polyclonal antibodies Search Results


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  • 97
    Thermo Fisher polyclonal antibody pab
    Polyclonal Antibody Pab, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 97/100, based on 17 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore polyclonal antibodies pabs
    Polyclonal Antibodies Pabs, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Covance polyclonal antibodies pab
    Biochemical characterization of novel termini-specific TDP-43 <t>polyclonal</t> antibodies. A: Schematic diagram of TDP-43 indicating the relative position of the peptides used to generate the pAbs against N-t and C-t regions. The diagram also shows, in scale, the most prominent features of the protein (domains and predicted localization signals). NLS, nuclear localization signal; NES, nuclear export signal; RRM, RNA-recognition motif; Gly-rich, glycine-rich domain. B and C: Representative images showing the immunoblotting pattern for TDP-43 antibodies using T7-tagged recombinant human TDP-43 (C-terminally truncated or full length) ( B ) or radioimmunoprecipitation assay (RIPA) lysates from QBI293 cells ( C ). D–F: TDP-43 immunobotting of sarkosyl-insoluble fractions from different FTLD-U subtype cases before (−) and after (+) alkaline phosphatase (AP) treatment. Proteins from frontal cortex of FTLD-U cases were sequentially extracted with buffers of increasing strength and subjected to SDS-polyacrylamide gel electrophoresis. Dephosphorylation of FTLD-U urea extracts with AP followed by immunoblotting with pan TDP-43 ( D ) and C-t TDP-43 <t>pAb</t> ( E ) collapsed the 45-kDa band into the 43-kDa band and separated TDP-43 fragments into four immunoreactive ∼23- to ∼27-kDa bands. Immunoblotting with N-t TDP-43 pAb ( F ) shows the collapse of the 45-kDa band, but no evidence for low molecular weight species. This indicates that pathological, sarkosyl-insoluble TDP-43 is abnormally phosphorylated and that low molecular weight pathological bands contain extreme C-t TDP-43 fragments.
    Polyclonal Antibodies Pab, supplied by Covance, used in various techniques. Bioz Stars score: 88/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher jam a pabs
    Biochemical characterization of novel termini-specific TDP-43 <t>polyclonal</t> antibodies. A: Schematic diagram of TDP-43 indicating the relative position of the peptides used to generate the pAbs against N-t and C-t regions. The diagram also shows, in scale, the most prominent features of the protein (domains and predicted localization signals). NLS, nuclear localization signal; NES, nuclear export signal; RRM, RNA-recognition motif; Gly-rich, glycine-rich domain. B and C: Representative images showing the immunoblotting pattern for TDP-43 antibodies using T7-tagged recombinant human TDP-43 (C-terminally truncated or full length) ( B ) or radioimmunoprecipitation assay (RIPA) lysates from QBI293 cells ( C ). D–F: TDP-43 immunobotting of sarkosyl-insoluble fractions from different FTLD-U subtype cases before (−) and after (+) alkaline phosphatase (AP) treatment. Proteins from frontal cortex of FTLD-U cases were sequentially extracted with buffers of increasing strength and subjected to SDS-polyacrylamide gel electrophoresis. Dephosphorylation of FTLD-U urea extracts with AP followed by immunoblotting with pan TDP-43 ( D ) and C-t TDP-43 <t>pAb</t> ( E ) collapsed the 45-kDa band into the 43-kDa band and separated TDP-43 fragments into four immunoreactive ∼23- to ∼27-kDa bands. Immunoblotting with N-t TDP-43 pAb ( F ) shows the collapse of the 45-kDa band, but no evidence for low molecular weight species. This indicates that pathological, sarkosyl-insoluble TDP-43 is abnormally phosphorylated and that low molecular weight pathological bands contain extreme C-t TDP-43 fragments.
    Jam A Pabs, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc polyclonal antibody pab
    Biochemical characterization of novel termini-specific TDP-43 <t>polyclonal</t> antibodies. A: Schematic diagram of TDP-43 indicating the relative position of the peptides used to generate the pAbs against N-t and C-t regions. The diagram also shows, in scale, the most prominent features of the protein (domains and predicted localization signals). NLS, nuclear localization signal; NES, nuclear export signal; RRM, RNA-recognition motif; Gly-rich, glycine-rich domain. B and C: Representative images showing the immunoblotting pattern for TDP-43 antibodies using T7-tagged recombinant human TDP-43 (C-terminally truncated or full length) ( B ) or radioimmunoprecipitation assay (RIPA) lysates from QBI293 cells ( C ). D–F: TDP-43 immunobotting of sarkosyl-insoluble fractions from different FTLD-U subtype cases before (−) and after (+) alkaline phosphatase (AP) treatment. Proteins from frontal cortex of FTLD-U cases were sequentially extracted with buffers of increasing strength and subjected to SDS-polyacrylamide gel electrophoresis. Dephosphorylation of FTLD-U urea extracts with AP followed by immunoblotting with pan TDP-43 ( D ) and C-t TDP-43 <t>pAb</t> ( E ) collapsed the 45-kDa band into the 43-kDa band and separated TDP-43 fragments into four immunoreactive ∼23- to ∼27-kDa bands. Immunoblotting with N-t TDP-43 pAb ( F ) shows the collapse of the 45-kDa band, but no evidence for low molecular weight species. This indicates that pathological, sarkosyl-insoluble TDP-43 is abnormally phosphorylated and that low molecular weight pathological bands contain extreme C-t TDP-43 fragments.
    Polyclonal Antibody Pab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 89/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology polyclonal antibody pab c20
    Biochemical characterization of novel termini-specific TDP-43 <t>polyclonal</t> antibodies. A: Schematic diagram of TDP-43 indicating the relative position of the peptides used to generate the pAbs against N-t and C-t regions. The diagram also shows, in scale, the most prominent features of the protein (domains and predicted localization signals). NLS, nuclear localization signal; NES, nuclear export signal; RRM, RNA-recognition motif; Gly-rich, glycine-rich domain. B and C: Representative images showing the immunoblotting pattern for TDP-43 antibodies using T7-tagged recombinant human TDP-43 (C-terminally truncated or full length) ( B ) or radioimmunoprecipitation assay (RIPA) lysates from QBI293 cells ( C ). D–F: TDP-43 immunobotting of sarkosyl-insoluble fractions from different FTLD-U subtype cases before (−) and after (+) alkaline phosphatase (AP) treatment. Proteins from frontal cortex of FTLD-U cases were sequentially extracted with buffers of increasing strength and subjected to SDS-polyacrylamide gel electrophoresis. Dephosphorylation of FTLD-U urea extracts with AP followed by immunoblotting with pan TDP-43 ( D ) and C-t TDP-43 <t>pAb</t> ( E ) collapsed the 45-kDa band into the 43-kDa band and separated TDP-43 fragments into four immunoreactive ∼23- to ∼27-kDa bands. Immunoblotting with N-t TDP-43 pAb ( F ) shows the collapse of the 45-kDa band, but no evidence for low molecular weight species. This indicates that pathological, sarkosyl-insoluble TDP-43 is abnormally phosphorylated and that low molecular weight pathological bands contain extreme C-t TDP-43 fragments.
    Polyclonal Antibody Pab C20, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 85/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    R&D Systems msln polyclonal antibody pab
