rabbit igg  (Bio-Rad)

 
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 95
    Name:
    Rabbit F ab 2 anti Human IgG H L Mouse Adsorbed
    Description:

    Catalog Number:
    STAR201
    Price:
    None
    Applications:
    ELISA, Immunofluorescence, Western Blotting
    Format:
    Purified
    Buy from Supplier


    Structured Review

    Bio-Rad rabbit igg
    PAK4 interacts with and phosphorylates N-WASP (A) PAK4 mediated phosphorylation was analyzed by an in vitro kinase assay using recombinant HIS-PAK4 together with the Arp2/3 complex (left panel) or GST-VCA (right panel) as substrates, with GST as a negative control and GST-RAF1 (332–344) as a positive control (upper panels). The lower panels display the protein loading in the assays by Coomassie Brilliant Blue staining. (B) HIS-PAK4 phosphorylation of the WASP VCA domain was analyzed using an anti-N-WASP pSer484/Ser485 antibody after a kinase assay using recombinant HIS-PAK4 with GST-VCA as a substrate. GST serves as a negative control, while the anti-RAF1 pSer338 antibody was used as a positive control to detect GST-RAF1 phosphorylated by PAK4 (upper panel). The lower panel shows the loading of HIS-PAK4 protein and GST-fusion proteins used in the assay by silver staining. (C) HIS-PAK4 was pulled-down in the presence of GST-VCA or the Arp2/3 complex with Ni-NTA agarose and input (I), supernatant (S) and pellet (P) analyzed by silver staining. (D) IP of EGFP control or EGFP-PAK4 transiently expressed in H1299 cells analyzed by immunoblotting using an anti-N-WASP antibody (upper panel right two lanes). The left two lanes show immunoblotting of the input lysates. <t>Anti-GFP</t> was used to control the expression and IP efficiency in the lower panel. (E) N-WASP was immunoprecipitated with an anti-N-WASP antibody from lysates of H1299 cells transiently expressing EGFP-PAK4 and samples were analyzed by immunoblot using an anti-GFP antibody with the lysate input to the left (upper panel). Anti-N-WASP was used to control the expression and IP efficiency in the lower panel. (F) PAK4 was immunoprecipitated with an anti-PAK4 antibody from lysates of MCF7 cells, with rabbit <t>IgG</t> as a control, samples were analyzed by immunoblot using an anti-N-WASP antibody with the lysate input to the left (upper panel). Anti-PAK4 blotting was used to control IP efficiency in the lower panel. (G) N-WASP was immunoprecipitated with an anti-N-WASP antibody from lysates of H1299 cells, with rabbit IgG as a control, samples were analyzed by immunoblot using an anti-PAK4 antibody with the lysate input to the left (upper panel). Anti-N-WASP blotting was used to control IP efficiency in the lower panel. (H) PAK4, N-WASP and F-actin co-localized in the cell periphery after re-plating. FLAG-PAK4 was labeled with an anti-FLAG mab (Green), N-WASP with an anti-N-WASP antibody (Red), F-actin with SiR-actin (Purple) and Nuclei with Hoechst (Blue), Scale bar: 10 μm.

    https://www.bioz.com/result/rabbit igg/product/Bio-Rad
    Average 95 stars, based on 33 article reviews
    Price from $9.99 to $1999.99
    rabbit igg - by Bioz Stars, 2020-09
    95/100 stars

    Images

    1) Product Images from "Identification of the PAK4 interactome reveals PAK4 phosphorylation of N-WASP and promotion of Arp2/3-dependent actin polymerization"

    Article Title: Identification of the PAK4 interactome reveals PAK4 phosphorylation of N-WASP and promotion of Arp2/3-dependent actin polymerization

    Journal: Oncotarget

    doi: 10.18632/oncotarget.20352

    PAK4 interacts with and phosphorylates N-WASP (A) PAK4 mediated phosphorylation was analyzed by an in vitro kinase assay using recombinant HIS-PAK4 together with the Arp2/3 complex (left panel) or GST-VCA (right panel) as substrates, with GST as a negative control and GST-RAF1 (332–344) as a positive control (upper panels). The lower panels display the protein loading in the assays by Coomassie Brilliant Blue staining. (B) HIS-PAK4 phosphorylation of the WASP VCA domain was analyzed using an anti-N-WASP pSer484/Ser485 antibody after a kinase assay using recombinant HIS-PAK4 with GST-VCA as a substrate. GST serves as a negative control, while the anti-RAF1 pSer338 antibody was used as a positive control to detect GST-RAF1 phosphorylated by PAK4 (upper panel). The lower panel shows the loading of HIS-PAK4 protein and GST-fusion proteins used in the assay by silver staining. (C) HIS-PAK4 was pulled-down in the presence of GST-VCA or the Arp2/3 complex with Ni-NTA agarose and input (I), supernatant (S) and pellet (P) analyzed by silver staining. (D) IP of EGFP control or EGFP-PAK4 transiently expressed in H1299 cells analyzed by immunoblotting using an anti-N-WASP antibody (upper panel right two lanes). The left two lanes show immunoblotting of the input lysates. Anti-GFP was used to control the expression and IP efficiency in the lower panel. (E) N-WASP was immunoprecipitated with an anti-N-WASP antibody from lysates of H1299 cells transiently expressing EGFP-PAK4 and samples were analyzed by immunoblot using an anti-GFP antibody with the lysate input to the left (upper panel). Anti-N-WASP was used to control the expression and IP efficiency in the lower panel. (F) PAK4 was immunoprecipitated with an anti-PAK4 antibody from lysates of MCF7 cells, with rabbit IgG as a control, samples were analyzed by immunoblot using an anti-N-WASP antibody with the lysate input to the left (upper panel). Anti-PAK4 blotting was used to control IP efficiency in the lower panel. (G) N-WASP was immunoprecipitated with an anti-N-WASP antibody from lysates of H1299 cells, with rabbit IgG as a control, samples were analyzed by immunoblot using an anti-PAK4 antibody with the lysate input to the left (upper panel). Anti-N-WASP blotting was used to control IP efficiency in the lower panel. (H) PAK4, N-WASP and F-actin co-localized in the cell periphery after re-plating. FLAG-PAK4 was labeled with an anti-FLAG mab (Green), N-WASP with an anti-N-WASP antibody (Red), F-actin with SiR-actin (Purple) and Nuclei with Hoechst (Blue), Scale bar: 10 μm.
    Figure Legend Snippet: PAK4 interacts with and phosphorylates N-WASP (A) PAK4 mediated phosphorylation was analyzed by an in vitro kinase assay using recombinant HIS-PAK4 together with the Arp2/3 complex (left panel) or GST-VCA (right panel) as substrates, with GST as a negative control and GST-RAF1 (332–344) as a positive control (upper panels). The lower panels display the protein loading in the assays by Coomassie Brilliant Blue staining. (B) HIS-PAK4 phosphorylation of the WASP VCA domain was analyzed using an anti-N-WASP pSer484/Ser485 antibody after a kinase assay using recombinant HIS-PAK4 with GST-VCA as a substrate. GST serves as a negative control, while the anti-RAF1 pSer338 antibody was used as a positive control to detect GST-RAF1 phosphorylated by PAK4 (upper panel). The lower panel shows the loading of HIS-PAK4 protein and GST-fusion proteins used in the assay by silver staining. (C) HIS-PAK4 was pulled-down in the presence of GST-VCA or the Arp2/3 complex with Ni-NTA agarose and input (I), supernatant (S) and pellet (P) analyzed by silver staining. (D) IP of EGFP control or EGFP-PAK4 transiently expressed in H1299 cells analyzed by immunoblotting using an anti-N-WASP antibody (upper panel right two lanes). The left two lanes show immunoblotting of the input lysates. Anti-GFP was used to control the expression and IP efficiency in the lower panel. (E) N-WASP was immunoprecipitated with an anti-N-WASP antibody from lysates of H1299 cells transiently expressing EGFP-PAK4 and samples were analyzed by immunoblot using an anti-GFP antibody with the lysate input to the left (upper panel). Anti-N-WASP was used to control the expression and IP efficiency in the lower panel. (F) PAK4 was immunoprecipitated with an anti-PAK4 antibody from lysates of MCF7 cells, with rabbit IgG as a control, samples were analyzed by immunoblot using an anti-N-WASP antibody with the lysate input to the left (upper panel). Anti-PAK4 blotting was used to control IP efficiency in the lower panel. (G) N-WASP was immunoprecipitated with an anti-N-WASP antibody from lysates of H1299 cells, with rabbit IgG as a control, samples were analyzed by immunoblot using an anti-PAK4 antibody with the lysate input to the left (upper panel). Anti-N-WASP blotting was used to control IP efficiency in the lower panel. (H) PAK4, N-WASP and F-actin co-localized in the cell periphery after re-plating. FLAG-PAK4 was labeled with an anti-FLAG mab (Green), N-WASP with an anti-N-WASP antibody (Red), F-actin with SiR-actin (Purple) and Nuclei with Hoechst (Blue), Scale bar: 10 μm.

