    Horseradish Peroxidase Streptavidin, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 79/100, based on 49 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    84
    Agilent technologies streptavidin horseradish
    Expression of protocadherins. GFP was electroporated alone or in combination with protocadherins into K562 cells. a Immunoblotting of cell lysates with anti-GFP shows bands compatible with the expected molecular weights for GFP (27 kDa) and mature PCDHB11-GFP (110 kDa); image representative of three transfections. b Immunoblotting of cell lysates with anti-HA shows bands compatible with the expected molecular weights for mature HA-PCDHB11-GFP (113 kDa) and HA-PCDHGA3 (99 kDa); image representative of two transfections. c Proportion of medium and large clusters was lower in HA-PCDHB11-GFP-transfected than in HA-PCDHGA3-transfected cells, but higher than in control cells ( n = 10-12 images per condition). d Proportion of medium to large cell clusters when normalized by HA-PCDHGA3. For visualization of surface protocadherins, live cells transfected with GFP alone (e) or in combination with HA-PCDHB11-GFP (f) or HA-PCDHGA3 (g) were stained with anti-HA-biotin and <t>streptavidin-Alexa555,</t> then fixed. Blue: DAPI. Green: GFP. Red: surface HA-tagged protocadherins. Scale bar: 10 μm
    Streptavidin Horseradish, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 84/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Abcam streptavidin hrp conjugate
    Target-selective protein labelling with LDNASA chemistry. a Western blotting analysis of FKBP12 labelling in cell lysates. HeLa cell lysate was mixed with recombinant FKBP12 (1 µM) and incubated with reagent in 50 mM HEPES buffer, pH 7.2, 37 °C, 1 h. <t>SAv-HRP,</t> <t>streptavidin–horseradish</t> peroxidase conjugate; CBB, Coomassie brilliant blue staining. The high background (smear) signals of lane 6 and 7 may suggest unspecific labelling due to a high concentration of reagent (20 µM), whereas such background signals were less in lanes 1–5 (1–5 µM of reagent). b Western blotting analysis of endogenous FKBP12 labelling in live C2C12 cells. The cells were treated with 1 or 5 (1 µM) for 0–120 min at 37 °C in medium. c Time course plot of the endogenous FKBP12 labelling with 1 . d Molecular structures of LDNASA 9 and LDAI 10 for FR labelling. e In-gel fluorescence and western blotting analysis of endogenous FR labelling in KB cells. The cells were treated with 9 or 10 (1 µM) for 0–60 min at 37 °C in medium. FA, Folic acid (competitive inhibitor). f Time profile of the endogenous FR labelling with 9 . I and I 30 min are band intensities of Oregon Green-labelled FR at the indicated time point and at 30 min, respectively. Error bars represent s.d., n = 3
    Streptavidin Hrp Conjugate, supplied by Abcam, used in various techniques. Bioz Stars score: 90/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Agilent technologies streptavidin horseradish peroxidiase hrp
    Target-selective protein labelling with LDNASA chemistry. a Western blotting analysis of FKBP12 labelling in cell lysates. HeLa cell lysate was mixed with recombinant FKBP12 (1 µM) and incubated with reagent in 50 mM HEPES buffer, pH 7.2, 37 °C, 1 h. <t>SAv-HRP,</t> <t>streptavidin–horseradish</t> peroxidase conjugate; CBB, Coomassie brilliant blue staining. The high background (smear) signals of lane 6 and 7 may suggest unspecific labelling due to a high concentration of reagent (20 µM), whereas such background signals were less in lanes 1–5 (1–5 µM of reagent). b Western blotting analysis of endogenous FKBP12 labelling in live C2C12 cells. The cells were treated with 1 or 5 (1 µM) for 0–120 min at 37 °C in medium. c Time course plot of the endogenous FKBP12 labelling with 1 . d Molecular structures of LDNASA 9 and LDAI 10 for FR labelling. e In-gel fluorescence and western blotting analysis of endogenous FR labelling in KB cells. The cells were treated with 9 or 10 (1 µM) for 0–60 min at 37 °C in medium. FA, Folic acid (competitive inhibitor). f Time profile of the endogenous FR labelling with 9 . I and I 30 min are band intensities of Oregon Green-labelled FR at the indicated time point and at 30 min, respectively. Error bars represent s.d., n = 3
    Streptavidin Horseradish Peroxidiase Hrp, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 78/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    BioLegend horseradish peroxidase streptavidin
    SDS-PAGE analysis of the albumin- and IgG-depleted and AAL-captured glycoproteins from the pooled serum samples of HE and patients with SCLC. A, pattern check of the albumin- and IgG-depleted human serum samples. The pooled sera from HE, LD, and ED patients were depleted of albumin and IgG using immunoaffinity columns, followed by SDS-PAGE. The purified proteins were visualized by Coomassie Brilliant Blue staining. T, total crude sera; B, albumin and IgG column-bound proteins; D, albumin- and IgG-depleted sera. The most prominent removal was observed in serum albumin (∼66 kDa), which represents ∼50% of the total protein content in crude sera. The IgG heavy chain (∼55 kDa) was also efficiently removed. B, depleted sera were enriched for fucosylated glycoproteins using AAL columns. The flow-through and the AAL-bound fucosylation enriched-proteins were visualized by Coomassie Brilliant Blue staining. Flow-through , AAL column unbound proteins; Elution , AAL column-bound proteins. C, visualization of the same samples from B was performed by AAL blot analysis using biotinylated AAL and horseradish peroxidase-conjugated <t>streptavidin.</t>
    Horseradish Peroxidase Streptavidin, supplied by BioLegend, used in various techniques. Bioz Stars score: 90/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Thermo Fisher streptavidin avidin horseradish peroxidase
    SDS-PAGE analysis of the albumin- and IgG-depleted and AAL-captured glycoproteins from the pooled serum samples of HE and patients with SCLC. A, pattern check of the albumin- and IgG-depleted human serum samples. The pooled sera from HE, LD, and ED patients were depleted of albumin and IgG using immunoaffinity columns, followed by SDS-PAGE. The purified proteins were visualized by Coomassie Brilliant Blue staining. T, total crude sera; B, albumin and IgG column-bound proteins; D, albumin- and IgG-depleted sera. The most prominent removal was observed in serum albumin (∼66 kDa), which represents ∼50% of the total protein content in crude sera. The IgG heavy chain (∼55 kDa) was also efficiently removed. B, depleted sera were enriched for fucosylated glycoproteins using AAL columns. The flow-through and the AAL-bound fucosylation enriched-proteins were visualized by Coomassie Brilliant Blue staining. Flow-through , AAL column unbound proteins; Elution , AAL column-bound proteins. C, visualization of the same samples from B was performed by AAL blot analysis using biotinylated AAL and horseradish peroxidase-conjugated <t>streptavidin.</t>
    Streptavidin Avidin Horseradish Peroxidase, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Biogenex streptavidin horseradish peroixidase
    SDS-PAGE analysis of the albumin- and IgG-depleted and AAL-captured glycoproteins from the pooled serum samples of HE and patients with SCLC. A, pattern check of the albumin- and IgG-depleted human serum samples. The pooled sera from HE, LD, and ED patients were depleted of albumin and IgG using immunoaffinity columns, followed by SDS-PAGE. The purified proteins were visualized by Coomassie Brilliant Blue staining. T, total crude sera; B, albumin and IgG column-bound proteins; D, albumin- and IgG-depleted sera. The most prominent removal was observed in serum albumin (∼66 kDa), which represents ∼50% of the total protein content in crude sera. The IgG heavy chain (∼55 kDa) was also efficiently removed. B, depleted sera were enriched for fucosylated glycoproteins using AAL columns. The flow-through and the AAL-bound fucosylation enriched-proteins were visualized by Coomassie Brilliant Blue staining. Flow-through , AAL column unbound proteins; Elution , AAL column-bound proteins. C, visualization of the same samples from B was performed by AAL blot analysis using biotinylated AAL and horseradish peroxidase-conjugated <t>streptavidin.</t>