    Mesothelin Immunoassay using A) covalently immobilized <t>pAb</t> for antigen capture and fluorescently labelled scFv for display, and B) covalently immobilized scFv for capture and fluorescently labelled pAb as display of increasing concentrations of <t>MSLN</t> spiked in PBS buffer (■), and 50% human serum / 50% PBS buffer (▲). The assay dynamic ranges are determined by non-specific adsorption of display agents onto PEGylated particle platform surface (background noise, ◊), and unmodified particles (expected maximum signal, ♦)
    Msln Polyclonal Antibody Pab, supplied by R&D Systems, used in various techniques. Bioz Stars score: 85/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    InvivoGen polyclonal antibody pab control
    Mesothelin Immunoassay using A) covalently immobilized <t>pAb</t> for antigen capture and fluorescently labelled scFv for display, and B) covalently immobilized scFv for capture and fluorescently labelled pAb as display of increasing concentrations of <t>MSLN</t> spiked in PBS buffer (■), and 50% human serum / 50% PBS buffer (▲). The assay dynamic ranges are determined by non-specific adsorption of display agents onto PEGylated particle platform surface (background noise, ◊), and unmodified particles (expected maximum signal, ♦)
    Polyclonal Antibody Pab Control, supplied by InvivoGen, used in various techniques. Bioz Stars score: 93/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cedarlane polyclonal antibodies pab
    Mesothelin Immunoassay using A) covalently immobilized <t>pAb</t> for antigen capture and fluorescently labelled scFv for display, and B) covalently immobilized scFv for capture and fluorescently labelled pAb as display of increasing concentrations of <t>MSLN</t> spiked in PBS buffer (■), and 50% human serum / 50% PBS buffer (▲). The assay dynamic ranges are determined by non-specific adsorption of display agents onto PEGylated particle platform surface (background noise, ◊), and unmodified particles (expected maximum signal, ♦)
    Polyclonal Antibodies Pab, supplied by Cedarlane, used in various techniques. Bioz Stars score: 85/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Agilent technologies polyclonal antibody pab a0485
    Case 3 (A) Hematoxylin/eosin staining. (B) Circumferential, weak, incomplete membrane staining > 10% of tumor cells obtained by the PC-7 using the Herceptest (score 2+). (C) Faint, barely perceptible incomplete membrane staining in > 10% of tumor cells obtained by the RC using the MAb 4B5 (score 1+). (D) Circumferential, weak, incomplete membrane staining > 10% of tumor cells obtained by the RC using the <t>PAb</t> <t>A0485</t> (score 2+; original magnification ×20). Tables report the pathology consensus for each IHC slide.
    Polyclonal Antibody Pab A0485, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 88/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology src polyclonal antibody pab
    VarV recruits host cell factors required for actin polymerization. (a) Image of 3T3 cell infected with VarV-BSH and stained with FITC-phalloidin to visualize actin (green), with pY MAb (red), and with DAPI to visualize DNA (blue). (b to i) Images of actin tails on 3T3 cells infected with VarV strain BSH or SLN and stained with FITC-phalloidin (green) and the following antibodies against cellular and viral proteins (red): B5R MAb (b), <t>Src</t> <t>PAb</t> (c), Fyn MAb (d), Yes MAb (e), Abl1 MAb (f), Grb2 PAb (g), Nck MAb (h), and Abl2 MAb (i). Panels j to l depict DAPI staining (blue) at the tips of tails from panels g to i. Bars, 5 μm (a) and 1 μm (b to i).
    Src Polyclonal Antibody Pab, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher kif17 polyclonal antibody pab
    VarV recruits host cell factors required for actin polymerization. (a) Image of 3T3 cell infected with VarV-BSH and stained with FITC-phalloidin to visualize actin (green), with pY MAb (red), and with DAPI to visualize DNA (blue). (b to i) Images of actin tails on 3T3 cells infected with VarV strain BSH or SLN and stained with FITC-phalloidin (green) and the following antibodies against cellular and viral proteins (red): B5R MAb (b), <t>Src</t> <t>PAb</t> (c), Fyn MAb (d), Yes MAb (e), Abl1 MAb (f), Grb2 PAb (g), Nck MAb (h), and Abl2 MAb (i). Panels j to l depict DAPI staining (blue) at the tips of tails from panels g to i. Bars, 5 μm (a) and 1 μm (b to i).
    Kif17 Polyclonal Antibody Pab, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher rabbit polyclonal antibody pab
    Bacteria cells are separated by MMSs coupled with specific peptides or <t>polyclonal</t> antibodies. Notes: The fluorescent signal of QDs can be detected for imaging. The principle of the assay is based upon the conformation of the ternary complex, composed of bacterial cells, MMSs coupled with H 37 R v binding peptides as well as the polyclonal antibodies, and QDs conjugated with H 37 R v binding peptides or the monoclonal antibodies. Upon magnetic separation by MMSs, the complexes are tagged with functional QDs for detection of the fluorescent signal. Abbreviations: MMSs, magnetic microspheres; QDs, quantum dots.
    Rabbit Polyclonal Antibody Pab, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Upstate Biotechnology Inc materials polyclonal antibody pab myc
    Bacteria cells are separated by MMSs coupled with specific peptides or <t>polyclonal</t> antibodies. Notes: The fluorescent signal of QDs can be detected for imaging. The principle of the assay is based upon the conformation of the ternary complex, composed of bacterial cells, MMSs coupled with H 37 R v binding peptides as well as the polyclonal antibodies, and QDs conjugated with H 37 R v binding peptides or the monoclonal antibodies. Upon magnetic separation by MMSs, the complexes are tagged with functional QDs for detection of the fluorescent signal. Abbreviations: MMSs, magnetic microspheres; QDs, quantum dots.
    Materials Polyclonal Antibody Pab Myc, supplied by Upstate Biotechnology Inc, used in various techniques. Bioz Stars score: 85/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher 3nt pab
    Bacteria cells are separated by MMSs coupled with specific peptides or <t>polyclonal</t> antibodies. Notes: The fluorescent signal of QDs can be detected for imaging. The principle of the assay is based upon the conformation of the ternary complex, composed of bacterial cells, MMSs coupled with H 37 R v binding peptides as well as the polyclonal antibodies, and QDs conjugated with H 37 R v binding peptides or the monoclonal antibodies. Upon magnetic separation by MMSs, the complexes are tagged with functional QDs for detection of the fluorescent signal. Abbreviations: MMSs, magnetic microspheres; QDs, quantum dots.
    3nt Pab, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology stat1 polyclonal antibody pab
    Bacteria cells are separated by MMSs coupled with specific peptides or <t>polyclonal</t> antibodies. Notes: The fluorescent signal of QDs can be detected for imaging. The principle of the assay is based upon the conformation of the ternary complex, composed of bacterial cells, MMSs coupled with H 37 R v binding peptides as well as the polyclonal antibodies, and QDs conjugated with H 37 R v binding peptides or the monoclonal antibodies. Upon magnetic separation by MMSs, the complexes are tagged with functional QDs for detection of the fluorescent signal. Abbreviations: MMSs, magnetic microspheres; QDs, quantum dots.
    Stat1 Polyclonal Antibody Pab, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 85/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher rab11 pabs