    Techniques Used: In Vitro, Kinase Assay, Recombinant, Negative Control, Positive Control, Staining, Silver Staining, Expressing, Immunoprecipitation, Labeling

    2) Product Images from "RUNX3 Regulates Intercellular Adhesion Molecule 3 (ICAM-3) Expression during Macrophage Differentiation and Monocyte Extravasation"

    Article Title: RUNX3 Regulates Intercellular Adhesion Molecule 3 (ICAM-3) Expression during Macrophage Differentiation and Monocyte Extravasation

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0033313

    Identification and characterization of RUNX and C/EBP-binding elements within the ICAM-3 gene proximal regulatory region. A. EMSA was performed on the indicated oligonucleotides spanning the −157/−14 region of the ICAM-3 promoter using nuclear extracts from THP-1, K-562 and Jurkat cells. The position of the major retarded species is indicated. B. EMSA was performed on the ICAM3.3 and ICAM3.5 oligonucleotides using nuclear extracts from the indicated COS-7 cells transfected with an empty expression vector (pCDNA3) or with either RUNX1 or RUNX3 together with CBF-β expression vector. The position of the RUNX1- and RUNX3-containing complex is shown. C. EMSA was performed on the ICAM3.5 and ICAM3.3 oligonucleotides using nuclear extracts from Jurkat cells in the absence (−) or presence of unlabeled competitor oligonucleotides (ICAM3.5, ICAM3.5mutRUNX, ICAM3.3, ICAM3.3mutRUNX, AMLcons) or polyclonal antisera against CD209 (Control antibody, Cnt Ab) or RUNX1 proteins (R-3034). The position of RUNX1-containing complexes are shown. Unlabeled competitor oligonucleotides were added at a 100-fold molar excess. D. EMSA was performed on the ICAM3.4 oligonucleotide using nuclear extracts from THP-1 cells in the absence (−) or presence of unlabeled competitor oligonucleotides (ICAM3.4, ICAM3.4mutCEBP, C/EBPcons) or polyclonal antibody against CD209 (Control antibody, Cnt Ab) or C/EBPα proteins (α-C/EBPα). The position of C/EBPα-containing complexes are shown. Unlabeled competitor oligonucleotides were added at a 100-fold molar excess. In A–D, EMSA's were performed twice with similar result and a representative experiment is shown. E. ICAM-3 promoter-based oligonucleotides with mutated nucleotides in lowercase and their relative positions. F. In vivo occupancy of the ICAM-3 promoter by RUNX1. Chromatin immunoprecipitation on Jurkat cells was performed with an affinity-purified polyclonal antisera specific for RUNX1 or purified rabbit IgG. Immunoprecipitated chromatin was analyzed by PCR using a pair of ICAM-3 promoter-specific primers that amplify a 234-bp fragment flanking the RUNX-binding sites at −80 and −29. ChIP experiment was performed twice with similar results, and a representative experiment is shown.
    Figure Legend Snippet: Identification and characterization of RUNX and C/EBP-binding elements within the ICAM-3 gene proximal regulatory region. A. EMSA was performed on the indicated oligonucleotides spanning the −157/−14 region of the ICAM-3 promoter using nuclear extracts from THP-1, K-562 and Jurkat cells. The position of the major retarded species is indicated. B. EMSA was performed on the ICAM3.3 and ICAM3.5 oligonucleotides using nuclear extracts from the indicated COS-7 cells transfected with an empty expression vector (pCDNA3) or with either RUNX1 or RUNX3 together with CBF-β expression vector. The position of the RUNX1- and RUNX3-containing complex is shown. C. EMSA was performed on the ICAM3.5 and ICAM3.3 oligonucleotides using nuclear extracts from Jurkat cells in the absence (−) or presence of unlabeled competitor oligonucleotides (ICAM3.5, ICAM3.5mutRUNX, ICAM3.3, ICAM3.3mutRUNX, AMLcons) or polyclonal antisera against CD209 (Control antibody, Cnt Ab) or RUNX1 proteins (R-3034). The position of RUNX1-containing complexes are shown. Unlabeled competitor oligonucleotides were added at a 100-fold molar excess. D. EMSA was performed on the ICAM3.4 oligonucleotide using nuclear extracts from THP-1 cells in the absence (−) or presence of unlabeled competitor oligonucleotides (ICAM3.4, ICAM3.4mutCEBP, C/EBPcons) or polyclonal antibody against CD209 (Control antibody, Cnt Ab) or C/EBPα proteins (α-C/EBPα). The position of C/EBPα-containing complexes are shown. Unlabeled competitor oligonucleotides were added at a 100-fold molar excess. In A–D, EMSA's were performed twice with similar result and a representative experiment is shown. E. ICAM-3 promoter-based oligonucleotides with mutated nucleotides in lowercase and their relative positions. F. In vivo occupancy of the ICAM-3 promoter by RUNX1. Chromatin immunoprecipitation on Jurkat cells was performed with an affinity-purified polyclonal antisera specific for RUNX1 or purified rabbit IgG. Immunoprecipitated chromatin was analyzed by PCR using a pair of ICAM-3 promoter-specific primers that amplify a 234-bp fragment flanking the RUNX-binding sites at −80 and −29. ChIP experiment was performed twice with similar results, and a representative experiment is shown.

