goat anti mouse hrp secondary antibody  (Abcam)

 
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 99
    Name:
    Goat Anti Mouse IgG H L HRP
    Description:

    Catalog Number:
    AB205719
    Price:
    None
    Buy from Supplier


    Structured Review

    Abcam goat anti mouse hrp secondary antibody
    Conjugation efficiency and biodistribution analysis of CRISPR-modified antibody. ( a ) Coomassie blue stained gel of sortase-mediated conjugation of modified antibody to GGG-fluorophore. ( b ) Fluorescence scan of the antibody-fluorophore, stained with <t>anti-Flag-HRP,</t> showing the antibody conjugated fluorophore (red tab) compared to free fluorophore (black tab). ( c ) HPLC fluorescence trace antibody-fluorophore conjugates at different molar ratios. ( d ) Quantitative analysis of the percent of antibody modification. ( e ) Binding of 125 I-labeled CRISPR-modified antibody to REN-ICAM and REN-WT cells. ( f ) Biodistribution of 125 I-labeled CRISPR-modified anti-ICAM mAb in mice at 30 min. Tissue uptake is indicated as mean ± SEM (n = 3). Biodistribution analysis was performed comparing 111 In-labeled site-specific CRISPR/Cas9- to chemically-modified mAb. ( g ) Biodistribution of 111 In-labeled anti-ICAM mAb modified in mice at 30 min. Tissue uptake is indicated as mean ± SEM. ( h ) Localization ratio of selected organs. Significant differences were determined by t-test with Bonferroni correction to account for multiple comparisons.

    https://www.bioz.com/result/goat anti mouse hrp secondary antibody/product/Abcam
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    goat anti mouse hrp secondary antibody - by Bioz Stars, 2021-06
    99/100 stars

    Images

    1) Product Images from "Molecular engineering of antibodies for site-specific covalent conjugation using CRISPR/Cas9"

    Article Title: Molecular engineering of antibodies for site-specific covalent conjugation using CRISPR/Cas9

    Journal: Scientific Reports

    doi: 10.1038/s41598-018-19784-2

    Conjugation efficiency and biodistribution analysis of CRISPR-modified antibody. ( a ) Coomassie blue stained gel of sortase-mediated conjugation of modified antibody to GGG-fluorophore. ( b ) Fluorescence scan of the antibody-fluorophore, stained with anti-Flag-HRP, showing the antibody conjugated fluorophore (red tab) compared to free fluorophore (black tab). ( c ) HPLC fluorescence trace antibody-fluorophore conjugates at different molar ratios. ( d ) Quantitative analysis of the percent of antibody modification. ( e ) Binding of 125 I-labeled CRISPR-modified antibody to REN-ICAM and REN-WT cells. ( f ) Biodistribution of 125 I-labeled CRISPR-modified anti-ICAM mAb in mice at 30 min. Tissue uptake is indicated as mean ± SEM (n = 3). Biodistribution analysis was performed comparing 111 In-labeled site-specific CRISPR/Cas9- to chemically-modified mAb. ( g ) Biodistribution of 111 In-labeled anti-ICAM mAb modified in mice at 30 min. Tissue uptake is indicated as mean ± SEM. ( h ) Localization ratio of selected organs. Significant differences were determined by t-test with Bonferroni correction to account for multiple comparisons.
    Figure Legend Snippet: Conjugation efficiency and biodistribution analysis of CRISPR-modified antibody. ( a ) Coomassie blue stained gel of sortase-mediated conjugation of modified antibody to GGG-fluorophore. ( b ) Fluorescence scan of the antibody-fluorophore, stained with anti-Flag-HRP, showing the antibody conjugated fluorophore (red tab) compared to free fluorophore (black tab). ( c ) HPLC fluorescence trace antibody-fluorophore conjugates at different molar ratios. ( d ) Quantitative analysis of the percent of antibody modification. ( e ) Binding of 125 I-labeled CRISPR-modified antibody to REN-ICAM and REN-WT cells. ( f ) Biodistribution of 125 I-labeled CRISPR-modified anti-ICAM mAb in mice at 30 min. Tissue uptake is indicated as mean ± SEM (n = 3). Biodistribution analysis was performed comparing 111 In-labeled site-specific CRISPR/Cas9- to chemically-modified mAb. ( g ) Biodistribution of 111 In-labeled anti-ICAM mAb modified in mice at 30 min. Tissue uptake is indicated as mean ± SEM. ( h ) Localization ratio of selected organs. Significant differences were determined by t-test with Bonferroni correction to account for multiple comparisons.