    Streptavidin Horseradish Peroixidase, supplied by Biogenex, used in various techniques. Bioz Stars score: 79/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Jackson Immuno horseradish streptavidin peroxydase
    SDS-PAGE analysis of the albumin- and IgG-depleted and AAL-captured glycoproteins from the pooled serum samples of HE and patients with SCLC. A, pattern check of the albumin- and IgG-depleted human serum samples. The pooled sera from HE, LD, and ED patients were depleted of albumin and IgG using immunoaffinity columns, followed by SDS-PAGE. The purified proteins were visualized by Coomassie Brilliant Blue staining. T, total crude sera; B, albumin and IgG column-bound proteins; D, albumin- and IgG-depleted sera. The most prominent removal was observed in serum albumin (∼66 kDa), which represents ∼50% of the total protein content in crude sera. The IgG heavy chain (∼55 kDa) was also efficiently removed. B, depleted sera were enriched for fucosylated glycoproteins using AAL columns. The flow-through and the AAL-bound fucosylation enriched-proteins were visualized by Coomassie Brilliant Blue staining. Flow-through , AAL column unbound proteins; Elution , AAL column-bound proteins. C, visualization of the same samples from B was performed by AAL blot analysis using biotinylated AAL and horseradish peroxidase-conjugated <t>streptavidin.</t>
    Horseradish Streptavidin Peroxydase, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 78/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Ventana Medical streptavidin horseradish conjugate
    SDS-PAGE analysis of the albumin- and IgG-depleted and AAL-captured glycoproteins from the pooled serum samples of HE and patients with SCLC. A, pattern check of the albumin- and IgG-depleted human serum samples. The pooled sera from HE, LD, and ED patients were depleted of albumin and IgG using immunoaffinity columns, followed by SDS-PAGE. The purified proteins were visualized by Coomassie Brilliant Blue staining. T, total crude sera; B, albumin and IgG column-bound proteins; D, albumin- and IgG-depleted sera. The most prominent removal was observed in serum albumin (∼66 kDa), which represents ∼50% of the total protein content in crude sera. The IgG heavy chain (∼55 kDa) was also efficiently removed. B, depleted sera were enriched for fucosylated glycoproteins using AAL columns. The flow-through and the AAL-bound fucosylation enriched-proteins were visualized by Coomassie Brilliant Blue staining. Flow-through , AAL column unbound proteins; Elution , AAL column-bound proteins. C, visualization of the same samples from B was performed by AAL blot analysis using biotinylated AAL and horseradish peroxidase-conjugated <t>streptavidin.</t>
    Streptavidin Horseradish Conjugate, supplied by Ventana Medical, used in various techniques. Bioz Stars score: 75/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Agilent technologies streptavidin horseradish system
    SDS-PAGE analysis of the albumin- and IgG-depleted and AAL-captured glycoproteins from the pooled serum samples of HE and patients with SCLC. A, pattern check of the albumin- and IgG-depleted human serum samples. The pooled sera from HE, LD, and ED patients were depleted of albumin and IgG using immunoaffinity columns, followed by SDS-PAGE. The purified proteins were visualized by Coomassie Brilliant Blue staining. T, total crude sera; B, albumin and IgG column-bound proteins; D, albumin- and IgG-depleted sera. The most prominent removal was observed in serum albumin (∼66 kDa), which represents ∼50% of the total protein content in crude sera. The IgG heavy chain (∼55 kDa) was also efficiently removed. B, depleted sera were enriched for fucosylated glycoproteins using AAL columns. The flow-through and the AAL-bound fucosylation enriched-proteins were visualized by Coomassie Brilliant Blue staining. Flow-through , AAL column unbound proteins; Elution , AAL column-bound proteins. C, visualization of the same samples from B was performed by AAL blot analysis using biotinylated AAL and horseradish peroxidase-conjugated <t>streptavidin.</t>
    Streptavidin Horseradish System, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 78/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare streptavidin horseradish complex
    SDS-PAGE analysis of the albumin- and IgG-depleted and AAL-captured glycoproteins from the pooled serum samples of HE and patients with SCLC. A, pattern check of the albumin- and IgG-depleted human serum samples. The pooled sera from HE, LD, and ED patients were depleted of albumin and IgG using immunoaffinity columns, followed by SDS-PAGE. The purified proteins were visualized by Coomassie Brilliant Blue staining. T, total crude sera; B, albumin and IgG column-bound proteins; D, albumin- and IgG-depleted sera. The most prominent removal was observed in serum albumin (∼66 kDa), which represents ∼50% of the total protein content in crude sera. The IgG heavy chain (∼55 kDa) was also efficiently removed. B, depleted sera were enriched for fucosylated glycoproteins using AAL columns. The flow-through and the AAL-bound fucosylation enriched-proteins were visualized by Coomassie Brilliant Blue staining. Flow-through , AAL column unbound proteins; Elution , AAL column-bound proteins. C, visualization of the same samples from B was performed by AAL blot analysis using biotinylated AAL and horseradish peroxidase-conjugated <t>streptavidin.</t>
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    Agilent technologies horseradish peroxidase streptavidin
    SDS-PAGE analysis of the albumin- and IgG-depleted and AAL-captured glycoproteins from the pooled serum samples of HE and patients with SCLC. A, pattern check of the albumin- and IgG-depleted human serum samples. The pooled sera from HE, LD, and ED patients were depleted of albumin and IgG using immunoaffinity columns, followed by SDS-PAGE. The purified proteins were visualized by Coomassie Brilliant Blue staining. T, total crude sera; B, albumin and IgG column-bound proteins; D, albumin- and IgG-depleted sera. The most prominent removal was observed in serum albumin (∼66 kDa), which represents ∼50% of the total protein content in crude sera. The IgG heavy chain (∼55 kDa) was also efficiently removed. B, depleted sera were enriched for fucosylated glycoproteins using AAL columns. The flow-through and the AAL-bound fucosylation enriched-proteins were visualized by Coomassie Brilliant Blue staining. Flow-through , AAL column unbound proteins; Elution , AAL column-bound proteins. C, visualization of the same samples from B was performed by AAL blot analysis using biotinylated AAL and horseradish peroxidase-conjugated <t>streptavidin.</t>
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    Santa Cruz Biotechnology horseradish peroxidase streptavidin
    SDS-PAGE analysis of the albumin- and IgG-depleted and AAL-captured glycoproteins from the pooled serum samples of HE and patients with SCLC. A, pattern check of the albumin- and IgG-depleted human serum samples. The pooled sera from HE, LD, and ED patients were depleted of albumin and IgG using immunoaffinity columns, followed by SDS-PAGE. The purified proteins were visualized by Coomassie Brilliant Blue staining. T, total crude sera; B, albumin and IgG column-bound proteins; D, albumin- and IgG-depleted sera. The most prominent removal was observed in serum albumin (∼66 kDa), which represents ∼50% of the total protein content in crude sera. The IgG heavy chain (∼55 kDa) was also efficiently removed. B, depleted sera were enriched for fucosylated glycoproteins using AAL columns. The flow-through and the AAL-bound fucosylation enriched-proteins were visualized by Coomassie Brilliant Blue staining. Flow-through , AAL column unbound proteins; Elution , AAL column-bound proteins. C, visualization of the same samples from B was performed by AAL blot analysis using biotinylated AAL and horseradish peroxidase-conjugated <t>streptavidin.</t>
