horseradish peroxidase hrp Search Results


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  • 99
    Thermo Fisher horseradish peroxidase hrp
    Caveolin-1 interacts with the RSV G and M protein complex on the surface of infected cells. (A) Immunoprecipitations of RSV G, M and M2-1 proteins from HeLa whole-cell lysates of mock-infected or RSV-infected cells (22 hpi). Immunoprecipitates were probed for G protein (top panel), M protein (middle panel) and caveolin-1 (bottom panel). Caveolin-1 protein was measured by densitometry (bottom graph). (B) <t>Streptavidin–HRP</t> blot of lysates of surface-biotinylated HeLa cells. M, mock infected; I, RSV infected. (C) Streptavidin–HRP blot of immunoprecipitates from lysates shown in B, using antibodies against RSV G protein or caveolin-1. Representative data of two independent experiments are shown.
    Horseradish Peroxidase Hrp, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 2896 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Jackson Immuno horseradish peroxidase hrp
    Western blot analysis of eight CHO-S clones demonstrated various levels of scFv-QuVHVL expression. The blot was probed for 6xHis tagged protein with a mouse anti-6xHis mAb followed by goat anti-mouse <t>IgG-HRP.</t> The target protein was a ∼30kD protein.
    Horseradish Peroxidase Hrp, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 93/100, based on 903 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam horseradish peroxidase hrp
    The reactivity in the ELISA test of <t>polyclonal</t> anti- Escherichia coli antibody conjugated with <t>HRP</t> (1:2000) with Escherichia coli strains: 056, K12, 0111, 024, 104, B, and Lactobacillus rhamnosus LOCK 0919 (919). L-0.25 mg of lyophilized bacterial mass/1 mL of PBS; 10 8 CFU/mL, 10 7 CFU/mL, 10 6 CFU/mL of alive bacterial culture in PBS. Pooled results from three independent experiments are shown. *, P
    Horseradish Peroxidase Hrp, supplied by Abcam, used in various techniques. Bioz Stars score: 93/100, based on 689 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Promega horseradish peroxidase hrp
    TLF2 is a protein complex. One microgram of TLF2 was immunoprecipitated by antibodies to human Hp (MAb; α-Hp), human apoA-I (polyclonal antibodies from sheep and goat; α-apoA-I), and human IgM (MAb; α-IgM). Following immunoprecipitation, the pellet (P) and supernatant (S) were separated by reducing SDS-PAGE (12% gel) and transferred to PVDF membranes. The IgM μ chain was detected with rabbit anti-IgM μ-chain antibody followed by goat anti-rabbit <t>IgG-HRP</t> and exposed for 30 s by ECL.
    Horseradish Peroxidase Hrp, supplied by Promega, used in various techniques. Bioz Stars score: 99/100, based on 190 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Rockland Immunochemicals horseradish peroxidase hrp
    PrP C expression levels in uninfected N2a cells treated with the 16 validated antiprion compounds at the indicated concentrations for 5 days. Conjugated <t>D13-HRP</t> was used to detect PrP in Western immunoblots. Lane numbers correspond to compound IDs in
    Horseradish Peroxidase Hrp, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 92/100, based on 69 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    GE Healthcare horseradish peroxidase hrp
    Isolation of MIP from phage-displayed combinatorial peptide library. ), a single peptide ligand, MIP (NH 2 -AIRINPNGTWSRQAETVES-COOH; insert (underlined) and flanking region), was identified to bind a <t>GST-MLK3</t> SH3 domain fusion protein. ELISA shows the phage-displayed MIP to bind to the WT form of the MLK3 SH3 domain (SH3 WT) but not the GST fusion partner. The presence of virions in the supernatant was determined by coating the wells of the microtiter plate with an anti-M13 mAb ( anti-M13 Ab ). Virions, which were retained in the microtiter plate wells, were detected with anti-M13 mAb conjugated to <t>HRP.</t> Experiments were performed in duplicate, and the results are an averaged value; error bars .
    Horseradish Peroxidase Hrp, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 94/100, based on 2176 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology horseradish peroxidase hrp
    SmpB-SsrA Mediated Protein Tagging Activity Is Observed in Y. pseudotuberculosis (A) Schematic representation of the λ-cI-N-trpAt reporter construct encoded on the pKW540 plasmid and anticipated outcomes of protein tagging in wild-type (WT) or ΔBA strains. (B) The λ-cI-N-trpAt reporter was induced in wild-type and mutant (ΔBA) strains, and protein samples were analyzed by Western blot using <t>HRP-conjugated</t> <t>anti-H6</t> serum. MW stds, protein molecular weight standards.
    Horseradish Peroxidase Hrp, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 2165 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Beyotime horseradish peroxidase hrp
    SmpB-SsrA Mediated Protein Tagging Activity Is Observed in Y. pseudotuberculosis (A) Schematic representation of the λ-cI-N-trpAt reporter construct encoded on the pKW540 plasmid and anticipated outcomes of protein tagging in wild-type (WT) or ΔBA strains. (B) The λ-cI-N-trpAt reporter was induced in wild-type and mutant (ΔBA) strains, and protein samples were analyzed by Western blot using <t>HRP-conjugated</t> <t>anti-H6</t> serum. MW stds, protein molecular weight standards.
    Horseradish Peroxidase Hrp, supplied by Beyotime, used in various techniques. Bioz Stars score: 92/100, based on 267 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    SouthernBiotech horseradish peroxidase hrp
    Specific binding of HBcAg VLP-displayed zDIII by monoclonal antibodies that recognize EDIII conformational epitopes. Serial dilutions of ZV54 and E16 mAbs that recognize a lateral ridge conformational epitope on EDIII of ZIKV and WNV, respectively, were incubated in microtiter wells coated with HBcAg-zDIII VLPs and detected with an <t>HRP-conjugated</t> goat anti-mouse <t>IgG</t> antibody. 6D8: an anti-Ebola isotype negative control mAb. Mean ± SD of samples from three independent experiments is presented.
    Horseradish Peroxidase Hrp, supplied by SouthernBiotech, used in various techniques. Bioz Stars score: 92/100, based on 359 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Becton Dickinson horseradish peroxidase hrp