    Techniques Used: Binding Assay, Transfection, Expressing, Plasmid Preparation, In Vivo, Chromatin Immunoprecipitation, Affinity Purification, Purification, Immunoprecipitation, Polymerase Chain Reaction

    3) Product Images from "mBet3p is required for homotypic COPII vesicle tethering in mammalian cells"

    Article Title: mBet3p is required for homotypic COPII vesicle tethering in mammalian cells

    Journal: The Journal of Cell Biology

    doi: 10.1083/jcb.200603044

    mBet3p links COPII vesicles to each other. (A) COPII vesicle coisolation in vitro. Vesicles marked in two different ways were released from permeabilized NRK cells during the stage I incubation. During the stage II incubation, vesicles tethered to each other and subsequently fused. (B) Anti-Bet3p antibody blocks the coisolation of COPII vesicles. Two COPII vesicle populations were formed in vitro in a first-stage incubation, as previously described ( Xu and Hay, 2004 ). The two vesicle populations were then combined and preincubated together for 20 min on ice in the absence or presence of antibody. After the incubation, one sample was kept on ice, while the other samples were incubated at 32°C for 60 min in a second-stage incubation. 1, one population of vesicles was untagged instead of Myc-tagged; 2, incubated on ice for 60 min; 3, complete reaction incubated without antibody; 4, contained α-mBet3p (168 nM; ∼5μg per reaction); 5, contained α-syntaxin-5 (168 nM); 6, contained rabbit IgG (168 nM). (C) Bet3p is present on nascent VTCs formed in vitro. Stage I reactions were performed in the presence or absence of GDP-locked Sar1 T39N. Lane 1, complete reaction; lane 2, complete reaction plus GDP-locked Sar1 T39N (800 nM); lane 3, vesicles were formed from NRK cells expressing untagged VSV-G. Vesicles released during stage I were then incubated in stage II (60 min at 32°C) and immunoisolated with anti-Myc antibody. The final immunoisolates were subjected to Western blot analysis to detect mBet3p (bottom) and VSV-Myc (top). (D) Anti-Bet3p antibody stimulates the release of COPII vesicles from permeabilized cells when added during the stage I incubation. COPII vesicle populations were formed in vitro using permeabilized NRK cells as in B, only the incubation was performed for 90 min (as described in Fig. 1 A of Xu and Hay, 2004 ). The permeabilized cells were removed by centrifugation, and the released vesicles were immunoisolated with an antibody to the integral membrane protein p24. The VSV-G* in the precipitate was quantified by autoradiography and reported as the percentage of the total VSV-G* in the starting cells. 1, complete reaction without antibody; 2, Sar1 T39N was included in the reaction at a concentration of 1 μM; 3, complete reaction plus 110 nM anti-mBet3 antibody. Error bars are the SEM.
    Figure Legend Snippet: mBet3p links COPII vesicles to each other. (A) COPII vesicle coisolation in vitro. Vesicles marked in two different ways were released from permeabilized NRK cells during the stage I incubation. During the stage II incubation, vesicles tethered to each other and subsequently fused. (B) Anti-Bet3p antibody blocks the coisolation of COPII vesicles. Two COPII vesicle populations were formed in vitro in a first-stage incubation, as previously described ( Xu and Hay, 2004 ). The two vesicle populations were then combined and preincubated together for 20 min on ice in the absence or presence of antibody. After the incubation, one sample was kept on ice, while the other samples were incubated at 32°C for 60 min in a second-stage incubation. 1, one population of vesicles was untagged instead of Myc-tagged; 2, incubated on ice for 60 min; 3, complete reaction incubated without antibody; 4, contained α-mBet3p (168 nM; ∼5μg per reaction); 5, contained α-syntaxin-5 (168 nM); 6, contained rabbit IgG (168 nM). (C) Bet3p is present on nascent VTCs formed in vitro. Stage I reactions were performed in the presence or absence of GDP-locked Sar1 T39N. Lane 1, complete reaction; lane 2, complete reaction plus GDP-locked Sar1 T39N (800 nM); lane 3, vesicles were formed from NRK cells expressing untagged VSV-G. Vesicles released during stage I were then incubated in stage II (60 min at 32°C) and immunoisolated with anti-Myc antibody. The final immunoisolates were subjected to Western blot analysis to detect mBet3p (bottom) and VSV-Myc (top). (D) Anti-Bet3p antibody stimulates the release of COPII vesicles from permeabilized cells when added during the stage I incubation. COPII vesicle populations were formed in vitro using permeabilized NRK cells as in B, only the incubation was performed for 90 min (as described in Fig. 1 A of Xu and Hay, 2004 ). The permeabilized cells were removed by centrifugation, and the released vesicles were immunoisolated with an antibody to the integral membrane protein p24. The VSV-G* in the precipitate was quantified by autoradiography and reported as the percentage of the total VSV-G* in the starting cells. 1, complete reaction without antibody; 2, Sar1 T39N was included in the reaction at a concentration of 1 μM; 3, complete reaction plus 110 nM anti-mBet3 antibody. Error bars are the SEM.