    Bacteria cells are separated by MMSs coupled with specific peptides or <t>polyclonal</t> antibodies. Notes: The fluorescent signal of QDs can be detected for imaging. The principle of the assay is based upon the conformation of the ternary complex, composed of bacterial cells, MMSs coupled with H 37 R v binding peptides as well as the polyclonal antibodies, and QDs conjugated with H 37 R v binding peptides or the monoclonal antibodies. Upon magnetic separation by MMSs, the complexes are tagged with functional QDs for detection of the fluorescent signal. Abbreviations: MMSs, magnetic microspheres; QDs, quantum dots.
    Rab11 Pabs, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Swant calbindin polyclonal antibody pab
    Bacteria cells are separated by MMSs coupled with specific peptides or <t>polyclonal</t> antibodies. Notes: The fluorescent signal of QDs can be detected for imaging. The principle of the assay is based upon the conformation of the ternary complex, composed of bacterial cells, MMSs coupled with H 37 R v binding peptides as well as the polyclonal antibodies, and QDs conjugated with H 37 R v binding peptides or the monoclonal antibodies. Upon magnetic separation by MMSs, the complexes are tagged with functional QDs for detection of the fluorescent signal. Abbreviations: MMSs, magnetic microspheres; QDs, quantum dots.
    Calbindin Polyclonal Antibody Pab, supplied by Swant, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Novocastra polyclonal antibodies pabs
    Bacteria cells are separated by MMSs coupled with specific peptides or <t>polyclonal</t> antibodies. Notes: The fluorescent signal of QDs can be detected for imaging. The principle of the assay is based upon the conformation of the ternary complex, composed of bacterial cells, MMSs coupled with H 37 R v binding peptides as well as the polyclonal antibodies, and QDs conjugated with H 37 R v binding peptides or the monoclonal antibodies. Upon magnetic separation by MMSs, the complexes are tagged with functional QDs for detection of the fluorescent signal. Abbreviations: MMSs, magnetic microspheres; QDs, quantum dots.
    Polyclonal Antibodies Pabs, supplied by Novocastra, used in various techniques. Bioz Stars score: 89/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Agilent technologies polyclonal antibody pab
    Cerebrospinal fluid (CSF) levels of compleasome in herpes simplex encephalitis (HSE) patients, separated into early, acute (12 samples from 8 patients) and late infection (42 samples from 22 patients). The complex was measured with sandwich enzyme-linked immunosorbent assay (ELISA) using monoclonal antibody (mAb) against proteasome subunit 20Sα6 as catching antibody and <t>polyclonal</t> antibody <t>(pAb)</t> against complement factor 3 (C3) as detecting antibody. a Samples of CSF collected early in the infection at the acute phase had significantly higher levels of compleasome compared with samples collected more than 10 days after onset of symptoms. b Data from late infection were further separated into 11–30 days and 31–523 days after onset of symptoms. The level of compleasome had significantly decreased in the CSF samples collected after the first 30 days. Data are expressed as mean ± standard deviation (SD). Significant differences ( p
    Polyclonal Antibody Pab, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 92/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology polyclonal antibody pab
    The effect of amitriptyline on FGF-2 production in cortical astrocyte cultures. A, The time course of amitriptyline (Ami)-induced FGF-2 production. Cells were treated with 25 µM of Ami for the indicated periods of time, and the FGF-2 protein levels were analyzed by an immunoblotting analysis using a <t>polyclonal</t> antibody <t>(pAb)</t> against FGF-2 (Santa Cruz Biotechnology). The β-actin levels were used as a loading control. Immunoblots from a representative experiment are shown. B, Quantitation of the protein levels in Fig. A. The values are shown as the ratio of FGF-2 to β-actin. The data are expressed as the means ± S.E.M. * p
    Polyclonal Antibody Pab, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 89/100, based on 60 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Virostat anti momp polyclonal antibodies pab
    PmpD translation, processing, and secretion. McCoy cells infected with C. trachomatis serovar L2 were harvested at 6, 12, 24, 36, and 48 hours after infection and soluble and insoluble protein fractions separated. A. The insoluble fractions were loaded for equal <t>MOMP</t> amounts. B. The soluble fractions were loaded as described in METHODS. Both nitrocellulose membranes were reacted with antibodies against fragment 2 of PmpD. Lane 1, 0 h p.i. (uninfected cells). Lane 2, 6 h p.i. Lane 3, 12 h p.i. Lane 4, 24 h p.i. Lane 5, 36 h p.i. Lane 6, 48 h p.i. Reaction of MOMP used for the total protein normalization in the insoluble fractions, with anti-MOMP <t>pAb</t> is shown in a separate box. The quantity of MOMP was determined using the Packard Instrument OptiQuant software (version 03.10).
    Anti Momp Polyclonal Antibodies Pab, supplied by Virostat, used in various techniques. Bioz Stars score: 85/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Enzo Biochem polyclonal antibody pab
    PmpD translation, processing, and secretion. McCoy cells infected with C. trachomatis serovar L2 were harvested at 6, 12, 24, 36, and 48 hours after infection and soluble and insoluble protein fractions separated. A. The insoluble fractions were loaded for equal <t>MOMP</t> amounts. B. The soluble fractions were loaded as described in METHODS. Both nitrocellulose membranes were reacted with antibodies against fragment 2 of PmpD. Lane 1, 0 h p.i. (uninfected cells). Lane 2, 6 h p.i. Lane 3, 12 h p.i. Lane 4, 24 h p.i. Lane 5, 36 h p.i. Lane 6, 48 h p.i. Reaction of MOMP used for the total protein normalization in the insoluble fractions, with anti-MOMP <t>pAb</t> is shown in a separate box. The quantity of MOMP was determined using the Packard Instrument OptiQuant software (version 03.10).
    Polyclonal Antibody Pab, supplied by Enzo Biochem, used in various techniques. Bioz Stars score: 94/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Biochemical characterization of novel termini-specific TDP-43 polyclonal antibodies. A: Schematic diagram of TDP-43 indicating the relative position of the peptides used to generate the pAbs against N-t and C-t regions. The diagram also shows, in scale, the most prominent features of the protein (domains and predicted localization signals). NLS, nuclear localization signal; NES, nuclear export signal; RRM, RNA-recognition motif; Gly-rich, glycine-rich domain. B and C: Representative images showing the immunoblotting pattern for TDP-43 antibodies using T7-tagged recombinant human TDP-43 (C-terminally truncated or full length) ( B ) or radioimmunoprecipitation assay (RIPA) lysates from QBI293 cells ( C ). D–F: TDP-43 immunobotting of sarkosyl-insoluble fractions from different FTLD-U subtype cases before (−) and after (+) alkaline phosphatase (AP) treatment. Proteins from frontal cortex of FTLD-U cases were sequentially extracted with buffers of increasing strength and subjected to SDS-polyacrylamide gel electrophoresis. Dephosphorylation of FTLD-U urea extracts with AP followed by immunoblotting with pan TDP-43 ( D ) and C-t TDP-43 pAb ( E ) collapsed the 45-kDa band into the 43-kDa band and separated TDP-43 fragments into four immunoreactive ∼23- to ∼27-kDa bands. Immunoblotting with N-t TDP-43 pAb ( F ) shows the collapse of the 45-kDa band, but no evidence for low molecular weight species. This indicates that pathological, sarkosyl-insoluble TDP-43 is abnormally phosphorylated and that low molecular weight pathological bands contain extreme C-t TDP-43 fragments.