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    GE Healthcare horseradish peroxidase streptavidin
    Coimmunoprecipitation of HA-SH3p4 and Flag-β1-adrenergic receptor from HEK293 cells. pcDNA3 Flag-β1-AR ( Left ) or pcDNA3 Flag-β2-AR ( Right ) were transiently transfected into HEK293 cells in the absence or presence of pcDNA3 HA-SH3p4 or pcDNA3 HA-SH3p4 ΔSH3. Nonstimulated cells and cells stimulated with 10 μM isoproterenol for various periods of time were lysed in digitonin buffer. Flag-β1-AR was immunoprecipitated with M2 anti-Flag affinity gel from samples containing equal amounts of protein. Immunoprecipitates were subjected to SDS/PAGE and Western blot analysis. The blot was initially probed with anti-HA rabbit polyclonal antibody to detect HA-SH3p4 and HA-SH3p4 ΔSH3. The blot was subsequently stripped and reprobed with biotinylated-M2 anti-Flag antibody and <t>streptavidin/horseradish</t> peroxidase conjugates to detect Flag-βAR. Overexpression of HA-SH3p4 or HA-SH3p4ΔSH3 in whole cell lysate also was monitored. The experiment was repeated at least three times with similar results. The diffuse doublet of both Flag-β1-AR and Flag-β2-AR in the middle panel likely represents differentially glycosylated forms of these receptors.
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    The Jackson Laboratory horseradish peroxidase streptavidin
    Coimmunoprecipitation of HA-SH3p4 and Flag-β1-adrenergic receptor from HEK293 cells. pcDNA3 Flag-β1-AR ( Left ) or pcDNA3 Flag-β2-AR ( Right ) were transiently transfected into HEK293 cells in the absence or presence of pcDNA3 HA-SH3p4 or pcDNA3 HA-SH3p4 ΔSH3. Nonstimulated cells and cells stimulated with 10 μM isoproterenol for various periods of time were lysed in digitonin buffer. Flag-β1-AR was immunoprecipitated with M2 anti-Flag affinity gel from samples containing equal amounts of protein. Immunoprecipitates were subjected to SDS/PAGE and Western blot analysis. The blot was initially probed with anti-HA rabbit polyclonal antibody to detect HA-SH3p4 and HA-SH3p4 ΔSH3. The blot was subsequently stripped and reprobed with biotinylated-M2 anti-Flag antibody and <t>streptavidin/horseradish</t> peroxidase conjugates to detect Flag-βAR. Overexpression of HA-SH3p4 or HA-SH3p4ΔSH3 in whole cell lysate also was monitored. The experiment was repeated at least three times with similar results. The diffuse doublet of both Flag-β1-AR and Flag-β2-AR in the middle panel likely represents differentially glycosylated forms of these receptors.
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    R&D Systems streptavidin horseradish peroxydase
    Coimmunoprecipitation of HA-SH3p4 and Flag-β1-adrenergic receptor from HEK293 cells. pcDNA3 Flag-β1-AR ( Left ) or pcDNA3 Flag-β2-AR ( Right ) were transiently transfected into HEK293 cells in the absence or presence of pcDNA3 HA-SH3p4 or pcDNA3 HA-SH3p4 ΔSH3. Nonstimulated cells and cells stimulated with 10 μM isoproterenol for various periods of time were lysed in digitonin buffer. Flag-β1-AR was immunoprecipitated with M2 anti-Flag affinity gel from samples containing equal amounts of protein. Immunoprecipitates were subjected to SDS/PAGE and Western blot analysis. The blot was initially probed with anti-HA rabbit polyclonal antibody to detect HA-SH3p4 and HA-SH3p4 ΔSH3. The blot was subsequently stripped and reprobed with biotinylated-M2 anti-Flag antibody and <t>streptavidin/horseradish</t> peroxidase conjugates to detect Flag-βAR. Overexpression of HA-SH3p4 or HA-SH3p4ΔSH3 in whole cell lysate also was monitored. The experiment was repeated at least three times with similar results. The diffuse doublet of both Flag-β1-AR and Flag-β2-AR in the middle panel likely represents differentially glycosylated forms of these receptors.
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    Boster Bio horseradish peroxidase streptavidin
    Coimmunoprecipitation of HA-SH3p4 and Flag-β1-adrenergic receptor from HEK293 cells. pcDNA3 Flag-β1-AR ( Left ) or pcDNA3 Flag-β2-AR ( Right ) were transiently transfected into HEK293 cells in the absence or presence of pcDNA3 HA-SH3p4 or pcDNA3 HA-SH3p4 ΔSH3. Nonstimulated cells and cells stimulated with 10 μM isoproterenol for various periods of time were lysed in digitonin buffer. Flag-β1-AR was immunoprecipitated with M2 anti-Flag affinity gel from samples containing equal amounts of protein. Immunoprecipitates were subjected to SDS/PAGE and Western blot analysis. The blot was initially probed with anti-HA rabbit polyclonal antibody to detect HA-SH3p4 and HA-SH3p4 ΔSH3. The blot was subsequently stripped and reprobed with biotinylated-M2 anti-Flag antibody and <t>streptavidin/horseradish</t> peroxidase conjugates to detect Flag-βAR. Overexpression of HA-SH3p4 or HA-SH3p4ΔSH3 in whole cell lysate also was monitored. The experiment was repeated at least three times with similar results. The diffuse doublet of both Flag-β1-AR and Flag-β2-AR in the middle panel likely represents differentially glycosylated forms of these receptors.
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    Maixin-Bio horseradish peroxidase streptavidin
    Coimmunoprecipitation of HA-SH3p4 and Flag-β1-adrenergic receptor from HEK293 cells. pcDNA3 Flag-β1-AR ( Left ) or pcDNA3 Flag-β2-AR ( Right ) were transiently transfected into HEK293 cells in the absence or presence of pcDNA3 HA-SH3p4 or pcDNA3 HA-SH3p4 ΔSH3. Nonstimulated cells and cells stimulated with 10 μM isoproterenol for various periods of time were lysed in digitonin buffer. Flag-β1-AR was immunoprecipitated with M2 anti-Flag affinity gel from samples containing equal amounts of protein. Immunoprecipitates were subjected to SDS/PAGE and Western blot analysis. The blot was initially probed with anti-HA rabbit polyclonal antibody to detect HA-SH3p4 and HA-SH3p4 ΔSH3. The blot was subsequently stripped and reprobed with biotinylated-M2 anti-Flag antibody and <t>streptavidin/horseradish</t> peroxidase conjugates to detect Flag-βAR. Overexpression of HA-SH3p4 or HA-SH3p4ΔSH3 in whole cell lysate also was monitored. The experiment was repeated at least three times with similar results. The diffuse doublet of both Flag-β1-AR and Flag-β2-AR in the middle panel likely represents differentially glycosylated forms of these receptors.
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    OriGene horseradish peroxidase streptavidin
    Coimmunoprecipitation of HA-SH3p4 and Flag-β1-adrenergic receptor from HEK293 cells. pcDNA3 Flag-β1-AR ( Left ) or pcDNA3 Flag-β2-AR ( Right ) were transiently transfected into HEK293 cells in the absence or presence of pcDNA3 HA-SH3p4 or pcDNA3 HA-SH3p4 ΔSH3. Nonstimulated cells and cells stimulated with 10 μM isoproterenol for various periods of time were lysed in digitonin buffer. Flag-β1-AR was immunoprecipitated with M2 anti-Flag affinity gel from samples containing equal amounts of protein. Immunoprecipitates were subjected to SDS/PAGE and Western blot analysis. The blot was initially probed with anti-HA rabbit polyclonal antibody to detect HA-SH3p4 and HA-SH3p4 ΔSH3. The blot was subsequently stripped and reprobed with biotinylated-M2 anti-Flag antibody and <t>streptavidin/horseradish</t> peroxidase conjugates to detect Flag-βAR. Overexpression of HA-SH3p4 or HA-SH3p4ΔSH3 in whole cell lysate also was monitored. The experiment was repeated at least three times with similar results. The diffuse doublet of both Flag-β1-AR and Flag-β2-AR in the middle panel likely represents differentially glycosylated forms of these receptors.
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    Image Search Results