    Techniques Used: In Vitro, Incubation, Expressing, Western Blot, Centrifugation, Autoradiography, Concentration Assay

    Cargo accumulates in structures that colocalize with COPII when mBet3p is inactivated in vivo. (A) The trafficking of YFP-tagged tsO45 VSV-G to the cell surface was quantitated in HeLa cells that were microinjected with α-mBet3p or control IgG, as described in the Materials and methods. Error bars are the SD. (B) Intracellular trafficking was monitored in BSC-1 cells that were injected with cDNA encoding CD8. After CD8 mRNA accumulated, the cells were injected with α-mBet3p or IgG. Subsequent to a 1-h incubation at 37°C, the cells were washed and the synthesis and transport of CD8 was continued for 3 h. Finally, CD8 was chased for 45 min in the presence of cycloheximide. The cells were stained for CD8, Sec31p, or Golgin-84. To visualize Sec31p and Golgin-84, antibodies were directly conjugated to Alexa Fluor 594 and viewed in the red channel. To visualize CD8, the secondary antibody was conjugated to Alexa Fluor 488 and viewed in the green channel. The inset shows the merge of CD8, Sec31p, and Golgin-84 in the α-mBet3p–injected cell. The merged image is on the right. Bar, 20 μm.
    Figure Legend Snippet: Cargo accumulates in structures that colocalize with COPII when mBet3p is inactivated in vivo. (A) The trafficking of YFP-tagged tsO45 VSV-G to the cell surface was quantitated in HeLa cells that were microinjected with α-mBet3p or control IgG, as described in the Materials and methods. Error bars are the SD. (B) Intracellular trafficking was monitored in BSC-1 cells that were injected with cDNA encoding CD8. After CD8 mRNA accumulated, the cells were injected with α-mBet3p or IgG. Subsequent to a 1-h incubation at 37°C, the cells were washed and the synthesis and transport of CD8 was continued for 3 h. Finally, CD8 was chased for 45 min in the presence of cycloheximide. The cells were stained for CD8, Sec31p, or Golgin-84. To visualize Sec31p and Golgin-84, antibodies were directly conjugated to Alexa Fluor 594 and viewed in the red channel. To visualize CD8, the secondary antibody was conjugated to Alexa Fluor 488 and viewed in the green channel. The inset shows the merge of CD8, Sec31p, and Golgin-84 in the α-mBet3p–injected cell. The merged image is on the right. Bar, 20 μm.

    Techniques Used: In Vivo, Injection, Incubation, Staining

    Related Articles

    Chromatography:

    Article Title: Evaluation of the Potency of the Anti-Idiotypic Antibody Ab2/3H6 Mimicking gp41 as an HIV-1 Vaccine in a Rabbit Prime/Boost Study
    Article Snippet: .. Purification of rabbit IgG Purification of rabbit IgG from crude sera was performed on an Äkta Purifier chromatography system (GE) with the UNOsphere SUPrA Mini cartridge column (Biorad). ..

    Purification:

    Article Title: mBet3p is required for homotypic COPII vesicle tethering in mammalian cells
    Article Snippet: .. Rabbit IgG specific to mBet3p was purified on an Affigel column (Bio-Rad Laboratories) preloaded with His6 -tagged Bet3p. ..

    Article Title: Evaluation of the Potency of the Anti-Idiotypic Antibody Ab2/3H6 Mimicking gp41 as an HIV-1 Vaccine in a Rabbit Prime/Boost Study
    Article Snippet: .. Purification of rabbit IgG Purification of rabbit IgG from crude sera was performed on an Äkta Purifier chromatography system (GE) with the UNOsphere SUPrA Mini cartridge column (Biorad). ..

    Immunoprecipitation:

    Article Title: Regulation and Localization of the Bloom Syndrome Protein in Response to DNA Damage
    Article Snippet: .. For immunoprecipitation, SAOS-2 nuclear lysates were precleared by incubating with 5 μg rabbit IgG and Dynabeads-protein G (Bio-Rad Laboratories) for 1 h at 4°C with gentle agitation. .. The beads were collected and the supernatant was incubated with 5 μg rabbit anti-RAD51 (Oncogene Research Products) for 16 h at 4°C, followed by addition of Dynabeads for 1 h at 4°C.

    Incubation:

    Article Title: MiR-199a inhibits the ability of proliferation and migration by regulating CD44-Ezrin signaling in cutaneous squamous cell carcinoma cells
    Article Snippet: .. Protein extracts were incubated with 50 μl of normal rabbit IgG for 1 h, and precleared with proteinA-agarose beads (Bio-Rad, Germany) at 4°C for 30 min, then centrifuged at 12000 g for 10 min at 4°C. .. The total 60 μl of the supernatant were incubated with 2 μg of CD44 antibody at 4°C overnight, washed in lysis buffer and centrifugated at 2500 g for 5 min at 4°C.

    Fractionation:

    Article Title: Functional diversification of a basic helix-loop-helix protein due to alternative transcription during generation of amphidiploidy in tobacco plants
    Article Snippet: .. After fractionation by SDS/PAGE, proteins were electronically transferred on to cellulose membranes (Immobilon-N, Millipore), and NtWIN4/NsWIN4 was detected using rabbit antibodies raised against a synthetic peptide (MIKERIRREKQKQSY) or a His-tagged recombinant protein (amino acid positions 27–247) and horseradish peroxidase conjugated anti-rabbit antibodies (Bio-Rad Laboratories). ..

    Recombinant:

    Article Title: Functional diversification of a basic helix-loop-helix protein due to alternative transcription during generation of amphidiploidy in tobacco plants
    Article Snippet: .. After fractionation by SDS/PAGE, proteins were electronically transferred on to cellulose membranes (Immobilon-N, Millipore), and NtWIN4/NsWIN4 was detected using rabbit antibodies raised against a synthetic peptide (MIKERIRREKQKQSY) or a His-tagged recombinant protein (amino acid positions 27–247) and horseradish peroxidase conjugated anti-rabbit antibodies (Bio-Rad Laboratories). ..