    Specific binding of HBcAg VLP-displayed zDIII by monoclonal antibodies that recognize EDIII conformational epitopes. Serial dilutions of ZV54 and E16 mAbs that recognize a lateral ridge conformational epitope on EDIII of ZIKV and WNV, respectively, were incubated in microtiter wells coated with HBcAg-zDIII VLPs and detected with an <t>HRP-conjugated</t> goat anti-mouse <t>IgG</t> antibody. 6D8: an anti-Ebola isotype negative control mAb. Mean ± SD of samples from three independent experiments is presented.
    Horseradish Peroxidase Hrp, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 92/100, based on 134 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Proteintech horseradish peroxidase hrp
    Specific binding of HBcAg VLP-displayed zDIII by monoclonal antibodies that recognize EDIII conformational epitopes. Serial dilutions of ZV54 and E16 mAbs that recognize a lateral ridge conformational epitope on EDIII of ZIKV and WNV, respectively, were incubated in microtiter wells coated with HBcAg-zDIII VLPs and detected with an <t>HRP-conjugated</t> goat anti-mouse <t>IgG</t> antibody. 6D8: an anti-Ebola isotype negative control mAb. Mean ± SD of samples from three independent experiments is presented.
    Horseradish Peroxidase Hrp, supplied by Proteintech, used in various techniques. Bioz Stars score: 92/100, based on 95 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Agilent technologies horseradish peroxidase hrp
    Detection of VEGFR2 on vasculature of various tumors by RAFL-1 antibody. NCI-H358 human nonsmall lung carcinoma and L540 Hodgkin's disease tumors were grown in SCID mice. Meth A mouse fibrosarcoma and 3LL mouse lung carcinomas were grown in BALB/c and C57BL/6 mice, respectively. VEGFR2 was detected on frozen tumor sections by incubating them with RAFL-1 antibody (10 µg/ml) followed by goat <t>antirat</t> IgG <t>HRP,</t> as described under Materials and Methods section. Sections were developed with DAB and counterstained with hematoxylin. Representative images from each tumor type are shown.
    Horseradish Peroxidase Hrp, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 94/100, based on 1469 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc horseradish peroxidase hrp
    Comparison in expression of TAP, LMP and B-7.1 peptides in parental and pAnti IGF-1 transfected and/or IGF-1R monoclonal antibody (mAb) treated HGB cell lines. A, Regulation of TAP-1 peptide in T98G and HG-2 TX cells was determined by Western Blot. Cell lysate was prepared from cells of TX and corresponding NT cell lines pretreated as described in Fig 4 and then subjected to SDS-PAGE and electronically blotted to nitrocellulose membrane. TAP-1 peptide on the membrane was probed by anti-human TAP-1 monoclonal Ab+anti-mouse <t>IgG</t> <t>HRP-linked</t> Ab; and, signal was detected by LumiGLO reagent. Lanes 1, 2 are NT cells from the T98G and HG-2 cell lines respectively. Lane 3, 4 are TX cells from clone b and c of the T98G cell line; Lane 5, 6 are TX cells from clone 5 and 11 of the HG-2 cell line. Re-probed membrane with anti-actin Ab demonstrates presence of the 42 kd actin. Up-regulation in expression of the 70 kd TAP-1 in the two pAnti IGF-1 transfected cell clones were demonstrated in this experiment. B, Up-regulation in TAP-1 and LMP-7 peptides, and, rescue in expression of TAP-2 and LMP-2 peptides following the exogenous addition of 10ug/ml IGF-1R mAb into cell culture medium for 48 hours were demonstrated by Western Blot. The lysates of wild type and IGF-1R antibody treated cells were prepared as described in A. Lanes 1, 2 and 3 represent T98G, HG-2 and HG-9 cell lines cultured in medium with no IGF-1R mAb added, while lanes 4, 5 and 6 are the corresponding respective cell lines cultured in medium with addition of exogenous IGF-1R mAb (10ug/ml), respectively. Rows 1, 2, 3 and 4 represent TAP-1, TAP-2, LMP-2 and LMP-7, respectively. Row 5 demonstrates the rescue in expression of the B-7.1 peptide in IGF-1R mAb treated T98G, HG-2 and HG-9 cell lines when compared to the wild types of the corresponding non-treated cells. The 42 kd band of actin is also shown as an internal control for the quantity of samples loaded. B represents the results from one set of the experiments, that were repeated×2; C, The densitometry analysis for the two sets of similar experiments was obtained by the NIH image J program. The differences in results between the groups with and without IGF-1R mAb in culture media were significant at p
    Horseradish Peroxidase Hrp, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1183 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    GeneTex horseradish peroxidase hrp
    Comparison in expression of TAP, LMP and B-7.1 peptides in parental and pAnti IGF-1 transfected and/or IGF-1R monoclonal antibody (mAb) treated HGB cell lines. A, Regulation of TAP-1 peptide in T98G and HG-2 TX cells was determined by Western Blot. Cell lysate was prepared from cells of TX and corresponding NT cell lines pretreated as described in Fig 4 and then subjected to SDS-PAGE and electronically blotted to nitrocellulose membrane. TAP-1 peptide on the membrane was probed by anti-human TAP-1 monoclonal Ab+anti-mouse <t>IgG</t> <t>HRP-linked</t> Ab; and, signal was detected by LumiGLO reagent. Lanes 1, 2 are NT cells from the T98G and HG-2 cell lines respectively. Lane 3, 4 are TX cells from clone b and c of the T98G cell line; Lane 5, 6 are TX cells from clone 5 and 11 of the HG-2 cell line. Re-probed membrane with anti-actin Ab demonstrates presence of the 42 kd actin. Up-regulation in expression of the 70 kd TAP-1 in the two pAnti IGF-1 transfected cell clones were demonstrated in this experiment. B, Up-regulation in TAP-1 and LMP-7 peptides, and, rescue in expression of TAP-2 and LMP-2 peptides following the exogenous addition of 10ug/ml IGF-1R mAb into cell culture medium for 48 hours were demonstrated by Western Blot. The lysates of wild type and IGF-1R antibody treated cells were prepared as described in A. Lanes 1, 2 and 3 represent T98G, HG-2 and HG-9 cell lines cultured in medium with no IGF-1R mAb added, while lanes 4, 5 and 6 are the corresponding respective cell lines cultured in medium with addition of exogenous IGF-1R mAb (10ug/ml), respectively. Rows 1, 2, 3 and 4 represent TAP-1, TAP-2, LMP-2 and LMP-7, respectively. Row 5 demonstrates the rescue in expression of the B-7.1 peptide in IGF-1R mAb treated T98G, HG-2 and HG-9 cell lines when compared to the wild types of the corresponding non-treated cells. The 42 kd band of actin is also shown as an internal control for the quantity of samples loaded. B represents the results from one set of the experiments, that were repeated×2; C, The densitometry analysis for the two sets of similar experiments was obtained by the NIH image J program. The differences in results between the groups with and without IGF-1R mAb in culture media were significant at p