    Proximity Utilizing Biotinylation (PUB) allows for detection of nuclear envelope-proximal regions on mitotic chromosomes. ( A ) The Proximity Utilizing Biotinylation principle. The PUB approach is based on coexpression of protein X fused to biotin ligase (BirA) and protein Y fused to biotin acceptor peptide (BAP). When the proteins are in sufficient proximity or interact with each other in cells harboring the corresponding plasmids, in the presence of biotin (pink), BirA specifically biotinylates the BAP peptide, resulting in a persistent label on the BAP-carrying protein. ( B ) Emerin is localized at the NE. 293T cells were transfected with emerin-GFP (green) and stained with DAPI (blue). Scale bar: 10 μm. ( C ) Biotinylation of NE proximal chromatin using BirA-emerin fusion. 293T cells were transfected with BirA-emerin and BAP-H2A or BAP-H3.1, followed by biotin pulse labeling and counterstaining with streptavidin-Cy3 (red) and DAPI (blue). Scale bar: 10 μm. ( D ) The biotin label depends on BAP-histone biotinylation. Western blot analysis was performed on nuclei from control (untransfected) and transfected 293T cells using anti-His-HRP (left) or streptavidin-HRP (right). The bands corresponding to BAP-histones, biotinylated BAP-histones, the ubiquitinated form of BAP-H2A (Ub-BAP-H2A) and non-specific signals (NS) are indicated. ( E ) PUB pulse and chase principle. BirA is fused to a nuclear envelope (NE) protein and BAP to a histone resulting in biotin labeling of chromatin proximal to the NE during interphase. The resulting biotin signals appear as bands on mitotic chromosomes. ( F ) PUB pulse and chase experiment. Interphase 293T cells coexpressing BirA-emerin and BAP-H2A are biotin pulse labeled followed by streptavidin-Cy3 (red) and DAPI (blue) staining (top). After 4 h chase, biotin signal was revealed on mitotic chromosomes using the same staining dies as previously described (bottom). Scale bar: 10 μm.