    Journal: The American Journal of Pathology

    Article Title: Enrichment of C-Terminal Fragments in TAR DNA-Binding Protein-43 Cytoplasmic Inclusions in Brain but not in Spinal Cord of Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

    doi: 10.2353/ajpath.2008.080003

    Figure Lengend Snippet: Biochemical characterization of novel termini-specific TDP-43 polyclonal antibodies. A: Schematic diagram of TDP-43 indicating the relative position of the peptides used to generate the pAbs against N-t and C-t regions. The diagram also shows, in scale, the most prominent features of the protein (domains and predicted localization signals). NLS, nuclear localization signal; NES, nuclear export signal; RRM, RNA-recognition motif; Gly-rich, glycine-rich domain. B and C: Representative images showing the immunoblotting pattern for TDP-43 antibodies using T7-tagged recombinant human TDP-43 (C-terminally truncated or full length) ( B ) or radioimmunoprecipitation assay (RIPA) lysates from QBI293 cells ( C ). D–F: TDP-43 immunobotting of sarkosyl-insoluble fractions from different FTLD-U subtype cases before (−) and after (+) alkaline phosphatase (AP) treatment. Proteins from frontal cortex of FTLD-U cases were sequentially extracted with buffers of increasing strength and subjected to SDS-polyacrylamide gel electrophoresis. Dephosphorylation of FTLD-U urea extracts with AP followed by immunoblotting with pan TDP-43 ( D ) and C-t TDP-43 pAb ( E ) collapsed the 45-kDa band into the 43-kDa band and separated TDP-43 fragments into four immunoreactive ∼23- to ∼27-kDa bands. Immunoblotting with N-t TDP-43 pAb ( F ) shows the collapse of the 45-kDa band, but no evidence for low molecular weight species. This indicates that pathological, sarkosyl-insoluble TDP-43 is abnormally phosphorylated and that low molecular weight pathological bands contain extreme C-t TDP-43 fragments.

    Article Snippet: Two polyclonal antibodies (pAb) were produced by immunizing rabbits (Covance Research Products, Inc., Denver, PA).

    Techniques: Recombinant, Radio Immunoprecipitation, Polyacrylamide Gel Electrophoresis, De-Phosphorylation Assay, Molecular Weight

    Semiquantitative analysis of TDP-43-positive pathology in FTLD-U and ALS cases reveal differential enrichment of C-t fragments in brain regions. Scatter plots illustrating individual values and means of the neuropathological immunoreactivity scores for pan-TDP-43 (crosses), C-t TDP-43 (dots), and N-t TDP-43 (triangles) polyclonal antibodies. A: TDP-43 pathology score values from FTLD-U cases in frontal cortex gray matter ( left ), hippocampal dentate gyrus ( middle ), and lower motor neurons (LMN) in spinal cord ( right ). B: Comparable data sets compiled from FTLD-U with MND cases. C: Data from ALS cases. * P

    Journal: The American Journal of Pathology

    Article Title: Enrichment of C-Terminal Fragments in TAR DNA-Binding Protein-43 Cytoplasmic Inclusions in Brain but not in Spinal Cord of Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

    doi: 10.2353/ajpath.2008.080003

    Figure Lengend Snippet: Semiquantitative analysis of TDP-43-positive pathology in FTLD-U and ALS cases reveal differential enrichment of C-t fragments in brain regions. Scatter plots illustrating individual values and means of the neuropathological immunoreactivity scores for pan-TDP-43 (crosses), C-t TDP-43 (dots), and N-t TDP-43 (triangles) polyclonal antibodies. A: TDP-43 pathology score values from FTLD-U cases in frontal cortex gray matter ( left ), hippocampal dentate gyrus ( middle ), and lower motor neurons (LMN) in spinal cord ( right ). B: Comparable data sets compiled from FTLD-U with MND cases. C: Data from ALS cases. * P

    Article Snippet: Two polyclonal antibodies (pAb) were produced by immunizing rabbits (Covance Research Products, Inc., Denver, PA).

    Techniques:

    Mesothelin Immunoassay using A) covalently immobilized pAb for antigen capture and fluorescently labelled scFv for display, and B) covalently immobilized scFv for capture and fluorescently labelled pAb as display of increasing concentrations of MSLN spiked in PBS buffer (■), and 50% human serum / 50% PBS buffer (▲). The assay dynamic ranges are determined by non-specific adsorption of display agents onto PEGylated particle platform surface (background noise, ◊), and unmodified particles (expected maximum signal, ♦)

    Journal: Langmuir : the ACS journal of surfaces and colloids

    Article Title: Antifouling Surface Layers for Improved Signal-to-Noise of Particle-Based Immunoassays

    doi: 10.1021/la903148n

    Figure Lengend Snippet: Mesothelin Immunoassay using A) covalently immobilized pAb for antigen capture and fluorescently labelled scFv for display, and B) covalently immobilized scFv for capture and fluorescently labelled pAb as display of increasing concentrations of MSLN spiked in PBS buffer (■), and 50% human serum / 50% PBS buffer (▲). The assay dynamic ranges are determined by non-specific adsorption of display agents onto PEGylated particle platform surface (background noise, ◊), and unmodified particles (expected maximum signal, ♦)

    Article Snippet: The MSLN polyclonal antibody (pAb) was purchased from R & D systems (USA).

    Techniques: Adsorption

    Case 3 (A) Hematoxylin/eosin staining. (B) Circumferential, weak, incomplete membrane staining > 10% of tumor cells obtained by the PC-7 using the Herceptest (score 2+). (C) Faint, barely perceptible incomplete membrane staining in > 10% of tumor cells obtained by the RC using the MAb 4B5 (score 1+). (D) Circumferential, weak, incomplete membrane staining > 10% of tumor cells obtained by the RC using the PAb A0485 (score 2+; original magnification ×20). Tables report the pathology consensus for each IHC slide.

    Journal: Medicine

    Article Title: HER2 Status Determination: Analyzing the Problems to Find the Solutions

    doi: 10.1097/MD.0000000000000645

    Figure Lengend Snippet: Case 3 (A) Hematoxylin/eosin staining. (B) Circumferential, weak, incomplete membrane staining > 10% of tumor cells obtained by the PC-7 using the Herceptest (score 2+). (C) Faint, barely perceptible incomplete membrane staining in > 10% of tumor cells obtained by the RC using the MAb 4B5 (score 1+). (D) Circumferential, weak, incomplete membrane staining > 10% of tumor cells obtained by the RC using the PAb A0485 (score 2+; original magnification ×20). Tables report the pathology consensus for each IHC slide.

    Article Snippet: In particular, 3 PCs used the polyclonal antibody (PAb) A0485 ( Dako, Milan Italy), 2 used the Hercep Test kit (Dako), 3 the monoclonal antibody (MAb) 4B5 (Ventana, Roche Diagnostics, Milan, Italy), and 1 used the MAb CB11 (Leica, Oracle, Milan, Italy) (Figure B).

    Techniques: Staining, Immunohistochemistry

    Case 1 (A) Hematoxylin/eosin staining. (B) Faint, barely perceptible incomplete membrane staining ≤10% of tumor cells obtained by the PC-4 using the MAb CB11 (score 0). (C) No immunoreactivity obtained by the RC using the MAb 4B5 (score 0). (D) Aspecific cytoplasmic immunostaining obtained by RC using the PAb A0485 (original magnification ×20). Case 2 (E) Faint, barely perceptible incomplete membrane staining in > 10% of tumor cells obtained by the PC-1 using the PAb A0485 (score 1+). (F) Faint, barely perceptible incomplete membrane staining > 10% of tumor cells obtained by the RC using the MAb 4B5 (score 1+). (G) Circumferential weak, incomplete membrane staining > 10% of tumor cells obtained by the RC using the PAb A0485 (score 2+; original magnification ×20). (H) DDISH showing a ratio

    Journal: Medicine

    Article Title: HER2 Status Determination: Analyzing the Problems to Find the Solutions

    doi: 10.1097/MD.0000000000000645

    Figure Lengend Snippet: Case 1 (A) Hematoxylin/eosin staining. (B) Faint, barely perceptible incomplete membrane staining ≤10% of tumor cells obtained by the PC-4 using the MAb CB11 (score 0). (C) No immunoreactivity obtained by the RC using the MAb 4B5 (score 0). (D) Aspecific cytoplasmic immunostaining obtained by RC using the PAb A0485 (original magnification ×20). Case 2 (E) Faint, barely perceptible incomplete membrane staining in > 10% of tumor cells obtained by the PC-1 using the PAb A0485 (score 1+). (F) Faint, barely perceptible incomplete membrane staining > 10% of tumor cells obtained by the RC using the MAb 4B5 (score 1+). (G) Circumferential weak, incomplete membrane staining > 10% of tumor cells obtained by the RC using the PAb A0485 (score 2+; original magnification ×20). (H) DDISH showing a ratio

    Article Snippet: In particular, 3 PCs used the polyclonal antibody (PAb) A0485 ( Dako, Milan Italy), 2 used the Hercep Test kit (Dako), 3 the monoclonal antibody (MAb) 4B5 (Ventana, Roche Diagnostics, Milan, Italy), and 1 used the MAb CB11 (Leica, Oracle, Milan, Italy) (Figure B).