    Horseradish Peroxidase Hrp, supplied by GeneTex, used in various techniques. Bioz Stars score: 92/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Toyobo horseradish peroxidase hrp
    Comparison in expression of TAP, LMP and B-7.1 peptides in parental and pAnti IGF-1 transfected and/or IGF-1R monoclonal antibody (mAb) treated HGB cell lines. A, Regulation of TAP-1 peptide in T98G and HG-2 TX cells was determined by Western Blot. Cell lysate was prepared from cells of TX and corresponding NT cell lines pretreated as described in Fig 4 and then subjected to SDS-PAGE and electronically blotted to nitrocellulose membrane. TAP-1 peptide on the membrane was probed by anti-human TAP-1 monoclonal Ab+anti-mouse <t>IgG</t> <t>HRP-linked</t> Ab; and, signal was detected by LumiGLO reagent. Lanes 1, 2 are NT cells from the T98G and HG-2 cell lines respectively. Lane 3, 4 are TX cells from clone b and c of the T98G cell line; Lane 5, 6 are TX cells from clone 5 and 11 of the HG-2 cell line. Re-probed membrane with anti-actin Ab demonstrates presence of the 42 kd actin. Up-regulation in expression of the 70 kd TAP-1 in the two pAnti IGF-1 transfected cell clones were demonstrated in this experiment. B, Up-regulation in TAP-1 and LMP-7 peptides, and, rescue in expression of TAP-2 and LMP-2 peptides following the exogenous addition of 10ug/ml IGF-1R mAb into cell culture medium for 48 hours were demonstrated by Western Blot. The lysates of wild type and IGF-1R antibody treated cells were prepared as described in A. Lanes 1, 2 and 3 represent T98G, HG-2 and HG-9 cell lines cultured in medium with no IGF-1R mAb added, while lanes 4, 5 and 6 are the corresponding respective cell lines cultured in medium with addition of exogenous IGF-1R mAb (10ug/ml), respectively. Rows 1, 2, 3 and 4 represent TAP-1, TAP-2, LMP-2 and LMP-7, respectively. Row 5 demonstrates the rescue in expression of the B-7.1 peptide in IGF-1R mAb treated T98G, HG-2 and HG-9 cell lines when compared to the wild types of the corresponding non-treated cells. The 42 kd band of actin is also shown as an internal control for the quantity of samples loaded. B represents the results from one set of the experiments, that were repeated×2; C, The densitometry analysis for the two sets of similar experiments was obtained by the NIH image J program. The differences in results between the groups with and without IGF-1R mAb in culture media were significant at p
    Horseradish Peroxidase Hrp, supplied by Toyobo, used in various techniques. Bioz Stars score: 92/100, based on 17 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Bioss horseradish peroxidase hrp
    Comparison in expression of TAP, LMP and B-7.1 peptides in parental and pAnti IGF-1 transfected and/or IGF-1R monoclonal antibody (mAb) treated HGB cell lines. A, Regulation of TAP-1 peptide in T98G and HG-2 TX cells was determined by Western Blot. Cell lysate was prepared from cells of TX and corresponding NT cell lines pretreated as described in Fig 4 and then subjected to SDS-PAGE and electronically blotted to nitrocellulose membrane. TAP-1 peptide on the membrane was probed by anti-human TAP-1 monoclonal Ab+anti-mouse <t>IgG</t> <t>HRP-linked</t> Ab; and, signal was detected by LumiGLO reagent. Lanes 1, 2 are NT cells from the T98G and HG-2 cell lines respectively. Lane 3, 4 are TX cells from clone b and c of the T98G cell line; Lane 5, 6 are TX cells from clone 5 and 11 of the HG-2 cell line. Re-probed membrane with anti-actin Ab demonstrates presence of the 42 kd actin. Up-regulation in expression of the 70 kd TAP-1 in the two pAnti IGF-1 transfected cell clones were demonstrated in this experiment. B, Up-regulation in TAP-1 and LMP-7 peptides, and, rescue in expression of TAP-2 and LMP-2 peptides following the exogenous addition of 10ug/ml IGF-1R mAb into cell culture medium for 48 hours were demonstrated by Western Blot. The lysates of wild type and IGF-1R antibody treated cells were prepared as described in A. Lanes 1, 2 and 3 represent T98G, HG-2 and HG-9 cell lines cultured in medium with no IGF-1R mAb added, while lanes 4, 5 and 6 are the corresponding respective cell lines cultured in medium with addition of exogenous IGF-1R mAb (10ug/ml), respectively. Rows 1, 2, 3 and 4 represent TAP-1, TAP-2, LMP-2 and LMP-7, respectively. Row 5 demonstrates the rescue in expression of the B-7.1 peptide in IGF-1R mAb treated T98G, HG-2 and HG-9 cell lines when compared to the wild types of the corresponding non-treated cells. The 42 kd band of actin is also shown as an internal control for the quantity of samples loaded. B represents the results from one set of the experiments, that were repeated×2; C, The densitometry analysis for the two sets of similar experiments was obtained by the NIH image J program. The differences in results between the groups with and without IGF-1R mAb in culture media were significant at p
    Horseradish Peroxidase Hrp, supplied by Bioss, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Cayman Chemical horseradish peroxidase hrp