    SDS Page:

    Article Title: Functional diversification of a basic helix-loop-helix protein due to alternative transcription during generation of amphidiploidy in tobacco plants
    Article Snippet: .. After fractionation by SDS/PAGE, proteins were electronically transferred on to cellulose membranes (Immobilon-N, Millipore), and NtWIN4/NsWIN4 was detected using rabbit antibodies raised against a synthetic peptide (MIKERIRREKQKQSY) or a His-tagged recombinant protein (amino acid positions 27–247) and horseradish peroxidase conjugated anti-rabbit antibodies (Bio-Rad Laboratories). ..

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 90
    Bio-Rad peroxidase conjugated goat anti rabbit igg
    Localization of <t>ΔCT–P-selectin</t> in platelets by electron microscopy. Indirect immunogold labeling of P-selectin was performed in resting platelets from wild-type ( WT ) and ΔCT mice. Ultrathin frozen sections were stained with a rabbit antibody against P-selectin and visualized with a goat anti–rabbit <t>IgG</t> conjugated to 10-nm colloidal gold particles. The majority of the gold particles are associated with α-granules ( arrowheads ) in both wild-type and ΔCT platelets. A small amount of labeling was seen on the plasma membrane in both genotypes. Bars, 200 nm.
    Peroxidase Conjugated Goat Anti Rabbit Igg, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 90/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/peroxidase conjugated goat anti rabbit igg/product/Bio-Rad
    Average 90 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    peroxidase conjugated goat anti rabbit igg - by Bioz Stars, 2020-09
    90/100 stars
      Buy from Supplier

    90
    Bio-Rad horseradish peroxidase conjugated goat anti rabbit immunoglobulin g
    Antibody response induced by intradermal immunization with recombinant L. monocytogenes. Groups of 5 mice were sham-immunized or immunized i.d. twice at weeks 0 and 4 with LVS, vector control (rLmΔactA), or recombinant L. monocytog enes vaccines expressing KatG (rLm/katG), IglC (rLm/iglC), or the combination of both vaccines. At week 8, mice were euthanized and sera were collected to measure the antibody <t>(IgG)</t> response by ELISA. For measuring antibody response to KatG (A), sera were diluted 1:50. For measuring antibody response to IglC (B), sera were diluted 1:25. The antibody responses are presented as the Absorbance at 414 nm (A 414nm ) in the presence of antigen divided by the A 414nm in the absence of antigen for each individual mouse. Bars represent the mean of the antibody titer from the 5 mice per group. Asterisks indicate that the difference between the antibody response of mice in the indicated vaccinated group and mice in the sham-vaccinated group was significant. *, P
    Horseradish Peroxidase Conjugated Goat Anti Rabbit Immunoglobulin G, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 90/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/horseradish peroxidase conjugated goat anti rabbit immunoglobulin g/product/Bio-Rad
    Average 90 stars, based on 12 article reviews
    Price from $9.99 to $1999.99
    horseradish peroxidase conjugated goat anti rabbit immunoglobulin g - by Bioz Stars, 2020-09
    90/100 stars
      Buy from Supplier

    88
    Bio-Rad goat anti rabbit igg conjugated to horse radish peroxidase
    ProMMP-8 and proMMP-9 share binding sites on the surface of PMNs: In A and B , PMNs from <t>Mmp-8</t> −/− x Mmp-9 −/− mice were activated for 15 min at 37°C with 10 −6 M PAF followed by 10 −6 M fMLP to induce surface expression of Timp-1. In A , the activated PMNs were then pre-incubated for 45 min at 4°C with or without exogenous full length murine proMmp-8 (50–400 nM). Cells were then incubated for an additional 60 min at 4°C with 100 nM exogenous murine proMMP-9. Cells were then washed and immunostained with rabbit anti-murine Mmp-9 <t>IgG,</t> or non-immune rabbit IgG followed by goat anti-rabbit F(ab) 2 -conjugated to Alexa 488 to detect bound pro and active Mmp-9. In B , the PAF- and fMLP- activated and PMNs were pre-incubated for 45 min at 4°C with or without exogenous full length murine proMmp-9 (50–400 nM). Cells were then incubated for an additional 60 min at 4°C with 100 nM exogenous full length murine proMMP-8. Cells were then immunostained with rabbit anti-murine Mmp-8 IgG, or non-immune rabbit IgG followed by goat anti-rabbit F(ab) 2 -conjugated to Alexa 488 to detect bound pro and active Mmp-8. In A and B , images of immunostained cells were captured and surface-bound pro and active Mmp-9 (in A ) or pro and active Mmp-8 (in B ) were quantified using MetaMorph software. Data are mean + SEM (n = 150–200 cells/group). Data were analyzed using a One-Way ANOVA followed by pair-wise testing with two-tailed Student’s t-tests. Asterisk indicates P
    Goat Anti Rabbit Igg Conjugated To Horse Radish Peroxidase, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/goat anti rabbit igg conjugated to horse radish peroxidase/product/Bio-Rad
    Average 88 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    goat anti rabbit igg conjugated to horse radish peroxidase - by Bioz Stars, 2020-09
    88/100 stars
      Buy from Supplier

    96
    Bio-Rad rabbit anti immunoglobulin g igg
    Immunohistochemical evaluation of blood-brain barrier permeability. Blood–brain barrier permeability evaluated as <t>IgG</t> expression with respect to distance from the explanted microelectrode hole (μm). (A) 2 weeks. (B) 16 weeks. (C) Representative images of 2 weeks BBB permeability. (D) Representative images of 16 weeks BBB permeability. Scale bar: 100 μm. ∗ Denotes significance between silicon and thiol-ene probes.
    Rabbit Anti Immunoglobulin G Igg, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti immunoglobulin g igg/product/Bio-Rad
    Average 96 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    rabbit anti immunoglobulin g igg - by Bioz Stars, 2020-09
    96/100 stars
      Buy from Supplier

    Image Search Results


    Localization of ΔCT–P-selectin in platelets by electron microscopy. Indirect immunogold labeling of P-selectin was performed in resting platelets from wild-type ( WT ) and ΔCT mice. Ultrathin frozen sections were stained with a rabbit antibody against P-selectin and visualized with a goat anti–rabbit IgG conjugated to 10-nm colloidal gold particles. The majority of the gold particles are associated with α-granules ( arrowheads ) in both wild-type and ΔCT platelets. A small amount of labeling was seen on the plasma membrane in both genotypes. Bars, 200 nm.