    Techniques: Staining, Immunostaining

    Case 4 (A) Hematoxylin/eosin staining (PC-2, original magnification ×4). (B) IHC HER2 staining fading from the periphery to the center (original magnification ×10). (C–H) Circumferential moderate, incomplete membrane staining of tumor cells associated with a specific cytoplasmic staining obtained by the PC-9 and by the RC using both the MAb 4B5 and the PAb A0485 (score 2+; original magnification ×20). Tables report the pathology consensus for each IHC slide.

    Journal: Medicine

    Article Title: HER2 Status Determination: Analyzing the Problems to Find the Solutions

    doi: 10.1097/MD.0000000000000645

    Figure Lengend Snippet: Case 4 (A) Hematoxylin/eosin staining (PC-2, original magnification ×4). (B) IHC HER2 staining fading from the periphery to the center (original magnification ×10). (C–H) Circumferential moderate, incomplete membrane staining of tumor cells associated with a specific cytoplasmic staining obtained by the PC-9 and by the RC using both the MAb 4B5 and the PAb A0485 (score 2+; original magnification ×20). Tables report the pathology consensus for each IHC slide.

    Article Snippet: In particular, 3 PCs used the polyclonal antibody (PAb) A0485 ( Dako, Milan Italy), 2 used the Hercep Test kit (Dako), 3 the monoclonal antibody (MAb) 4B5 (Ventana, Roche Diagnostics, Milan, Italy), and 1 used the MAb CB11 (Leica, Oracle, Milan, Italy) (Figure B).

    Techniques: Staining, Immunohistochemistry

    VarV recruits host cell factors required for actin polymerization. (a) Image of 3T3 cell infected with VarV-BSH and stained with FITC-phalloidin to visualize actin (green), with pY MAb (red), and with DAPI to visualize DNA (blue). (b to i) Images of actin tails on 3T3 cells infected with VarV strain BSH or SLN and stained with FITC-phalloidin (green) and the following antibodies against cellular and viral proteins (red): B5R MAb (b), Src PAb (c), Fyn MAb (d), Yes MAb (e), Abl1 MAb (f), Grb2 PAb (g), Nck MAb (h), and Abl2 MAb (i). Panels j to l depict DAPI staining (blue) at the tips of tails from panels g to i. Bars, 5 μm (a) and 1 μm (b to i).

    Journal: Journal of Virology

    Article Title: Variola and Monkeypox Viruses Utilize Conserved Mechanisms of Virion Motility and Release That Depend on Abl and Src Family Tyrosine Kinases ▿Variola and Monkeypox Viruses Utilize Conserved Mechanisms of Virion Motility and Release That Depend on Abl and Src Family Tyrosine Kinases ▿ †

    doi: 10.1128/JVI.01814-10

    Figure Lengend Snippet: VarV recruits host cell factors required for actin polymerization. (a) Image of 3T3 cell infected with VarV-BSH and stained with FITC-phalloidin to visualize actin (green), with pY MAb (red), and with DAPI to visualize DNA (blue). (b to i) Images of actin tails on 3T3 cells infected with VarV strain BSH or SLN and stained with FITC-phalloidin (green) and the following antibodies against cellular and viral proteins (red): B5R MAb (b), Src PAb (c), Fyn MAb (d), Yes MAb (e), Abl1 MAb (f), Grb2 PAb (g), Nck MAb (h), and Abl2 MAb (i). Panels j to l depict DAPI staining (blue) at the tips of tails from panels g to i. Bars, 5 μm (a) and 1 μm (b to i).

    Article Snippet: The primary antibodies and concentrations used in this study were as follows: Nck monoclonal antibody (MAb) (1 μg/ml; Oncogene Research), Abl1 MAb (8E9) (0.05 μg/ml; Pharmingen), Src polyclonal antibody (PAb) (0.1 μg/ml; Santa Cruz), Fyn MAb (0.1 μg/ml; Abcam), Yes PAb (0.1 μg/ml; Cell Signaling), Abl2 PAb (1:200; UBI), Grb2 MAb (3F2) (1:200), and phosphotyrosine MAb (4g10) (1:200); the specificity of anti-kinase antibodies was confirmed by staining cell lines lacking particular kinases ( ).

    Techniques: Infection, Staining

    Bacteria cells are separated by MMSs coupled with specific peptides or polyclonal antibodies. Notes: The fluorescent signal of QDs can be detected for imaging. The principle of the assay is based upon the conformation of the ternary complex, composed of bacterial cells, MMSs coupled with H 37 R v binding peptides as well as the polyclonal antibodies, and QDs conjugated with H 37 R v binding peptides or the monoclonal antibodies. Upon magnetic separation by MMSs, the complexes are tagged with functional QDs for detection of the fluorescent signal. Abbreviations: MMSs, magnetic microspheres; QDs, quantum dots.

    Journal: International Journal of Nanomedicine

    Article Title: Detection of Mycobacterium tuberculosis based on H37Rv binding peptides using surface functionalized magnetic microspheres coupled with quantum dots – a nano detection method for Mycobacterium tuberculosis

    doi: 10.2147/IJN.S71700

    Figure Lengend Snippet: Bacteria cells are separated by MMSs coupled with specific peptides or polyclonal antibodies. Notes: The fluorescent signal of QDs can be detected for imaging. The principle of the assay is based upon the conformation of the ternary complex, composed of bacterial cells, MMSs coupled with H 37 R v binding peptides as well as the polyclonal antibodies, and QDs conjugated with H 37 R v binding peptides or the monoclonal antibodies. Upon magnetic separation by MMSs, the complexes are tagged with functional QDs for detection of the fluorescent signal. Abbreviations: MMSs, magnetic microspheres; QDs, quantum dots.

    Article Snippet: Antibodies The following antibodies were included in this study: a murine (mAb) and a rabbit polyclonal antibody (Pab), both against MTB along with a monoclonal antibody (mAbc) produced in murine against MTB heat shock protein 65, which reacts with related mycobacterial species, according to the manufacturer (Thermo Fisher Scientific, Waltham, MA, USA).