    Comparison in expression of TAP, LMP and B-7.1 peptides in parental and pAnti IGF-1 transfected and/or IGF-1R monoclonal antibody (mAb) treated HGB cell lines. A, Regulation of TAP-1 peptide in T98G and HG-2 TX cells was determined by Western Blot. Cell lysate was prepared from cells of TX and corresponding NT cell lines pretreated as described in Fig 4 and then subjected to SDS-PAGE and electronically blotted to nitrocellulose membrane. TAP-1 peptide on the membrane was probed by anti-human TAP-1 monoclonal Ab+anti-mouse <t>IgG</t> <t>HRP-linked</t> Ab; and, signal was detected by LumiGLO reagent. Lanes 1, 2 are NT cells from the T98G and HG-2 cell lines respectively. Lane 3, 4 are TX cells from clone b and c of the T98G cell line; Lane 5, 6 are TX cells from clone 5 and 11 of the HG-2 cell line. Re-probed membrane with anti-actin Ab demonstrates presence of the 42 kd actin. Up-regulation in expression of the 70 kd TAP-1 in the two pAnti IGF-1 transfected cell clones were demonstrated in this experiment. B, Up-regulation in TAP-1 and LMP-7 peptides, and, rescue in expression of TAP-2 and LMP-2 peptides following the exogenous addition of 10ug/ml IGF-1R mAb into cell culture medium for 48 hours were demonstrated by Western Blot. The lysates of wild type and IGF-1R antibody treated cells were prepared as described in A. Lanes 1, 2 and 3 represent T98G, HG-2 and HG-9 cell lines cultured in medium with no IGF-1R mAb added, while lanes 4, 5 and 6 are the corresponding respective cell lines cultured in medium with addition of exogenous IGF-1R mAb (10ug/ml), respectively. Rows 1, 2, 3 and 4 represent TAP-1, TAP-2, LMP-2 and LMP-7, respectively. Row 5 demonstrates the rescue in expression of the B-7.1 peptide in IGF-1R mAb treated T98G, HG-2 and HG-9 cell lines when compared to the wild types of the corresponding non-treated cells. The 42 kd band of actin is also shown as an internal control for the quantity of samples loaded. B represents the results from one set of the experiments, that were repeated×2; C, The densitometry analysis for the two sets of similar experiments was obtained by the NIH image J program. The differences in results between the groups with and without IGF-1R mAb in culture media were significant at p
    Horseradish Peroxidase Hrp, supplied by Cayman Chemical, used in various techniques. Bioz Stars score: 92/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Beijing CWBio horseradish peroxidase hrp
    Comparison in expression of TAP, LMP and B-7.1 peptides in parental and pAnti IGF-1 transfected and/or IGF-1R monoclonal antibody (mAb) treated HGB cell lines. A, Regulation of TAP-1 peptide in T98G and HG-2 TX cells was determined by Western Blot. Cell lysate was prepared from cells of TX and corresponding NT cell lines pretreated as described in Fig 4 and then subjected to SDS-PAGE and electronically blotted to nitrocellulose membrane. TAP-1 peptide on the membrane was probed by anti-human TAP-1 monoclonal Ab+anti-mouse <t>IgG</t> <t>HRP-linked</t> Ab; and, signal was detected by LumiGLO reagent. Lanes 1, 2 are NT cells from the T98G and HG-2 cell lines respectively. Lane 3, 4 are TX cells from clone b and c of the T98G cell line; Lane 5, 6 are TX cells from clone 5 and 11 of the HG-2 cell line. Re-probed membrane with anti-actin Ab demonstrates presence of the 42 kd actin. Up-regulation in expression of the 70 kd TAP-1 in the two pAnti IGF-1 transfected cell clones were demonstrated in this experiment. B, Up-regulation in TAP-1 and LMP-7 peptides, and, rescue in expression of TAP-2 and LMP-2 peptides following the exogenous addition of 10ug/ml IGF-1R mAb into cell culture medium for 48 hours were demonstrated by Western Blot. The lysates of wild type and IGF-1R antibody treated cells were prepared as described in A. Lanes 1, 2 and 3 represent T98G, HG-2 and HG-9 cell lines cultured in medium with no IGF-1R mAb added, while lanes 4, 5 and 6 are the corresponding respective cell lines cultured in medium with addition of exogenous IGF-1R mAb (10ug/ml), respectively. Rows 1, 2, 3 and 4 represent TAP-1, TAP-2, LMP-2 and LMP-7, respectively. Row 5 demonstrates the rescue in expression of the B-7.1 peptide in IGF-1R mAb treated T98G, HG-2 and HG-9 cell lines when compared to the wild types of the corresponding non-treated cells. The 42 kd band of actin is also shown as an internal control for the quantity of samples loaded. B represents the results from one set of the experiments, that were repeated×2; C, The densitometry analysis for the two sets of similar experiments was obtained by the NIH image J program. The differences in results between the groups with and without IGF-1R mAb in culture media were significant at p
    Horseradish Peroxidase Hrp, supplied by Beijing CWBio, used in various techniques. Bioz Stars score: 93/100, based on 185 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bethyl horseradish peroxidase hrp
    Confirmation of hIgG expression in the Tc goat with Western blotting. The purified hIgG from the Tc goat, positive control human IVIG, and negative control purified from commercial goat <t>IgG</t> was probed with anti-human IgG (heavy and light; H + L) <t>HRP.</t>
    Horseradish Peroxidase Hrp, supplied by Bethyl, used in various techniques. Bioz Stars score: 92/100, based on 98 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Confirmation of hIgG expression in the Tc goat with Western blotting. The purified hIgG from the Tc goat, positive control human IVIG, and negative control purified from commercial goat <t>IgG</t> was probed with anti-human IgG (heavy and light; H + L) <t>HRP.</t>
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    Confirmation of hIgG expression in the Tc goat with Western blotting. The purified hIgG from the Tc goat, positive control human IVIG, and negative control purified from commercial goat <t>IgG</t> was probed with anti-human IgG (heavy and light; H + L) <t>HRP.</t>
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    Confirmation of hIgG expression in the Tc goat with Western blotting. The purified hIgG from the Tc goat, positive control human IVIG, and negative control purified from commercial goat <t>IgG</t> was probed with anti-human IgG (heavy and light; H + L) <t>HRP.</t>
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    Confirmation of hIgG expression in the Tc goat with Western blotting. The purified hIgG from the Tc goat, positive control human IVIG, and negative control purified from commercial goat <t>IgG</t> was probed with anti-human IgG (heavy and light; H + L) <t>HRP.</t>
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    Analysis of the affinities of three <t>HRP</t> labeled <t>mAbs</t> (HRP-1E4, HRP-2C7, and HRP-2G9) for sORF2-C using direct ELISA. The three HRP-mAbs (1 mg/ml) in a dilution range of 10 −1 to 10 −4 were tested for reaction with the sORF2-C protein in the direct ELISA.
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    Image Search Results