    Journal: Nucleic Acids Research

    Article Title: Topokaryotyping demonstrates single cell variability and stress dependent variations in nuclear envelope associated domains

    doi: 10.1093/nar/gky818

    Figure Lengend Snippet: Proximity Utilizing Biotinylation (PUB) allows for detection of nuclear envelope-proximal regions on mitotic chromosomes. ( A ) The Proximity Utilizing Biotinylation principle. The PUB approach is based on coexpression of protein X fused to biotin ligase (BirA) and protein Y fused to biotin acceptor peptide (BAP). When the proteins are in sufficient proximity or interact with each other in cells harboring the corresponding plasmids, in the presence of biotin (pink), BirA specifically biotinylates the BAP peptide, resulting in a persistent label on the BAP-carrying protein. ( B ) Emerin is localized at the NE. 293T cells were transfected with emerin-GFP (green) and stained with DAPI (blue). Scale bar: 10 μm. ( C ) Biotinylation of NE proximal chromatin using BirA-emerin fusion. 293T cells were transfected with BirA-emerin and BAP-H2A or BAP-H3.1, followed by biotin pulse labeling and counterstaining with streptavidin-Cy3 (red) and DAPI (blue). Scale bar: 10 μm. ( D ) The biotin label depends on BAP-histone biotinylation. Western blot analysis was performed on nuclei from control (untransfected) and transfected 293T cells using anti-His-HRP (left) or streptavidin-HRP (right). The bands corresponding to BAP-histones, biotinylated BAP-histones, the ubiquitinated form of BAP-H2A (Ub-BAP-H2A) and non-specific signals (NS) are indicated. ( E ) PUB pulse and chase principle. BirA is fused to a nuclear envelope (NE) protein and BAP to a histone resulting in biotin labeling of chromatin proximal to the NE during interphase. The resulting biotin signals appear as bands on mitotic chromosomes. ( F ) PUB pulse and chase experiment. Interphase 293T cells coexpressing BirA-emerin and BAP-H2A are biotin pulse labeled followed by streptavidin-Cy3 (red) and DAPI (blue) staining (top). After 4 h chase, biotin signal was revealed on mitotic chromosomes using the same staining dies as previously described (bottom). Scale bar: 10 μm.

    Article Snippet: Expression of the BAP-tagged proteins was detected with an HRP-conjugated anti-polyHistidine antibody at 1:4000 (Sigma A7058) and biotinylated proteins were visualized with an HRP-conjugated streptavidin at 1:1000 (Sigma S2438).

    Techniques: Transfection, Staining, Labeling, Western Blot

    Western blot results of Avi-Tag SH2 domain proteins using an streptavidin-HRP conjugate to detect the presence of biotin. DOI: http://dx.doi.org/10.7554/eLife.24903.005

    Journal: eLife

    Article Title: Affimer proteins are versatile and renewable affinity reagents

    doi: 10.7554/eLife.24903

    Figure Lengend Snippet: Western blot results of Avi-Tag SH2 domain proteins using an streptavidin-HRP conjugate to detect the presence of biotin. DOI: http://dx.doi.org/10.7554/eLife.24903.005

    Article Snippet: Sections were then washed in TBS-T and bound Affimer was visualized using Streptavidin/HRP (1:300, 30 min, SA-5004;, Vector Laboratories Ltd, Peterborough, UK) with 3,3′-diaminobenzidine (DAB) as substrate (SK41-05; ImmPACT DAB, Vector Laboratories Ltd, Peterborough, UK).