    Techniques: Imaging, Binding Assay, Functional Assay

    LOD detection for six combinations of MMSs coupled with H8 or Pab and QDs conjugated with H8, Mab, or mabc. Notes: Differences in MTB detection capability between the combinations were evident for a range of MTB concentrations in the test. Combinations of MMS-H8+QD-mAb and MMS-Pab+QD-mAbc produced a strong signal for only 10 7 CFU/mL H 37 R v cells, indicating relatively poor MTB detection capability. Combinations of MMS-H8+QD-mAbc and MMS-Pab+QD-mAb exhibited a higher but decreasing fluorescence intensity of H 37 R v for 10 5 CFU/mL or 10 6 CFU/mL, showing improved MTB detection capability. Combinations of MMS-Pab+QD-H8 and MMS-H8+QD-H8 yield a significantly higher signal for 10 3 CFU/mL H 37 R v and thus demonstrated the best MTB detection capability. Abbreviations: LOD, limit of detection; MMSs, magnetic microspheres; QDs, quantum dots; Pab, a rabbit polyclonal antibody against MTB; mAb, a murine monoclonal antibody against MTB; mAbc, a murine monoclonal antibody against MTB heat shock protein 65 (HSP65); CFU, colony-forming unit; mAbc, .

    Journal: International Journal of Nanomedicine

    Article Title: Detection of Mycobacterium tuberculosis based on H37Rv binding peptides using surface functionalized magnetic microspheres coupled with quantum dots – a nano detection method for Mycobacterium tuberculosis

    doi: 10.2147/IJN.S71700

    Figure Lengend Snippet: LOD detection for six combinations of MMSs coupled with H8 or Pab and QDs conjugated with H8, Mab, or mabc. Notes: Differences in MTB detection capability between the combinations were evident for a range of MTB concentrations in the test. Combinations of MMS-H8+QD-mAb and MMS-Pab+QD-mAbc produced a strong signal for only 10 7 CFU/mL H 37 R v cells, indicating relatively poor MTB detection capability. Combinations of MMS-H8+QD-mAbc and MMS-Pab+QD-mAb exhibited a higher but decreasing fluorescence intensity of H 37 R v for 10 5 CFU/mL or 10 6 CFU/mL, showing improved MTB detection capability. Combinations of MMS-Pab+QD-H8 and MMS-H8+QD-H8 yield a significantly higher signal for 10 3 CFU/mL H 37 R v and thus demonstrated the best MTB detection capability. Abbreviations: LOD, limit of detection; MMSs, magnetic microspheres; QDs, quantum dots; Pab, a rabbit polyclonal antibody against MTB; mAb, a murine monoclonal antibody against MTB; mAbc, a murine monoclonal antibody against MTB heat shock protein 65 (HSP65); CFU, colony-forming unit; mAbc, .

    Article Snippet: Antibodies The following antibodies were included in this study: a murine (mAb) and a rabbit polyclonal antibody (Pab), both against MTB along with a monoclonal antibody (mAbc) produced in murine against MTB heat shock protein 65, which reacts with related mycobacterial species, according to the manufacturer (Thermo Fisher Scientific, Waltham, MA, USA).

    Techniques: Produced, Fluorescence

    Cerebrospinal fluid (CSF) levels of compleasome in herpes simplex encephalitis (HSE) patients, separated into early, acute (12 samples from 8 patients) and late infection (42 samples from 22 patients). The complex was measured with sandwich enzyme-linked immunosorbent assay (ELISA) using monoclonal antibody (mAb) against proteasome subunit 20Sα6 as catching antibody and polyclonal antibody (pAb) against complement factor 3 (C3) as detecting antibody. a Samples of CSF collected early in the infection at the acute phase had significantly higher levels of compleasome compared with samples collected more than 10 days after onset of symptoms. b Data from late infection were further separated into 11–30 days and 31–523 days after onset of symptoms. The level of compleasome had significantly decreased in the CSF samples collected after the first 30 days. Data are expressed as mean ± standard deviation (SD). Significant differences ( p

    Journal: Journal of Neurovirology

    Article Title: Increased level of compleasomes in cerebrospinal fluid of patients with herpes simplex encephalitis

    doi: 10.1007/s13365-018-0665-x

    Figure Lengend Snippet: Cerebrospinal fluid (CSF) levels of compleasome in herpes simplex encephalitis (HSE) patients, separated into early, acute (12 samples from 8 patients) and late infection (42 samples from 22 patients). The complex was measured with sandwich enzyme-linked immunosorbent assay (ELISA) using monoclonal antibody (mAb) against proteasome subunit 20Sα6 as catching antibody and polyclonal antibody (pAb) against complement factor 3 (C3) as detecting antibody. a Samples of CSF collected early in the infection at the acute phase had significantly higher levels of compleasome compared with samples collected more than 10 days after onset of symptoms. b Data from late infection were further separated into 11–30 days and 31–523 days after onset of symptoms. The level of compleasome had significantly decreased in the CSF samples collected after the first 30 days. Data are expressed as mean ± standard deviation (SD). Significant differences ( p

    Article Snippet: Polyclonal antibody (pAb) against proteasome 19S subunit was produced as previously described (Lonnroth et al. ), and pAb against C3 and C4 was obtained from Dako, Glostrup, Denmark.

    Techniques: Infection, Sandwich ELISA, Enzyme-linked Immunosorbent Assay, Standard Deviation

    Levels of compleasome complex in cerebrospinal fluid (CSF) samples from herpes simplex encephalitis (HSE) patients over time ( n = 13). The complex was measured with sandwich enzyme-linked immunosorbent assay (ELISA) using monoclonal antibody (mAb) against proteasome subunit 20Sα6 and polyclonal antibody (pAb) against complement factor 3 (C3) and is presented in relation to day of onset of neurological symptoms. Between two and ten samples of individual patients from different time points (collected 0–523 days after symptom onset) are presented. The inset shows a detailed graph of the CSF samples collected after 0–30 days. Median levels of compleasome complex in CSF of healthy controls (HCs) ( n = 23) are indicated with a dotted line and of patient controls (PCs) ( n = 27) with the dashed line

    Journal: Journal of Neurovirology

    Article Title: Increased level of compleasomes in cerebrospinal fluid of patients with herpes simplex encephalitis

    doi: 10.1007/s13365-018-0665-x

    Figure Lengend Snippet: Levels of compleasome complex in cerebrospinal fluid (CSF) samples from herpes simplex encephalitis (HSE) patients over time ( n = 13). The complex was measured with sandwich enzyme-linked immunosorbent assay (ELISA) using monoclonal antibody (mAb) against proteasome subunit 20Sα6 and polyclonal antibody (pAb) against complement factor 3 (C3) and is presented in relation to day of onset of neurological symptoms. Between two and ten samples of individual patients from different time points (collected 0–523 days after symptom onset) are presented. The inset shows a detailed graph of the CSF samples collected after 0–30 days. Median levels of compleasome complex in CSF of healthy controls (HCs) ( n = 23) are indicated with a dotted line and of patient controls (PCs) ( n = 27) with the dashed line

    Article Snippet: Polyclonal antibody (pAb) against proteasome 19S subunit was produced as previously described (Lonnroth et al. ), and pAb against C3 and C4 was obtained from Dako, Glostrup, Denmark.