    Caveolin-1 interacts with the RSV G and M protein complex on the surface of infected cells. (A) Immunoprecipitations of RSV G, M and M2-1 proteins from HeLa whole-cell lysates of mock-infected or RSV-infected cells (22 hpi). Immunoprecipitates were probed for G protein (top panel), M protein (middle panel) and caveolin-1 (bottom panel). Caveolin-1 protein was measured by densitometry (bottom graph). (B) Streptavidin–HRP blot of lysates of surface-biotinylated HeLa cells. M, mock infected; I, RSV infected. (C) Streptavidin–HRP blot of immunoprecipitates from lysates shown in B, using antibodies against RSV G protein or caveolin-1. Representative data of two independent experiments are shown.

    Journal: Journal of Cell Science

    Article Title: Caveolae provide a specialized membrane environment for respiratory syncytial virus assembly

    doi: 10.1242/jcs.198853

    Figure Lengend Snippet: Caveolin-1 interacts with the RSV G and M protein complex on the surface of infected cells. (A) Immunoprecipitations of RSV G, M and M2-1 proteins from HeLa whole-cell lysates of mock-infected or RSV-infected cells (22 hpi). Immunoprecipitates were probed for G protein (top panel), M protein (middle panel) and caveolin-1 (bottom panel). Caveolin-1 protein was measured by densitometry (bottom graph). (B) Streptavidin–HRP blot of lysates of surface-biotinylated HeLa cells. M, mock infected; I, RSV infected. (C) Streptavidin–HRP blot of immunoprecipitates from lysates shown in B, using antibodies against RSV G protein or caveolin-1. Representative data of two independent experiments are shown.

    Article Snippet: Streptavidin conjugated to horseradish peroxidase (HRP), CellMask™Orange, phalloidin–FITC, and Alexa Fluor 488, 555, 633- and HRP-conjugated secondary antibodies were from LifeTechnology, Singapore.

    Techniques: Infection

    Western blot analysis of eight CHO-S clones demonstrated various levels of scFv-QuVHVL expression. The blot was probed for 6xHis tagged protein with a mouse anti-6xHis mAb followed by goat anti-mouse IgG-HRP. The target protein was a ∼30kD protein.

    Journal: Molecular immunology

    Article Title: Highly Specific Inhibition of C1q Globular-Head Binding to Human IgG

    doi: 10.1016/j.molimm.2007.12.019

    Figure Lengend Snippet: Western blot analysis of eight CHO-S clones demonstrated various levels of scFv-QuVHVL expression. The blot was probed for 6xHis tagged protein with a mouse anti-6xHis mAb followed by goat anti-mouse IgG-HRP. The target protein was a ∼30kD protein.

    Article Snippet: The plates were washed again with TPBS and goat anti-mouse IgG conjugated to horseradish peroxidase (HRP) (Jackson Immunologicals, West Grove, PA) preparation in 0.1% ultrapure BSA in TPBS was added.

    Techniques: Western Blot, Clone Assay, Expressing

    The reactivity in the ELISA test of polyclonal anti- Escherichia coli antibody conjugated with HRP (1:2000) with Escherichia coli strains: 056, K12, 0111, 024, 104, B, and Lactobacillus rhamnosus LOCK 0919 (919). L-0.25 mg of lyophilized bacterial mass/1 mL of PBS; 10 8 CFU/mL, 10 7 CFU/mL, 10 6 CFU/mL of alive bacterial culture in PBS. Pooled results from three independent experiments are shown. *, P

    Journal: Sensors (Basel, Switzerland)

    Article Title: Effectiveness of Sensors Contact Metallization (Ti, Au, and Ru) and Biofunctionalization for Escherichia coli Detection

    doi: 10.3390/s18092912

    Figure Lengend Snippet: The reactivity in the ELISA test of polyclonal anti- Escherichia coli antibody conjugated with HRP (1:2000) with Escherichia coli strains: 056, K12, 0111, 024, 104, B, and Lactobacillus rhamnosus LOCK 0919 (919). L-0.25 mg of lyophilized bacterial mass/1 mL of PBS; 10 8 CFU/mL, 10 7 CFU/mL, 10 6 CFU/mL of alive bacterial culture in PBS. Pooled results from three independent experiments are shown. *, P

    Article Snippet: For the quantitative control of biofunctionalization, after the surfaces were washed, the rabbit polyclonal serum anti-Escherichia coli conjugated with horseradish peroxidase (HRP) was applied (1:2000, Abcam) and incubated at 37 °C for 1 h. Samples were washed five times with PBS and finally, the 3,3’,5,5’-tetramethylbenzidine (TMB) substrate was added to yield colored reaction.

    Techniques: Enzyme-linked Immunosorbent Assay

    TLF2 is a protein complex. One microgram of TLF2 was immunoprecipitated by antibodies to human Hp (MAb; α-Hp), human apoA-I (polyclonal antibodies from sheep and goat; α-apoA-I), and human IgM (MAb; α-IgM). Following immunoprecipitation, the pellet (P) and supernatant (S) were separated by reducing SDS-PAGE (12% gel) and transferred to PVDF membranes. The IgM μ chain was detected with rabbit anti-IgM μ-chain antibody followed by goat anti-rabbit IgG-HRP and exposed for 30 s by ECL.

    Journal: Infection and Immunity

    Article Title: Characterization of a Novel Trypanosome Lytic Factor from Human Serum

    doi:

    Figure Lengend Snippet: TLF2 is a protein complex. One microgram of TLF2 was immunoprecipitated by antibodies to human Hp (MAb; α-Hp), human apoA-I (polyclonal antibodies from sheep and goat; α-apoA-I), and human IgM (MAb; α-IgM). Following immunoprecipitation, the pellet (P) and supernatant (S) were separated by reducing SDS-PAGE (12% gel) and transferred to PVDF membranes. The IgM μ chain was detected with rabbit anti-IgM μ-chain antibody followed by goat anti-rabbit IgG-HRP and exposed for 30 s by ECL.

    Article Snippet: The secondary antibodies, goat anti-rabbit IgG conjugated to horseradish peroxidase (HRP) (W401B; Promega), rabbit anti-sheep IgG conjugated to HRP (605 345; Boehringer Mannheim), and rabbit anti-mouse IgG conjugated to HRP (W402B; Promega), were diluted 1:20,000 in TBST containing 4% BSA.