    Techniques: Western Blot

    Target-selective protein labelling with LDNASA chemistry. a Western blotting analysis of FKBP12 labelling in cell lysates. HeLa cell lysate was mixed with recombinant FKBP12 (1 µM) and incubated with reagent in 50 mM HEPES buffer, pH 7.2, 37 °C, 1 h. SAv-HRP, streptavidin–horseradish peroxidase conjugate; CBB, Coomassie brilliant blue staining. The high background (smear) signals of lane 6 and 7 may suggest unspecific labelling due to a high concentration of reagent (20 µM), whereas such background signals were less in lanes 1–5 (1–5 µM of reagent). b Western blotting analysis of endogenous FKBP12 labelling in live C2C12 cells. The cells were treated with 1 or 5 (1 µM) for 0–120 min at 37 °C in medium. c Time course plot of the endogenous FKBP12 labelling with 1 . d Molecular structures of LDNASA 9 and LDAI 10 for FR labelling. e In-gel fluorescence and western blotting analysis of endogenous FR labelling in KB cells. The cells were treated with 9 or 10 (1 µM) for 0–60 min at 37 °C in medium. FA, Folic acid (competitive inhibitor). f Time profile of the endogenous FR labelling with 9 . I and I 30 min are band intensities of Oregon Green-labelled FR at the indicated time point and at 30 min, respectively. Error bars represent s.d., n = 3

    Journal: Nature Communications

    Article Title: Rapid labelling and covalent inhibition of intracellular native proteins using ligand-directed N-acyl-N-alkyl sulfonamide

    doi: 10.1038/s41467-018-04343-0

    Figure Lengend Snippet: Target-selective protein labelling with LDNASA chemistry. a Western blotting analysis of FKBP12 labelling in cell lysates. HeLa cell lysate was mixed with recombinant FKBP12 (1 µM) and incubated with reagent in 50 mM HEPES buffer, pH 7.2, 37 °C, 1 h. SAv-HRP, streptavidin–horseradish peroxidase conjugate; CBB, Coomassie brilliant blue staining. The high background (smear) signals of lane 6 and 7 may suggest unspecific labelling due to a high concentration of reagent (20 µM), whereas such background signals were less in lanes 1–5 (1–5 µM of reagent). b Western blotting analysis of endogenous FKBP12 labelling in live C2C12 cells. The cells were treated with 1 or 5 (1 µM) for 0–120 min at 37 °C in medium. c Time course plot of the endogenous FKBP12 labelling with 1 . d Molecular structures of LDNASA 9 and LDAI 10 for FR labelling. e In-gel fluorescence and western blotting analysis of endogenous FR labelling in KB cells. The cells were treated with 9 or 10 (1 µM) for 0–60 min at 37 °C in medium. FA, Folic acid (competitive inhibitor). f Time profile of the endogenous FR labelling with 9 . I and I 30 min are band intensities of Oregon Green-labelled FR at the indicated time point and at 30 min, respectively. Error bars represent s.d., n = 3

    Article Snippet: The samples were analysed by western blotting using Streptavidin-HRP conjugate (SAv-HRP, Thermo, S911, 1:5000) and Coomassie Brilliant Blue (CBB) stain.

    Techniques: Western Blot, Recombinant, Incubation, Staining, Concentration Assay, Fluorescence

    Expression of protocadherins. GFP was electroporated alone or in combination with protocadherins into K562 cells. a Immunoblotting of cell lysates with anti-GFP shows bands compatible with the expected molecular weights for GFP (27 kDa) and mature PCDHB11-GFP (110 kDa); image representative of three transfections. b Immunoblotting of cell lysates with anti-HA shows bands compatible with the expected molecular weights for mature HA-PCDHB11-GFP (113 kDa) and HA-PCDHGA3 (99 kDa); image representative of two transfections. c Proportion of medium and large clusters was lower in HA-PCDHB11-GFP-transfected than in HA-PCDHGA3-transfected cells, but higher than in control cells ( n = 10-12 images per condition). d Proportion of medium to large cell clusters when normalized by HA-PCDHGA3. For visualization of surface protocadherins, live cells transfected with GFP alone (e) or in combination with HA-PCDHB11-GFP (f) or HA-PCDHGA3 (g) were stained with anti-HA-biotin and streptavidin-Alexa555, then fixed. Blue: DAPI. Green: GFP. Red: surface HA-tagged protocadherins. Scale bar: 10 μm

    Journal: BMC Evolutionary Biology

    Article Title: Functional test of PCDHB11, the most human-specific neuronal surface protein

    doi: 10.1186/s12862-016-0652-x

    Figure Lengend Snippet: Expression of protocadherins. GFP was electroporated alone or in combination with protocadherins into K562 cells. a Immunoblotting of cell lysates with anti-GFP shows bands compatible with the expected molecular weights for GFP (27 kDa) and mature PCDHB11-GFP (110 kDa); image representative of three transfections. b Immunoblotting of cell lysates with anti-HA shows bands compatible with the expected molecular weights for mature HA-PCDHB11-GFP (113 kDa) and HA-PCDHGA3 (99 kDa); image representative of two transfections. c Proportion of medium and large clusters was lower in HA-PCDHB11-GFP-transfected than in HA-PCDHGA3-transfected cells, but higher than in control cells ( n = 10-12 images per condition). d Proportion of medium to large cell clusters when normalized by HA-PCDHGA3. For visualization of surface protocadherins, live cells transfected with GFP alone (e) or in combination with HA-PCDHB11-GFP (f) or HA-PCDHGA3 (g) were stained with anti-HA-biotin and streptavidin-Alexa555, then fixed. Blue: DAPI. Green: GFP. Red: surface HA-tagged protocadherins. Scale bar: 10 μm

    Article Snippet: For GFP detection, membranes were incubated with a rabbit polyclonal antibody (Life Technologies, A-11122) diluted 1:2000 in 50 mM Tris, 100 mM NaCl, 0.1 % Tween 20, pH 7.4, with 3 % bovine serum albumine (Sigma, St. Louis, MO) and a horse-radish peroxidase-conjugated anti-rabbit secondary antibody (Invitrogen, Waltham, MA), while for HA revelation, they were incubated with biotinylated 3 F10 rat monoclonal antibody (Roche Life Science, Indianapolis, IN) diluted 1:500 in the same buffer, and streptavidin-horseradish peroxidase (Invitrogen, Waltham, MA).