    Journal: The Journal of Cell Biology

    Article Title: Role of P-Selectin Cytoplasmic Domain in Granular Targeting In Vivo and in Early Inflammatory Responses

    doi:

    Figure Lengend Snippet: Localization of ΔCT–P-selectin in platelets by electron microscopy. Indirect immunogold labeling of P-selectin was performed in resting platelets from wild-type ( WT ) and ΔCT mice. Ultrathin frozen sections were stained with a rabbit antibody against P-selectin and visualized with a goat anti–rabbit IgG conjugated to 10-nm colloidal gold particles. The majority of the gold particles are associated with α-granules ( arrowheads ) in both wild-type and ΔCT platelets. A small amount of labeling was seen on the plasma membrane in both genotypes. Bars, 200 nm.

    Article Snippet: The antibody bound to P-selectin was detected with a horseradish peroxidase-conjugated goat anti–rabbit IgG (Bio-Rad, Hercules, CA) and an enhanced chemiluminescence kit ( Sigma Chemical Co. , St. Louis, MO).

    Techniques: Electron Microscopy, Labeling, Mouse Assay, Staining

    Flow cytometry analysis of P-selectin expression on platelets. Wild-type and ΔCT platelets were stained for membrane P-selectin and analyzed by flow cytometry. In the resting state, platelets of both genotypes displayed virtually no P-selectin on their plasma membranes. Thrombin activation induced in wild-type as well as in mutant platelets a similar increase in mean fluorescence with ∼90% of P-selectin–positive platelets. Representative histograms are shown. Shaded area , negative control staining with only the FITC-conjugated goat anti–rabbit IgG.

    Journal: The Journal of Cell Biology

    Article Title: Role of P-Selectin Cytoplasmic Domain in Granular Targeting In Vivo and in Early Inflammatory Responses

    doi:

    Figure Lengend Snippet: Flow cytometry analysis of P-selectin expression on platelets. Wild-type and ΔCT platelets were stained for membrane P-selectin and analyzed by flow cytometry. In the resting state, platelets of both genotypes displayed virtually no P-selectin on their plasma membranes. Thrombin activation induced in wild-type as well as in mutant platelets a similar increase in mean fluorescence with ∼90% of P-selectin–positive platelets. Representative histograms are shown. Shaded area , negative control staining with only the FITC-conjugated goat anti–rabbit IgG.

    Article Snippet: The antibody bound to P-selectin was detected with a horseradish peroxidase-conjugated goat anti–rabbit IgG (Bio-Rad, Hercules, CA) and an enhanced chemiluminescence kit ( Sigma Chemical Co. , St. Louis, MO).

    Techniques: Flow Cytometry, Cytometry, Expressing, Staining, Activation Assay, Mutagenesis, Fluorescence, Negative Control

    Antibody response induced by intradermal immunization with recombinant L. monocytogenes. Groups of 5 mice were sham-immunized or immunized i.d. twice at weeks 0 and 4 with LVS, vector control (rLmΔactA), or recombinant L. monocytog enes vaccines expressing KatG (rLm/katG), IglC (rLm/iglC), or the combination of both vaccines. At week 8, mice were euthanized and sera were collected to measure the antibody (IgG) response by ELISA. For measuring antibody response to KatG (A), sera were diluted 1:50. For measuring antibody response to IglC (B), sera were diluted 1:25. The antibody responses are presented as the Absorbance at 414 nm (A 414nm ) in the presence of antigen divided by the A 414nm in the absence of antigen for each individual mouse. Bars represent the mean of the antibody titer from the 5 mice per group. Asterisks indicate that the difference between the antibody response of mice in the indicated vaccinated group and mice in the sham-vaccinated group was significant. *, P

    Journal: Vaccine

    Article Title: Recombinant Attenuated Listeria monocytogenes Vaccine Expressing Francisella tularensis IglC Induces Protection in Mice Against Aerosolized Type A F. tularensis

    doi: 10.1016/j.vaccine.2008.12.014

    Figure Lengend Snippet: Antibody response induced by intradermal immunization with recombinant L. monocytogenes. Groups of 5 mice were sham-immunized or immunized i.d. twice at weeks 0 and 4 with LVS, vector control (rLmΔactA), or recombinant L. monocytog enes vaccines expressing KatG (rLm/katG), IglC (rLm/iglC), or the combination of both vaccines. At week 8, mice were euthanized and sera were collected to measure the antibody (IgG) response by ELISA. For measuring antibody response to KatG (A), sera were diluted 1:50. For measuring antibody response to IglC (B), sera were diluted 1:25. The antibody responses are presented as the Absorbance at 414 nm (A 414nm ) in the presence of antigen divided by the A 414nm in the absence of antigen for each individual mouse. Bars represent the mean of the antibody titer from the 5 mice per group. Asterisks indicate that the difference between the antibody response of mice in the indicated vaccinated group and mice in the sham-vaccinated group was significant. *, P

    Article Snippet: Protein expression by recombinant L. monocytogenes was analyzed by Western blotting using rabbit polyclonal antibodies specific to AcpA, Bfr, DnaK, GroEL, IglC, KatG, or Pld at a dilution of 1:5,000 and subsequently horseradish peroxidase-conjugated goat anti-rabbit immunoglobulin G (Bio-Rad) at a dilution of 1:25,000.

    Techniques: Recombinant, Mouse Assay, Plasmid Preparation, Expressing, Enzyme-linked Immunosorbent Assay

    ProMMP-8 and proMMP-9 share binding sites on the surface of PMNs: In A and B , PMNs from Mmp-8 −/− x Mmp-9 −/− mice were activated for 15 min at 37°C with 10 −6 M PAF followed by 10 −6 M fMLP to induce surface expression of Timp-1. In A , the activated PMNs were then pre-incubated for 45 min at 4°C with or without exogenous full length murine proMmp-8 (50–400 nM). Cells were then incubated for an additional 60 min at 4°C with 100 nM exogenous murine proMMP-9. Cells were then washed and immunostained with rabbit anti-murine Mmp-9 IgG, or non-immune rabbit IgG followed by goat anti-rabbit F(ab) 2 -conjugated to Alexa 488 to detect bound pro and active Mmp-9. In B , the PAF- and fMLP- activated and PMNs were pre-incubated for 45 min at 4°C with or without exogenous full length murine proMmp-9 (50–400 nM). Cells were then incubated for an additional 60 min at 4°C with 100 nM exogenous full length murine proMMP-8. Cells were then immunostained with rabbit anti-murine Mmp-8 IgG, or non-immune rabbit IgG followed by goat anti-rabbit F(ab) 2 -conjugated to Alexa 488 to detect bound pro and active Mmp-8. In A and B , images of immunostained cells were captured and surface-bound pro and active Mmp-9 (in A ) or pro and active Mmp-8 (in B ) were quantified using MetaMorph software. Data are mean + SEM (n = 150–200 cells/group). Data were analyzed using a One-Way ANOVA followed by pair-wise testing with two-tailed Student’s t-tests. Asterisk indicates P