    Techniques: Immunoprecipitation, SDS Page

    PrP C expression levels in uninfected N2a cells treated with the 16 validated antiprion compounds at the indicated concentrations for 5 days. Conjugated D13-HRP was used to detect PrP in Western immunoblots. Lane numbers correspond to compound IDs in

    Journal: The Journal of Biological Chemistry

    Article Title: A Survey of Antiprion Compounds Reveals the Prevalence of Non-PrP Molecular Targets *

    doi: 10.1074/jbc.M111.234393

    Figure Lengend Snippet: PrP C expression levels in uninfected N2a cells treated with the 16 validated antiprion compounds at the indicated concentrations for 5 days. Conjugated D13-HRP was used to detect PrP in Western immunoblots. Lane numbers correspond to compound IDs in

    Article Snippet: PrP was detected by using D13 antibody Fab fragment conjugated ( ) with horseradish peroxidase (HRP) (Rockland Immunochemicals Inc.).

    Techniques: Expressing, Western Blot

    Isolation of MIP from phage-displayed combinatorial peptide library. ), a single peptide ligand, MIP (NH 2 -AIRINPNGTWSRQAETVES-COOH; insert (underlined) and flanking region), was identified to bind a GST-MLK3 SH3 domain fusion protein. ELISA shows the phage-displayed MIP to bind to the WT form of the MLK3 SH3 domain (SH3 WT) but not the GST fusion partner. The presence of virions in the supernatant was determined by coating the wells of the microtiter plate with an anti-M13 mAb ( anti-M13 Ab ). Virions, which were retained in the microtiter plate wells, were detected with anti-M13 mAb conjugated to HRP. Experiments were performed in duplicate, and the results are an averaged value; error bars .

    Journal: The Journal of Biological Chemistry

    Article Title: Identification of two distinct peptide-binding pockets in the SH3 domain of human mixed-lineage kinase 3

    doi: 10.1074/jbc.RA117.000262

    Figure Lengend Snippet: Isolation of MIP from phage-displayed combinatorial peptide library. ), a single peptide ligand, MIP (NH 2 -AIRINPNGTWSRQAETVES-COOH; insert (underlined) and flanking region), was identified to bind a GST-MLK3 SH3 domain fusion protein. ELISA shows the phage-displayed MIP to bind to the WT form of the MLK3 SH3 domain (SH3 WT) but not the GST fusion partner. The presence of virions in the supernatant was determined by coating the wells of the microtiter plate with an anti-M13 mAb ( anti-M13 Ab ). Virions, which were retained in the microtiter plate wells, were detected with anti-M13 mAb conjugated to HRP. Experiments were performed in duplicate, and the results are an averaged value; error bars .

    Article Snippet: After three washes with PBS containing 0.1% Tween 20 (PBST), retention of the SH3 domain fusion protein in wells was detected with an anti-GST antibody conjugated to horseradish peroxidase (HRP) (GE Healthcare; 45 min; 1:5000 in PBST).

    Techniques: Isolation, Enzyme-linked Immunosorbent Assay

    Competition ELISA between MIP and NS5A peptide. To determine whether the MIP and NS5A peptides competitively bind the SH3 domain of MLK3, a GST-MLK3 SH3(43–104) fusion protein was preincubated with increasing concentrations of unlabeled MIP peptide or unlabeled NS5A peptide as competitor and then allowed to interact with biotinylated MIP ( A ) or biotinylated NS5A ( B ) peptide probes immobilized on a NeutrAvidin-coated 96-well ELISA plate. Binding of the SH3 domain was detected with an anti-GST antibody conjugated to HRP, and the signal levels are presented as a percentage of binding in the absence of competitor. Experiments were performed in triplicate, and the results are an averaged value; error bars reflect the standard deviation of each point. Curve fitting was performed with OriginPro 2017.

    Journal: The Journal of Biological Chemistry

    Article Title: Identification of two distinct peptide-binding pockets in the SH3 domain of human mixed-lineage kinase 3

    doi: 10.1074/jbc.RA117.000262

    Figure Lengend Snippet: Competition ELISA between MIP and NS5A peptide. To determine whether the MIP and NS5A peptides competitively bind the SH3 domain of MLK3, a GST-MLK3 SH3(43–104) fusion protein was preincubated with increasing concentrations of unlabeled MIP peptide or unlabeled NS5A peptide as competitor and then allowed to interact with biotinylated MIP ( A ) or biotinylated NS5A ( B ) peptide probes immobilized on a NeutrAvidin-coated 96-well ELISA plate. Binding of the SH3 domain was detected with an anti-GST antibody conjugated to HRP, and the signal levels are presented as a percentage of binding in the absence of competitor. Experiments were performed in triplicate, and the results are an averaged value; error bars reflect the standard deviation of each point. Curve fitting was performed with OriginPro 2017.

    Article Snippet: After three washes with PBS containing 0.1% Tween 20 (PBST), retention of the SH3 domain fusion protein in wells was detected with an anti-GST antibody conjugated to horseradish peroxidase (HRP) (GE Healthcare; 45 min; 1:5000 in PBST).

    Techniques: Enzyme-linked Immunosorbent Assay, Binding Assay, Standard Deviation

    Binding of MIP and NS5A peptides to SH3 domain of other members of MLK subfamily (MLK1–4). To determine whether MIP and NS5A can interact with SH3 domains of MLK1–4 proteins, the purified GST-MLK1–4 SH3 domains were incubated with biotinylated peptides, NS5A peptide (KKAPTPPPRRRR-GGG-K-biotin), MIP (AIRINPNGTWSRQAETVES-K-biotin), and MIP-R12A (AIRINPNGTWSAQAETVES-K-biotin), immobilized on a NeutrAvidin-coated 96-well ELISA plate. Binding of SH3 domain was detected with anti-GST antibody conjugated to HRP. Experiments were performed in triplicate, and the results are an averaged value; error bars .

    Journal: The Journal of Biological Chemistry

    Article Title: Identification of two distinct peptide-binding pockets in the SH3 domain of human mixed-lineage kinase 3

    doi: 10.1074/jbc.RA117.000262

    Figure Lengend Snippet: Binding of MIP and NS5A peptides to SH3 domain of other members of MLK subfamily (MLK1–4). To determine whether MIP and NS5A can interact with SH3 domains of MLK1–4 proteins, the purified GST-MLK1–4 SH3 domains were incubated with biotinylated peptides, NS5A peptide (KKAPTPPPRRRR-GGG-K-biotin), MIP (AIRINPNGTWSRQAETVES-K-biotin), and MIP-R12A (AIRINPNGTWSAQAETVES-K-biotin), immobilized on a NeutrAvidin-coated 96-well ELISA plate. Binding of SH3 domain was detected with anti-GST antibody conjugated to HRP. Experiments were performed in triplicate, and the results are an averaged value; error bars .