    Techniques: Expressing, Transfection, Staining

    Target-selective protein labelling with LDNASA chemistry. a Western blotting analysis of FKBP12 labelling in cell lysates. HeLa cell lysate was mixed with recombinant FKBP12 (1 µM) and incubated with reagent in 50 mM HEPES buffer, pH 7.2, 37 °C, 1 h. SAv-HRP, streptavidin–horseradish peroxidase conjugate; CBB, Coomassie brilliant blue staining. The high background (smear) signals of lane 6 and 7 may suggest unspecific labelling due to a high concentration of reagent (20 µM), whereas such background signals were less in lanes 1–5 (1–5 µM of reagent). b Western blotting analysis of endogenous FKBP12 labelling in live C2C12 cells. The cells were treated with 1 or 5 (1 µM) for 0–120 min at 37 °C in medium. c Time course plot of the endogenous FKBP12 labelling with 1 . d Molecular structures of LDNASA 9 and LDAI 10 for FR labelling. e In-gel fluorescence and western blotting analysis of endogenous FR labelling in KB cells. The cells were treated with 9 or 10 (1 µM) for 0–60 min at 37 °C in medium. FA, Folic acid (competitive inhibitor). f Time profile of the endogenous FR labelling with 9 . I and I 30 min are band intensities of Oregon Green-labelled FR at the indicated time point and at 30 min, respectively. Error bars represent s.d., n = 3

    Journal: Nature Communications

    Article Title: Rapid labelling and covalent inhibition of intracellular native proteins using ligand-directed N-acyl-N-alkyl sulfonamide

    doi: 10.1038/s41467-018-04343-0

    Figure Lengend Snippet: Target-selective protein labelling with LDNASA chemistry. a Western blotting analysis of FKBP12 labelling in cell lysates. HeLa cell lysate was mixed with recombinant FKBP12 (1 µM) and incubated with reagent in 50 mM HEPES buffer, pH 7.2, 37 °C, 1 h. SAv-HRP, streptavidin–horseradish peroxidase conjugate; CBB, Coomassie brilliant blue staining. The high background (smear) signals of lane 6 and 7 may suggest unspecific labelling due to a high concentration of reagent (20 µM), whereas such background signals were less in lanes 1–5 (1–5 µM of reagent). b Western blotting analysis of endogenous FKBP12 labelling in live C2C12 cells. The cells were treated with 1 or 5 (1 µM) for 0–120 min at 37 °C in medium. c Time course plot of the endogenous FKBP12 labelling with 1 . d Molecular structures of LDNASA 9 and LDAI 10 for FR labelling. e In-gel fluorescence and western blotting analysis of endogenous FR labelling in KB cells. The cells were treated with 9 or 10 (1 µM) for 0–60 min at 37 °C in medium. FA, Folic acid (competitive inhibitor). f Time profile of the endogenous FR labelling with 9 . I and I 30 min are band intensities of Oregon Green-labelled FR at the indicated time point and at 30 min, respectively. Error bars represent s.d., n = 3

    Article Snippet: The labelled FKBP12 was detected by chemiluminescence analysis using Streptavidin-HRP conjugate, rabbit anti-FKBP12 antibody (Abcam, ab2918, 1:1000) and anti-rabbit IgG-HRP conjugate (CST, #7074 S, 1:5000).

    Techniques: Western Blot, Recombinant, Incubation, Staining, Concentration Assay, Fluorescence

    SDS-PAGE analysis of the albumin- and IgG-depleted and AAL-captured glycoproteins from the pooled serum samples of HE and patients with SCLC. A, pattern check of the albumin- and IgG-depleted human serum samples. The pooled sera from HE, LD, and ED patients were depleted of albumin and IgG using immunoaffinity columns, followed by SDS-PAGE. The purified proteins were visualized by Coomassie Brilliant Blue staining. T, total crude sera; B, albumin and IgG column-bound proteins; D, albumin- and IgG-depleted sera. The most prominent removal was observed in serum albumin (∼66 kDa), which represents ∼50% of the total protein content in crude sera. The IgG heavy chain (∼55 kDa) was also efficiently removed. B, depleted sera were enriched for fucosylated glycoproteins using AAL columns. The flow-through and the AAL-bound fucosylation enriched-proteins were visualized by Coomassie Brilliant Blue staining. Flow-through , AAL column unbound proteins; Elution , AAL column-bound proteins. C, visualization of the same samples from B was performed by AAL blot analysis using biotinylated AAL and horseradish peroxidase-conjugated streptavidin.

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title: Integrated Glycoproteomics Demonstrates Fucosylated Serum Paraoxonase 1 Alterations in Small Cell Lung Cancer *

    doi: 10.1074/mcp.M113.028621

    Figure Lengend Snippet: SDS-PAGE analysis of the albumin- and IgG-depleted and AAL-captured glycoproteins from the pooled serum samples of HE and patients with SCLC. A, pattern check of the albumin- and IgG-depleted human serum samples. The pooled sera from HE, LD, and ED patients were depleted of albumin and IgG using immunoaffinity columns, followed by SDS-PAGE. The purified proteins were visualized by Coomassie Brilliant Blue staining. T, total crude sera; B, albumin and IgG column-bound proteins; D, albumin- and IgG-depleted sera. The most prominent removal was observed in serum albumin (∼66 kDa), which represents ∼50% of the total protein content in crude sera. The IgG heavy chain (∼55 kDa) was also efficiently removed. B, depleted sera were enriched for fucosylated glycoproteins using AAL columns. The flow-through and the AAL-bound fucosylation enriched-proteins were visualized by Coomassie Brilliant Blue staining. Flow-through , AAL column unbound proteins; Elution , AAL column-bound proteins. C, visualization of the same samples from B was performed by AAL blot analysis using biotinylated AAL and horseradish peroxidase-conjugated streptavidin.

    Article Snippet: The membranes were blocked with phosphate-buffered saline (PBS) containing 3% bovine serum albumin (BSA) at 4 °C overnight and then incubated with biotinylated AAL (1.0 μg/μl; Vector Laboratories) at RT for 1 h. Next, the membranes were washed three times with Tris-buffered saline/Tween 20 (TBS-T), incubated with diluted horseradish peroxidase/streptavidin (Biolegend, CA) at RT for 1 h, washed three additional times with TBS-T, and developed using an ECL system (Amersham Biosciences).