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    Article Title: Tissue Inhibitor of Metalloproteinase-1 (TIMP-1) Promotes PMN Pericellular Proteolysis by Anchoring Matrix Metalloproteinase-8 and -9 to PMN Surfaces

    doi: 10.4049/jimmunol.1801466

    Figure Lengend Snippet: ProMMP-8 and proMMP-9 share binding sites on the surface of PMNs: In A and B , PMNs from Mmp-8 −/− x Mmp-9 −/− mice were activated for 15 min at 37°C with 10 −6 M PAF followed by 10 −6 M fMLP to induce surface expression of Timp-1. In A , the activated PMNs were then pre-incubated for 45 min at 4°C with or without exogenous full length murine proMmp-8 (50–400 nM). Cells were then incubated for an additional 60 min at 4°C with 100 nM exogenous murine proMMP-9. Cells were then washed and immunostained with rabbit anti-murine Mmp-9 IgG, or non-immune rabbit IgG followed by goat anti-rabbit F(ab) 2 -conjugated to Alexa 488 to detect bound pro and active Mmp-9. In B , the PAF- and fMLP- activated and PMNs were pre-incubated for 45 min at 4°C with or without exogenous full length murine proMmp-9 (50–400 nM). Cells were then incubated for an additional 60 min at 4°C with 100 nM exogenous full length murine proMMP-8. Cells were then immunostained with rabbit anti-murine Mmp-8 IgG, or non-immune rabbit IgG followed by goat anti-rabbit F(ab) 2 -conjugated to Alexa 488 to detect bound pro and active Mmp-8. In A and B , images of immunostained cells were captured and surface-bound pro and active Mmp-9 (in A ) or pro and active Mmp-8 (in B ) were quantified using MetaMorph software. Data are mean + SEM (n = 150–200 cells/group). Data were analyzed using a One-Way ANOVA followed by pair-wise testing with two-tailed Student’s t-tests. Asterisk indicates P

    Article Snippet: Briefly, samples were subjected to electrophoresis on 8% SDS-PAGE under reducing conditions, proteins transferred to PVDF membranes, and probed with polyclonal rabbit anti-murine Mmp-9 IgG (AB19047) or rabbit anti-murine Mmp-8 IgG (Ab19045), followed by goat anti-rabbit IgG conjugated to horse radish peroxidase (Biorad, Hercules, CA), and a chemiluminescence detection system following the manufacturer’s instructions.

    Techniques: Binding Assay, Mouse Assay, Expressing, Incubation, Software, Two Tailed Test

    TIMP-1 is co-localized with MMP-8 and MMP-9 on the surface of activated human PMNs: Human PMNs were activated at 37°C with PAF at 10 −7 M for 15 min followed by fMLP at 10 −7 M for 30 min. Cells were double immunostained with Alexa 546 and murine anti-MMP-9 IgG ( A , second panel), or murine anti-human MMP-8 IgG ( B , second panel) or non-immune murine (Ms) IgG ( C , second panel) and with Alexa 488 and rabbit anti-TIMP-1 IgG ( A and B third panels) or non-immune rabbit (Rb) IgG ( C , third panel). The anti-MMP-8 and anti-MMP-9 IgGs used recognize both pro and active forms of these MMPs. Cells were examined using a Normarski objective ( A-C , left panels) and co-localization of MMPs and TIMP-1 on the surface of the activated PMNs was assessed by confocal microscopy (see merged images in the right panels for A-C ). The white bars are 5 microns in length. Note the strong co-localization of TIMP-1 with both MMP-8 and MMP-9 on the surface of activated PMNs. The results shown are representative of at least 3 different PMN preparations.

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    Article Title: Tissue Inhibitor of Metalloproteinase-1 (TIMP-1) Promotes PMN Pericellular Proteolysis by Anchoring Matrix Metalloproteinase-8 and -9 to PMN Surfaces

    doi: 10.4049/jimmunol.1801466

    Figure Lengend Snippet: TIMP-1 is co-localized with MMP-8 and MMP-9 on the surface of activated human PMNs: Human PMNs were activated at 37°C with PAF at 10 −7 M for 15 min followed by fMLP at 10 −7 M for 30 min. Cells were double immunostained with Alexa 546 and murine anti-MMP-9 IgG ( A , second panel), or murine anti-human MMP-8 IgG ( B , second panel) or non-immune murine (Ms) IgG ( C , second panel) and with Alexa 488 and rabbit anti-TIMP-1 IgG ( A and B third panels) or non-immune rabbit (Rb) IgG ( C , third panel). The anti-MMP-8 and anti-MMP-9 IgGs used recognize both pro and active forms of these MMPs. Cells were examined using a Normarski objective ( A-C , left panels) and co-localization of MMPs and TIMP-1 on the surface of the activated PMNs was assessed by confocal microscopy (see merged images in the right panels for A-C ). The white bars are 5 microns in length. Note the strong co-localization of TIMP-1 with both MMP-8 and MMP-9 on the surface of activated PMNs. The results shown are representative of at least 3 different PMN preparations.

    Article Snippet: Briefly, samples were subjected to electrophoresis on 8% SDS-PAGE under reducing conditions, proteins transferred to PVDF membranes, and probed with polyclonal rabbit anti-murine Mmp-9 IgG (AB19047) or rabbit anti-murine Mmp-8 IgG (Ab19045), followed by goat anti-rabbit IgG conjugated to horse radish peroxidase (Biorad, Hercules, CA), and a chemiluminescence detection system following the manufacturer’s instructions.