    Article Snippet: After three washes with PBS containing 0.1% Tween 20 (PBST), retention of the SH3 domain fusion protein in wells was detected with an anti-GST antibody conjugated to horseradish peroxidase (HRP) (GE Healthcare; 45 min; 1:5000 in PBST).

    Techniques: Binding Assay, Purification, Incubation, Enzyme-linked Immunosorbent Assay

    SmpB-SsrA Mediated Protein Tagging Activity Is Observed in Y. pseudotuberculosis (A) Schematic representation of the λ-cI-N-trpAt reporter construct encoded on the pKW540 plasmid and anticipated outcomes of protein tagging in wild-type (WT) or ΔBA strains. (B) The λ-cI-N-trpAt reporter was induced in wild-type and mutant (ΔBA) strains, and protein samples were analyzed by Western blot using HRP-conjugated anti-H6 serum. MW stds, protein molecular weight standards.

    Journal: PLoS Pathogens

    Article Title: A Role for the SmpB-SsrA System in Yersinia pseudotuberculosis Pathogenesis

    doi: 10.1371/journal.ppat.0020006

    Figure Lengend Snippet: SmpB-SsrA Mediated Protein Tagging Activity Is Observed in Y. pseudotuberculosis (A) Schematic representation of the λ-cI-N-trpAt reporter construct encoded on the pKW540 plasmid and anticipated outcomes of protein tagging in wild-type (WT) or ΔBA strains. (B) The λ-cI-N-trpAt reporter was induced in wild-type and mutant (ΔBA) strains, and protein samples were analyzed by Western blot using HRP-conjugated anti-H6 serum. MW stds, protein molecular weight standards.

    Article Snippet: Resolved proteins were transferred to polyvinylidene difluoride (PVDF) membrane and probed with horseradish peroxidase (HRP) conjugated anti-H6 antibodies (Santa Cruz Biotechnology, Santa Cruz, California, United States) to detect the H6 epitope present in the λ-cI-N protein.

    Techniques: Activity Assay, Construct, Plasmid Preparation, Mutagenesis, Western Blot, Molecular Weight

    Specific binding of HBcAg VLP-displayed zDIII by monoclonal antibodies that recognize EDIII conformational epitopes. Serial dilutions of ZV54 and E16 mAbs that recognize a lateral ridge conformational epitope on EDIII of ZIKV and WNV, respectively, were incubated in microtiter wells coated with HBcAg-zDIII VLPs and detected with an HRP-conjugated goat anti-mouse IgG antibody. 6D8: an anti-Ebola isotype negative control mAb. Mean ± SD of samples from three independent experiments is presented.

    Journal: Scientific Reports

    Article Title: Virus-like particles that display Zika virus envelope protein domain III induce potent neutralizing immune responses in mice

    doi: 10.1038/s41598-017-08247-9

    Figure Lengend Snippet: Specific binding of HBcAg VLP-displayed zDIII by monoclonal antibodies that recognize EDIII conformational epitopes. Serial dilutions of ZV54 and E16 mAbs that recognize a lateral ridge conformational epitope on EDIII of ZIKV and WNV, respectively, were incubated in microtiter wells coated with HBcAg-zDIII VLPs and detected with an HRP-conjugated goat anti-mouse IgG antibody. 6D8: an anti-Ebola isotype negative control mAb. Mean ± SD of samples from three independent experiments is presented.

    Article Snippet: Membranes were subsequently incubated with a goat anti-mouse IgG conjugated with horseradish peroxidase (HRP) (Southern Biotech, AL).

    Techniques: Binding Assay, Incubation, Negative Control

    Detection of VEGFR2 on vasculature of various tumors by RAFL-1 antibody. NCI-H358 human nonsmall lung carcinoma and L540 Hodgkin's disease tumors were grown in SCID mice. Meth A mouse fibrosarcoma and 3LL mouse lung carcinomas were grown in BALB/c and C57BL/6 mice, respectively. VEGFR2 was detected on frozen tumor sections by incubating them with RAFL-1 antibody (10 µg/ml) followed by goat antirat IgG HRP, as described under Materials and Methods section. Sections were developed with DAB and counterstained with hematoxylin. Representative images from each tumor type are shown.

    Journal: Neoplasia (New York, N.Y.)

    Article Title: Evaluation of Novel Antimouse VEGFR2 Antibodies as Potential Antiangiogenic or Vascular Targeting Agents for Tumor Therapy 1

    doi:

    Figure Lengend Snippet: Detection of VEGFR2 on vasculature of various tumors by RAFL-1 antibody. NCI-H358 human nonsmall lung carcinoma and L540 Hodgkin's disease tumors were grown in SCID mice. Meth A mouse fibrosarcoma and 3LL mouse lung carcinomas were grown in BALB/c and C57BL/6 mice, respectively. VEGFR2 was detected on frozen tumor sections by incubating them with RAFL-1 antibody (10 µg/ml) followed by goat antirat IgG HRP, as described under Materials and Methods section. Sections were developed with DAB and counterstained with hematoxylin. Representative images from each tumor type are shown.

    Article Snippet: Goat antirat, antimouse, and antirabbit secondary antibodies conjugated to horseradish peroxidase (HRP) were purchased from Dako (Carpinteria, CA).