    Techniques: Sandwich ELISA, Enzyme-linked Immunosorbent Assay

    Detection of compleasome complexes in cerebrospinal fluid (CSF) taken from healthy controls (HCs), patient controls (PCs) and herpes simplex encephalitis (HSE) patients using sandwich enzyme-linked immunosorbent assay (ELISA). The figure presents results from four combinations of antibodies using monoclonal antibodies (mAb) against proteasome subunit 20Sα6 or AF1 as catching antibodies and polyclonal antibodies (pAb) against complement factors 3 and 4 (C3 and C4) as detecting antibodies. The patients with HSE ( n = 23 or 24) had significantly higher values compared with the HCs ( n = 23) and also with the PCs ( n = 25 or 27) tested with all four combinations of compleasome antibodies. Data are expressed as mean absorbance values, buffer blank corrected, ± standard deviation (SD). Significant differences between the samples are indicated by * p

    Journal: Journal of Neurovirology

    Article Title: Increased level of compleasomes in cerebrospinal fluid of patients with herpes simplex encephalitis

    doi: 10.1007/s13365-018-0665-x

    Figure Lengend Snippet: Detection of compleasome complexes in cerebrospinal fluid (CSF) taken from healthy controls (HCs), patient controls (PCs) and herpes simplex encephalitis (HSE) patients using sandwich enzyme-linked immunosorbent assay (ELISA). The figure presents results from four combinations of antibodies using monoclonal antibodies (mAb) against proteasome subunit 20Sα6 or AF1 as catching antibodies and polyclonal antibodies (pAb) against complement factors 3 and 4 (C3 and C4) as detecting antibodies. The patients with HSE ( n = 23 or 24) had significantly higher values compared with the HCs ( n = 23) and also with the PCs ( n = 25 or 27) tested with all four combinations of compleasome antibodies. Data are expressed as mean absorbance values, buffer blank corrected, ± standard deviation (SD). Significant differences between the samples are indicated by * p

    Article Snippet: Polyclonal antibody (pAb) against proteasome 19S subunit was produced as previously described (Lonnroth et al. ), and pAb against C3 and C4 was obtained from Dako, Glostrup, Denmark.

    Techniques: Sandwich ELISA, Enzyme-linked Immunosorbent Assay, Standard Deviation

    The effect of amitriptyline on FGF-2 production in cortical astrocyte cultures. A, The time course of amitriptyline (Ami)-induced FGF-2 production. Cells were treated with 25 µM of Ami for the indicated periods of time, and the FGF-2 protein levels were analyzed by an immunoblotting analysis using a polyclonal antibody (pAb) against FGF-2 (Santa Cruz Biotechnology). The β-actin levels were used as a loading control. Immunoblots from a representative experiment are shown. B, Quantitation of the protein levels in Fig. A. The values are shown as the ratio of FGF-2 to β-actin. The data are expressed as the means ± S.E.M. * p

    Journal: PLoS ONE

    Article Title: Antidepressant Acts on Astrocytes Leading to an Increase in the Expression of Neurotrophic/Growth Factors: Differential Regulation of FGF-2 by Noradrenaline

    doi: 10.1371/journal.pone.0051197

    Figure Lengend Snippet: The effect of amitriptyline on FGF-2 production in cortical astrocyte cultures. A, The time course of amitriptyline (Ami)-induced FGF-2 production. Cells were treated with 25 µM of Ami for the indicated periods of time, and the FGF-2 protein levels were analyzed by an immunoblotting analysis using a polyclonal antibody (pAb) against FGF-2 (Santa Cruz Biotechnology). The β-actin levels were used as a loading control. Immunoblots from a representative experiment are shown. B, Quantitation of the protein levels in Fig. A. The values are shown as the ratio of FGF-2 to β-actin. The data are expressed as the means ± S.E.M. * p

    Article Snippet: The membranes were blocked in blocking buffer for 1.5 h at room temperature and subsequently incubated with a purified polyclonal antibody (pAb) against FGF-2 (1∶1000; Santa Cruz Biotechnology, Santa Cruz, CA), monoclonal antibody against FGF-2 (1∶250; BD Transduction Laboratories, Franklin Lakes, NJ) or β-actin (1∶10000; Sigma-Aldrich) overnight at 4°C.

    Techniques: Western Blot, Quantitation Assay

    PmpD translation, processing, and secretion. McCoy cells infected with C. trachomatis serovar L2 were harvested at 6, 12, 24, 36, and 48 hours after infection and soluble and insoluble protein fractions separated. A. The insoluble fractions were loaded for equal MOMP amounts. B. The soluble fractions were loaded as described in METHODS. Both nitrocellulose membranes were reacted with antibodies against fragment 2 of PmpD. Lane 1, 0 h p.i. (uninfected cells). Lane 2, 6 h p.i. Lane 3, 12 h p.i. Lane 4, 24 h p.i. Lane 5, 36 h p.i. Lane 6, 48 h p.i. Reaction of MOMP used for the total protein normalization in the insoluble fractions, with anti-MOMP pAb is shown in a separate box. The quantity of MOMP was determined using the Packard Instrument OptiQuant software (version 03.10).

    Journal: PLoS ONE

    Article Title: Expression, Processing, and Localization of PmpD of Chlamydia trachomatis Serovar L2 during the Chlamydial Developmental Cycle

    doi: 10.1371/journal.pone.0000568

    Figure Lengend Snippet: PmpD translation, processing, and secretion. McCoy cells infected with C. trachomatis serovar L2 were harvested at 6, 12, 24, 36, and 48 hours after infection and soluble and insoluble protein fractions separated. A. The insoluble fractions were loaded for equal MOMP amounts. B. The soluble fractions were loaded as described in METHODS. Both nitrocellulose membranes were reacted with antibodies against fragment 2 of PmpD. Lane 1, 0 h p.i. (uninfected cells). Lane 2, 6 h p.i. Lane 3, 12 h p.i. Lane 4, 24 h p.i. Lane 5, 36 h p.i. Lane 6, 48 h p.i. Reaction of MOMP used for the total protein normalization in the insoluble fractions, with anti-MOMP pAb is shown in a separate box. The quantity of MOMP was determined using the Packard Instrument OptiQuant software (version 03.10).

    Article Snippet: At 24 and 48 h p.i., cells were fixed with 100% methanol, washed in PBS, and reacted with antibodies against each fragment of PmpD, anti-MOMP polyclonal antibodies (pAb) (ViroStat, Portland, ME), and rabbit pre-immune sera diluted in 3% bovine serum albumin (BSA) in PBS for 1 h at room temperature.

    Techniques: Infection, Software

    Reaction of pAb generated against PmpD recombinant protein fragments with total protein lysates prepared from purified RBs and EBs of C. trachomatis serovar L2. RBs (Lanes 1, 3, 5, and 7) and EBs (Lanes 2, 4, 6, and 8) were normalized against MOMP as described in METHODS. Lanes 1 and 2, pAb against fragment 1; Lanes 3 and 4, pAb against fragment 2; Lanes 5 and 6, pAb against fragment 3; Lanes 7 and 8, pAb against fragment 4. Protein markers in kDa are on the right side of the Western blot image.

    Journal: PLoS ONE

    Article Title: Expression, Processing, and Localization of PmpD of Chlamydia trachomatis Serovar L2 during the Chlamydial Developmental Cycle

    doi: 10.1371/journal.pone.0000568

    Figure Lengend Snippet: Reaction of pAb generated against PmpD recombinant protein fragments with total protein lysates prepared from purified RBs and EBs of C. trachomatis serovar L2. RBs (Lanes 1, 3, 5, and 7) and EBs (Lanes 2, 4, 6, and 8) were normalized against MOMP as described in METHODS. Lanes 1 and 2, pAb against fragment 1; Lanes 3 and 4, pAb against fragment 2; Lanes 5 and 6, pAb against fragment 3; Lanes 7 and 8, pAb against fragment 4. Protein markers in kDa are on the right side of the Western blot image.

    Article Snippet: At 24 and 48 h p.i., cells were fixed with 100% methanol, washed in PBS, and reacted with antibodies against each fragment of PmpD, anti-MOMP polyclonal antibodies (pAb) (ViroStat, Portland, ME), and rabbit pre-immune sera diluted in 3% bovine serum albumin (BSA) in PBS for 1 h at room temperature.