    Techniques: Confocal Microscopy

    Exogenous Timp-1 reconstitutes the binding of exogenous proMmp-9 and proMmp-8 to Timp-1 −/− PMNs: In A , PAF- and fMLP-activated PMNs from Mmp-9 −/− and Timp-1 −/− mice were incubated with or without 50–400 nM exogenous murine proMmp-9, and then immunostained with rabbit anti-Mmp-9 IgG, or non-immune rabbit IgG followed by goat anti-rabbit F(ab) 2 -conjugated to Alexa 488. In B , PAF- and fMLP-activated PMNs from Mmp-8 −/− and Timp-1 −/− mice were incubated with or without 50–400 nM exogenous murine proMmp-8, and then immunostained with rabbit anti-Mmp-8 IgG, or non-immune rabbit IgG followed by goat- anti-rabbit F(ab) 2 -conjugated to Alexa 488. In A-B , the antibodies used detect both the pro and active forms of the Mmps. Data are mean + SEM; n = 150–200 cells per group. Data were analyzed using a One-Way ANOVA followed by pair-wise testing with two-tailed Student’s t-tests. Asterisk indicates P

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    Article Title: Tissue Inhibitor of Metalloproteinase-1 (TIMP-1) Promotes PMN Pericellular Proteolysis by Anchoring Matrix Metalloproteinase-8 and -9 to PMN Surfaces

    doi: 10.4049/jimmunol.1801466

    Figure Lengend Snippet: Exogenous Timp-1 reconstitutes the binding of exogenous proMmp-9 and proMmp-8 to Timp-1 −/− PMNs: In A , PAF- and fMLP-activated PMNs from Mmp-9 −/− and Timp-1 −/− mice were incubated with or without 50–400 nM exogenous murine proMmp-9, and then immunostained with rabbit anti-Mmp-9 IgG, or non-immune rabbit IgG followed by goat anti-rabbit F(ab) 2 -conjugated to Alexa 488. In B , PAF- and fMLP-activated PMNs from Mmp-8 −/− and Timp-1 −/− mice were incubated with or without 50–400 nM exogenous murine proMmp-8, and then immunostained with rabbit anti-Mmp-8 IgG, or non-immune rabbit IgG followed by goat- anti-rabbit F(ab) 2 -conjugated to Alexa 488. In A-B , the antibodies used detect both the pro and active forms of the Mmps. Data are mean + SEM; n = 150–200 cells per group. Data were analyzed using a One-Way ANOVA followed by pair-wise testing with two-tailed Student’s t-tests. Asterisk indicates P

    Article Snippet: Briefly, samples were subjected to electrophoresis on 8% SDS-PAGE under reducing conditions, proteins transferred to PVDF membranes, and probed with polyclonal rabbit anti-murine Mmp-9 IgG (AB19047) or rabbit anti-murine Mmp-8 IgG (Ab19045), followed by goat anti-rabbit IgG conjugated to horse radish peroxidase (Biorad, Hercules, CA), and a chemiluminescence detection system following the manufacturer’s instructions.

    Techniques: Binding Assay, Mouse Assay, Incubation, Two Tailed Test

    Immunohistochemical evaluation of blood-brain barrier permeability. Blood–brain barrier permeability evaluated as IgG expression with respect to distance from the explanted microelectrode hole (μm). (A) 2 weeks. (B) 16 weeks. (C) Representative images of 2 weeks BBB permeability. (D) Representative images of 16 weeks BBB permeability. Scale bar: 100 μm. ∗ Denotes significance between silicon and thiol-ene probes.

    Journal: Frontiers in Neuroscience

    Article Title: Understanding the Effects of Both CD14-Mediated Innate Immunity and Device/Tissue Mechanical Mismatch in the Neuroinflammatory Response to Intracortical Microelectrodes

    doi: 10.3389/fnins.2018.00772

    Figure Lengend Snippet: Immunohistochemical evaluation of blood-brain barrier permeability. Blood–brain barrier permeability evaluated as IgG expression with respect to distance from the explanted microelectrode hole (μm). (A) 2 weeks. (B) 16 weeks. (C) Representative images of 2 weeks BBB permeability. (D) Representative images of 16 weeks BBB permeability. Scale bar: 100 μm. ∗ Denotes significance between silicon and thiol-ene probes.

    Article Snippet: After blocking the tissue (4% chicken serum, 0.3% Trition-X-100 in 1× PBS), the following primary antibodies (in 4% chicken serum, 0.3% Trition-X-100 in 1× PBS) were added to incubate overnight at 4 °C: Rabbit anti-GFAP (1:500, Z0334, Dako), mouse anti-neuronal nuclei (NeuN) (1:250, MAB377, Millipore), rat anti-CD68 (1:500, ab53444, Abcam), and rabbit anti-immunoglobulin G (IgG) (1:500, STAR26B, Bio-Rad).

    Techniques: Immunohistochemistry, Permeability, Expressing

    Immunohistochemical evaluation comparing the dual targeting of the innate immune response and mechanical mismatch to control at 2 weeks after implantation. All analyses were evaluated with respect to distance from the explanted microelectrode hole (μm). (A) Neuronal density evaluated as NeuN + cells. (B) Astrocyte encapsulation evaluated as GFAP expression. (C) Blood-brain barrier permeability evaluated as IgG expression. (D) Microglial and macrophage activation evaluated as CD68 expression. ∗ Denotes significance between silicon shank + WT and thiol-ene + Cd14 -/- ; # denotes significant difference from background neuronal density.

    Journal: Frontiers in Neuroscience

    Article Title: Understanding the Effects of Both CD14-Mediated Innate Immunity and Device/Tissue Mechanical Mismatch in the Neuroinflammatory Response to Intracortical Microelectrodes

    doi: 10.3389/fnins.2018.00772

    Figure Lengend Snippet: Immunohistochemical evaluation comparing the dual targeting of the innate immune response and mechanical mismatch to control at 2 weeks after implantation. All analyses were evaluated with respect to distance from the explanted microelectrode hole (μm). (A) Neuronal density evaluated as NeuN + cells. (B) Astrocyte encapsulation evaluated as GFAP expression. (C) Blood-brain barrier permeability evaluated as IgG expression. (D) Microglial and macrophage activation evaluated as CD68 expression. ∗ Denotes significance between silicon shank + WT and thiol-ene + Cd14 -/- ; # denotes significant difference from background neuronal density.

    Article Snippet: After blocking the tissue (4% chicken serum, 0.3% Trition-X-100 in 1× PBS), the following primary antibodies (in 4% chicken serum, 0.3% Trition-X-100 in 1× PBS) were added to incubate overnight at 4 °C: Rabbit anti-GFAP (1:500, Z0334, Dako), mouse anti-neuronal nuclei (NeuN) (1:250, MAB377, Millipore), rat anti-CD68 (1:500, ab53444, Abcam), and rabbit anti-immunoglobulin G (IgG) (1:500, STAR26B, Bio-Rad).

    Techniques: Immunohistochemistry, Expressing, Permeability, Activation Assay