    Techniques: Mouse Assay

    Comparison in expression of TAP, LMP and B-7.1 peptides in parental and pAnti IGF-1 transfected and/or IGF-1R monoclonal antibody (mAb) treated HGB cell lines. A, Regulation of TAP-1 peptide in T98G and HG-2 TX cells was determined by Western Blot. Cell lysate was prepared from cells of TX and corresponding NT cell lines pretreated as described in Fig 4 and then subjected to SDS-PAGE and electronically blotted to nitrocellulose membrane. TAP-1 peptide on the membrane was probed by anti-human TAP-1 monoclonal Ab+anti-mouse IgG HRP-linked Ab; and, signal was detected by LumiGLO reagent. Lanes 1, 2 are NT cells from the T98G and HG-2 cell lines respectively. Lane 3, 4 are TX cells from clone b and c of the T98G cell line; Lane 5, 6 are TX cells from clone 5 and 11 of the HG-2 cell line. Re-probed membrane with anti-actin Ab demonstrates presence of the 42 kd actin. Up-regulation in expression of the 70 kd TAP-1 in the two pAnti IGF-1 transfected cell clones were demonstrated in this experiment. B, Up-regulation in TAP-1 and LMP-7 peptides, and, rescue in expression of TAP-2 and LMP-2 peptides following the exogenous addition of 10ug/ml IGF-1R mAb into cell culture medium for 48 hours were demonstrated by Western Blot. The lysates of wild type and IGF-1R antibody treated cells were prepared as described in A. Lanes 1, 2 and 3 represent T98G, HG-2 and HG-9 cell lines cultured in medium with no IGF-1R mAb added, while lanes 4, 5 and 6 are the corresponding respective cell lines cultured in medium with addition of exogenous IGF-1R mAb (10ug/ml), respectively. Rows 1, 2, 3 and 4 represent TAP-1, TAP-2, LMP-2 and LMP-7, respectively. Row 5 demonstrates the rescue in expression of the B-7.1 peptide in IGF-1R mAb treated T98G, HG-2 and HG-9 cell lines when compared to the wild types of the corresponding non-treated cells. The 42 kd band of actin is also shown as an internal control for the quantity of samples loaded. B represents the results from one set of the experiments, that were repeated×2; C, The densitometry analysis for the two sets of similar experiments was obtained by the NIH image J program. The differences in results between the groups with and without IGF-1R mAb in culture media were significant at p

    Journal: PLoS ONE

    Article Title: Rescue of MHC-1 Antigen Processing Machinery by Down-Regulation in Expression of IGF-1 in Human Glioblastoma Cells

    doi: 10.1371/journal.pone.0058428

    Figure Lengend Snippet: Comparison in expression of TAP, LMP and B-7.1 peptides in parental and pAnti IGF-1 transfected and/or IGF-1R monoclonal antibody (mAb) treated HGB cell lines. A, Regulation of TAP-1 peptide in T98G and HG-2 TX cells was determined by Western Blot. Cell lysate was prepared from cells of TX and corresponding NT cell lines pretreated as described in Fig 4 and then subjected to SDS-PAGE and electronically blotted to nitrocellulose membrane. TAP-1 peptide on the membrane was probed by anti-human TAP-1 monoclonal Ab+anti-mouse IgG HRP-linked Ab; and, signal was detected by LumiGLO reagent. Lanes 1, 2 are NT cells from the T98G and HG-2 cell lines respectively. Lane 3, 4 are TX cells from clone b and c of the T98G cell line; Lane 5, 6 are TX cells from clone 5 and 11 of the HG-2 cell line. Re-probed membrane with anti-actin Ab demonstrates presence of the 42 kd actin. Up-regulation in expression of the 70 kd TAP-1 in the two pAnti IGF-1 transfected cell clones were demonstrated in this experiment. B, Up-regulation in TAP-1 and LMP-7 peptides, and, rescue in expression of TAP-2 and LMP-2 peptides following the exogenous addition of 10ug/ml IGF-1R mAb into cell culture medium for 48 hours were demonstrated by Western Blot. The lysates of wild type and IGF-1R antibody treated cells were prepared as described in A. Lanes 1, 2 and 3 represent T98G, HG-2 and HG-9 cell lines cultured in medium with no IGF-1R mAb added, while lanes 4, 5 and 6 are the corresponding respective cell lines cultured in medium with addition of exogenous IGF-1R mAb (10ug/ml), respectively. Rows 1, 2, 3 and 4 represent TAP-1, TAP-2, LMP-2 and LMP-7, respectively. Row 5 demonstrates the rescue in expression of the B-7.1 peptide in IGF-1R mAb treated T98G, HG-2 and HG-9 cell lines when compared to the wild types of the corresponding non-treated cells. The 42 kd band of actin is also shown as an internal control for the quantity of samples loaded. B represents the results from one set of the experiments, that were repeated×2; C, The densitometry analysis for the two sets of similar experiments was obtained by the NIH image J program. The differences in results between the groups with and without IGF-1R mAb in culture media were significant at p

    Article Snippet: Immuno-detection was performed using primary mouse anti-human TAP-1 monoclonal antibody (a gift from Dr. Robert Tampe, Philipps-University of Marburg, Germany) and secondary rabbit anti-mouse IgG antibody conjugated with horseradish peroxidase (HRP) (Cell Signaling Technology, Beverly, MA).

    Techniques: Expressing, Transfection, Western Blot, SDS Page, Clone Assay, Cell Culture

    Confirmation of hIgG expression in the Tc goat with Western blotting. The purified hIgG from the Tc goat, positive control human IVIG, and negative control purified from commercial goat IgG was probed with anti-human IgG (heavy and light; H + L) HRP.

    Journal: Scientific Reports

    Article Title: Generation of H7N9-specific human polyclonal antibodies from a transchromosomic goat (caprine) system

    doi: 10.1038/s41598-018-36961-5

    Figure Lengend Snippet: Confirmation of hIgG expression in the Tc goat with Western blotting. The purified hIgG from the Tc goat, positive control human IVIG, and negative control purified from commercial goat IgG was probed with anti-human IgG (heavy and light; H + L) HRP.

    Article Snippet: Following washing with PBST, goat anti-human IgG-Fc conjugated with horseradish peroxidase (HRP) (Bethyl) was added to plates and incubated for 1 hr at RT.

    Techniques: Expressing, Western Blot, Purification, Positive Control, Negative Control

    Analysis of the affinities of three HRP labeled mAbs (HRP-1E4, HRP-2C7, and HRP-2G9) for sORF2-C using direct ELISA. The three HRP-mAbs (1 mg/ml) in a dilution range of 10 −1 to 10 −4 were tested for reaction with the sORF2-C protein in the direct ELISA.

    Journal: PLoS ONE

    Article Title: A Novel Blocking ELISA for Detection of Antibodies against Hepatitis E Virus in Domestic Pigs

    doi: 10.1371/journal.pone.0152639

    Figure Lengend Snippet: Analysis of the affinities of three HRP labeled mAbs (HRP-1E4, HRP-2C7, and HRP-2G9) for sORF2-C using direct ELISA. The three HRP-mAbs (1 mg/ml) in a dilution range of 10 −1 to 10 −4 were tested for reaction with the sORF2-C protein in the direct ELISA.

    Article Snippet: After concentration determination, the purified mAbs were conjugated to horseradish peroxidase (HRP) using a kit according to the manufacturer’s instructions (Roche Diagnostics, Basel, Switzerland).

    Techniques: Labeling, Direct ELISA