    Techniques: Generated, Recombinant, Purification, Western Blot

    Processing of PmpD is inhibited in the presence of penicillin (A) and restored upon its removal (B). McCoy cells infected with C. trachomatis serovar L2 and incubated in the culture medium containing different doses of penicillin were harvested at 24 (A) or 48 (B) h p.i. and soluble and insoluble protein fractions separated. Both nitrocellulose membranes were reacted with pAb against fragment 2 of PmpD. A. Lines 1–5, the insoluble fractions were loaded for equal MOMP amounts (reaction with MOMP is shown in the small box). Lines 6–10, soluble fractions were loaded as described in METHODS. Lane 1 and 6, 0 penicillin. Lane 2 and 7, 0.01 U/ml penicillin. Lane 3 and 8, 0.1 U/ml penicillin. Lane 4 and 9, 1 U/ml penicillin. Lane 5 and 10, 10 U/ml penicillin. Note: a doublet of protein bands with molecular weights of ≈160 and 157 kDa is visible in both the insoluble and soluble fractions corresponding to penicillin concentrations of 0.1 U/ml and higher. B. Soluble fractions were loaded as described in METHODS. Lane1, 0 penicillin. Lane 2, 0.01 U/ml penicillin. Lane 3, 0.1 U/ml penicillin. Lane 4, 1 U/ml penicillin. Lane 5, 10 U/ml penicillin (indicated concentrations of penicillin were used before penicillin removal at 24 h p.i.). The quantity of MOMP and PmpD was determined using the Packard Instrument OptiQuant software (version 03.10).

    Journal: PLoS ONE

    Article Title: Expression, Processing, and Localization of PmpD of Chlamydia trachomatis Serovar L2 during the Chlamydial Developmental Cycle

    doi: 10.1371/journal.pone.0000568

    Figure Lengend Snippet: Processing of PmpD is inhibited in the presence of penicillin (A) and restored upon its removal (B). McCoy cells infected with C. trachomatis serovar L2 and incubated in the culture medium containing different doses of penicillin were harvested at 24 (A) or 48 (B) h p.i. and soluble and insoluble protein fractions separated. Both nitrocellulose membranes were reacted with pAb against fragment 2 of PmpD. A. Lines 1–5, the insoluble fractions were loaded for equal MOMP amounts (reaction with MOMP is shown in the small box). Lines 6–10, soluble fractions were loaded as described in METHODS. Lane 1 and 6, 0 penicillin. Lane 2 and 7, 0.01 U/ml penicillin. Lane 3 and 8, 0.1 U/ml penicillin. Lane 4 and 9, 1 U/ml penicillin. Lane 5 and 10, 10 U/ml penicillin. Note: a doublet of protein bands with molecular weights of ≈160 and 157 kDa is visible in both the insoluble and soluble fractions corresponding to penicillin concentrations of 0.1 U/ml and higher. B. Soluble fractions were loaded as described in METHODS. Lane1, 0 penicillin. Lane 2, 0.01 U/ml penicillin. Lane 3, 0.1 U/ml penicillin. Lane 4, 1 U/ml penicillin. Lane 5, 10 U/ml penicillin (indicated concentrations of penicillin were used before penicillin removal at 24 h p.i.). The quantity of MOMP and PmpD was determined using the Packard Instrument OptiQuant software (version 03.10).

    Article Snippet: At 24 and 48 h p.i., cells were fixed with 100% methanol, washed in PBS, and reacted with antibodies against each fragment of PmpD, anti-MOMP polyclonal antibodies (pAb) (ViroStat, Portland, ME), and rabbit pre-immune sera diluted in 3% bovine serum albumin (BSA) in PBS for 1 h at room temperature.

    Techniques: Infection, Incubation, Software

    Fluorescent photographs of unfixed RBs and EBs of C. trachomatis serovar L2. RBs (A, B, and C) and EBs (D, E, and F) were harvested and purified at 24 and 48 h p.i. respectively, and probed with pAb against fragment 2 of PmpD (A and D), anti-MOMP pAb (B and E), and rabbit pre-immune sera (C and F). Staining of EBs with anti-PmpD pAb was negligible while anti-MOMP Pab stained both RBs and EBs indicating that the PmpD passenger domain may be secreted during the conversion of RBs into EBs. The Figure was scanned using Image Pro-Plus 4.1 and prepared with Adobe Photoshop 6.0.

    Journal: PLoS ONE

    Article Title: Expression, Processing, and Localization of PmpD of Chlamydia trachomatis Serovar L2 during the Chlamydial Developmental Cycle

    doi: 10.1371/journal.pone.0000568

    Figure Lengend Snippet: Fluorescent photographs of unfixed RBs and EBs of C. trachomatis serovar L2. RBs (A, B, and C) and EBs (D, E, and F) were harvested and purified at 24 and 48 h p.i. respectively, and probed with pAb against fragment 2 of PmpD (A and D), anti-MOMP pAb (B and E), and rabbit pre-immune sera (C and F). Staining of EBs with anti-PmpD pAb was negligible while anti-MOMP Pab stained both RBs and EBs indicating that the PmpD passenger domain may be secreted during the conversion of RBs into EBs. The Figure was scanned using Image Pro-Plus 4.1 and prepared with Adobe Photoshop 6.0.

    Article Snippet: At 24 and 48 h p.i., cells were fixed with 100% methanol, washed in PBS, and reacted with antibodies against each fragment of PmpD, anti-MOMP polyclonal antibodies (pAb) (ViroStat, Portland, ME), and rabbit pre-immune sera diluted in 3% bovine serum albumin (BSA) in PBS for 1 h at room temperature.

    Techniques: Purification, Staining

    Fluorescent photographs of McCoy cells infected with C. trachomatis serovar L2. McCoy cells were methanol fixed at 24 (A, C, and E), and 48 (B, D, and F) h p.i. and probed with pAb against fragment 2 of PmpD (A and B), anti-MOMP PAb (C and D) and rabbit pre-immune sera (E and F). Ring shaped RBs of Chlamydia stained with anti-PmpD pAb indicate surface localization of PmpD in Chlamydia . Note: the lack of staining in the infected cell cytoplasm indicating that PmpD is not transported outside the inclusion. The Figure was scanned using Image Pro-Plus 4.1 and prepared with Adobe Photoshop 6.0.

    Journal: PLoS ONE

    Article Title: Expression, Processing, and Localization of PmpD of Chlamydia trachomatis Serovar L2 during the Chlamydial Developmental Cycle

    doi: 10.1371/journal.pone.0000568

    Figure Lengend Snippet: Fluorescent photographs of McCoy cells infected with C. trachomatis serovar L2. McCoy cells were methanol fixed at 24 (A, C, and E), and 48 (B, D, and F) h p.i. and probed with pAb against fragment 2 of PmpD (A and B), anti-MOMP PAb (C and D) and rabbit pre-immune sera (E and F). Ring shaped RBs of Chlamydia stained with anti-PmpD pAb indicate surface localization of PmpD in Chlamydia . Note: the lack of staining in the infected cell cytoplasm indicating that PmpD is not transported outside the inclusion. The Figure was scanned using Image Pro-Plus 4.1 and prepared with Adobe Photoshop 6.0.

    Article Snippet: At 24 and 48 h p.i., cells were fixed with 100% methanol, washed in PBS, and reacted with antibodies against each fragment of PmpD, anti-MOMP polyclonal antibodies (pAb) (ViroStat, Portland, ME), and rabbit pre-immune sera diluted in 3% bovine serum albumin (BSA) in PBS for 1 h at room temperature.

    Techniques: Infection, Staining