    Techniques: SDS Page, Purification, Staining, Flow Cytometry

    PON1 protein in the sera of the patients with SCLC is highly reactive with fucose-binding lectin. A, serum samples treated with or without PNGase F were analyzed by immunoblotting using a PON1 antibody. The PNGase F treatment reduced the size of the PON1 protein, indicating that the PON1 protein was N -linked glycosylated. Crude , five pooled HE crude sera; −, PNGase F-untreated crude sample; +, PNGase F-treated crude sample. B, comparison of the fucosylation levels of PON1 in the HE, LD, and ED samples. Upper panel, after the immunoprecipitation and purification of PON1 from the depleted serum samples, the same volumes of eluted protein were subjected to SDS-PAGE (12% gel), followed by Western blotting analysis using anti-PON1 antibody. Lower panel, reblotting of the same membrane using biotinylated AAL, followed by HRP-conjugated streptavidin for the detection of the levels of fucosylated PON1 protein.

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title: Integrated Glycoproteomics Demonstrates Fucosylated Serum Paraoxonase 1 Alterations in Small Cell Lung Cancer *

    doi: 10.1074/mcp.M113.028621

    Figure Lengend Snippet: PON1 protein in the sera of the patients with SCLC is highly reactive with fucose-binding lectin. A, serum samples treated with or without PNGase F were analyzed by immunoblotting using a PON1 antibody. The PNGase F treatment reduced the size of the PON1 protein, indicating that the PON1 protein was N -linked glycosylated. Crude , five pooled HE crude sera; −, PNGase F-untreated crude sample; +, PNGase F-treated crude sample. B, comparison of the fucosylation levels of PON1 in the HE, LD, and ED samples. Upper panel, after the immunoprecipitation and purification of PON1 from the depleted serum samples, the same volumes of eluted protein were subjected to SDS-PAGE (12% gel), followed by Western blotting analysis using anti-PON1 antibody. Lower panel, reblotting of the same membrane using biotinylated AAL, followed by HRP-conjugated streptavidin for the detection of the levels of fucosylated PON1 protein.

    Article Snippet: The membranes were blocked with phosphate-buffered saline (PBS) containing 3% bovine serum albumin (BSA) at 4 °C overnight and then incubated with biotinylated AAL (1.0 μg/μl; Vector Laboratories) at RT for 1 h. Next, the membranes were washed three times with Tris-buffered saline/Tween 20 (TBS-T), incubated with diluted horseradish peroxidase/streptavidin (Biolegend, CA) at RT for 1 h, washed three additional times with TBS-T, and developed using an ECL system (Amersham Biosciences).

    Techniques: Binding Assay, Immunoprecipitation, Purification, SDS Page, Western Blot

    Coimmunoprecipitation of HA-SH3p4 and Flag-β1-adrenergic receptor from HEK293 cells. pcDNA3 Flag-β1-AR ( Left ) or pcDNA3 Flag-β2-AR ( Right ) were transiently transfected into HEK293 cells in the absence or presence of pcDNA3 HA-SH3p4 or pcDNA3 HA-SH3p4 ΔSH3. Nonstimulated cells and cells stimulated with 10 μM isoproterenol for various periods of time were lysed in digitonin buffer. Flag-β1-AR was immunoprecipitated with M2 anti-Flag affinity gel from samples containing equal amounts of protein. Immunoprecipitates were subjected to SDS/PAGE and Western blot analysis. The blot was initially probed with anti-HA rabbit polyclonal antibody to detect HA-SH3p4 and HA-SH3p4 ΔSH3. The blot was subsequently stripped and reprobed with biotinylated-M2 anti-Flag antibody and streptavidin/horseradish peroxidase conjugates to detect Flag-βAR. Overexpression of HA-SH3p4 or HA-SH3p4ΔSH3 in whole cell lysate also was monitored. The experiment was repeated at least three times with similar results. The diffuse doublet of both Flag-β1-AR and Flag-β2-AR in the middle panel likely represents differentially glycosylated forms of these receptors.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Identification of the endophilins (SH3p4/p8/p13) as novel binding partners for the ?1-adrenergic receptor

    doi:

    Figure Lengend Snippet: Coimmunoprecipitation of HA-SH3p4 and Flag-β1-adrenergic receptor from HEK293 cells. pcDNA3 Flag-β1-AR ( Left ) or pcDNA3 Flag-β2-AR ( Right ) were transiently transfected into HEK293 cells in the absence or presence of pcDNA3 HA-SH3p4 or pcDNA3 HA-SH3p4 ΔSH3. Nonstimulated cells and cells stimulated with 10 μM isoproterenol for various periods of time were lysed in digitonin buffer. Flag-β1-AR was immunoprecipitated with M2 anti-Flag affinity gel from samples containing equal amounts of protein. Immunoprecipitates were subjected to SDS/PAGE and Western blot analysis. The blot was initially probed with anti-HA rabbit polyclonal antibody to detect HA-SH3p4 and HA-SH3p4 ΔSH3. The blot was subsequently stripped and reprobed with biotinylated-M2 anti-Flag antibody and streptavidin/horseradish peroxidase conjugates to detect Flag-βAR. Overexpression of HA-SH3p4 or HA-SH3p4ΔSH3 in whole cell lysate also was monitored. The experiment was repeated at least three times with similar results. The diffuse doublet of both Flag-β1-AR and Flag-β2-AR in the middle panel likely represents differentially glycosylated forms of these receptors.

    Article Snippet: Streptavidin horseradish peroxidase, anti-mouse horseradish peroxidase, and anti-rabbit horseradish peroxidase were obtained from Amersham Pharmacia.

    Techniques: Transfection, Immunoprecipitation, SDS Page, Western Blot, Over Expression