    Techniques Used: Conjugation Assay, CRISPR, Modification, Staining, Fluorescence, High Performance Liquid Chromatography, Binding Assay, Labeling, Mouse Assay

    Schematic diagram and characterization of CRISPR/Cas9 genome editing of hybridoma cells for site-specific modification of antibodies. C-terminal end of Ig gamma-2B gene from ( a ) rat chromosome 13q24, ( b ) Fcgr2b locus, was modified by ( c ) homology directed repair to incorporate sortase and flag tags. sgRNAs with best On-Target/Off-Target scores were selected in the region near the IgG2b stop codon. ( d ) Anti-ICAMIgG2b antibodies were generated incorporating Sortase and FLAG tags at their C-terminal end. Confirmation of insert was performed by ( e ) Agarose gel analysis of PCR fragments from positive and negative clones. ( f ) Verification of integration in positive clones by sanger sequencing. ( g ) Coomassie blue stained gel of three positive clones. ( h ) Western blot of a positive clone under reducing and non-reducing conditions, stained with anti-Flag-HRP.
    Figure Legend Snippet: Schematic diagram and characterization of CRISPR/Cas9 genome editing of hybridoma cells for site-specific modification of antibodies. C-terminal end of Ig gamma-2B gene from ( a ) rat chromosome 13q24, ( b ) Fcgr2b locus, was modified by ( c ) homology directed repair to incorporate sortase and flag tags. sgRNAs with best On-Target/Off-Target scores were selected in the region near the IgG2b stop codon. ( d ) Anti-ICAMIgG2b antibodies were generated incorporating Sortase and FLAG tags at their C-terminal end. Confirmation of insert was performed by ( e ) Agarose gel analysis of PCR fragments from positive and negative clones. ( f ) Verification of integration in positive clones by sanger sequencing. ( g ) Coomassie blue stained gel of three positive clones. ( h ) Western blot of a positive clone under reducing and non-reducing conditions, stained with anti-Flag-HRP.

    Techniques Used: CRISPR, Modification, Generated, Agarose Gel Electrophoresis, Polymerase Chain Reaction, Clone Assay, Sequencing, Staining, Western Blot

    2) Product Images from "Molecular engineering of antibodies for site-specific covalent conjugation using CRISPR/Cas9"

    Article Title: Molecular engineering of antibodies for site-specific covalent conjugation using CRISPR/Cas9

    Journal: Scientific Reports

    doi: 10.1038/s41598-018-19784-2

    Conjugation efficiency and biodistribution analysis of CRISPR-modified antibody. ( a ) Coomassie blue stained gel of sortase-mediated conjugation of modified antibody to GGG-fluorophore. ( b ) Fluorescence scan of the antibody-fluorophore, stained with anti-Flag-HRP, showing the antibody conjugated fluorophore (red tab) compared to free fluorophore (black tab). ( c ) HPLC fluorescence trace antibody-fluorophore conjugates at different molar ratios. ( d ) Quantitative analysis of the percent of antibody modification. ( e ) Binding of 125 I-labeled CRISPR-modified antibody to REN-ICAM and REN-WT cells. ( f ) Biodistribution of 125 I-labeled CRISPR-modified anti-ICAM mAb in mice at 30 min. Tissue uptake is indicated as mean ± SEM (n = 3). Biodistribution analysis was performed comparing 111 In-labeled site-specific CRISPR/Cas9- to chemically-modified mAb. ( g ) Biodistribution of 111 In-labeled anti-ICAM mAb modified in mice at 30 min. Tissue uptake is indicated as mean ± SEM. ( h ) Localization ratio of selected organs. Significant differences were determined by t-test with Bonferroni correction to account for multiple comparisons.
    Figure Legend Snippet: Conjugation efficiency and biodistribution analysis of CRISPR-modified antibody. ( a ) Coomassie blue stained gel of sortase-mediated conjugation of modified antibody to GGG-fluorophore. ( b ) Fluorescence scan of the antibody-fluorophore, stained with anti-Flag-HRP, showing the antibody conjugated fluorophore (red tab) compared to free fluorophore (black tab). ( c ) HPLC fluorescence trace antibody-fluorophore conjugates at different molar ratios. ( d ) Quantitative analysis of the percent of antibody modification. ( e ) Binding of 125 I-labeled CRISPR-modified antibody to REN-ICAM and REN-WT cells. ( f ) Biodistribution of 125 I-labeled CRISPR-modified anti-ICAM mAb in mice at 30 min. Tissue uptake is indicated as mean ± SEM (n = 3). Biodistribution analysis was performed comparing 111 In-labeled site-specific CRISPR/Cas9- to chemically-modified mAb. ( g ) Biodistribution of 111 In-labeled anti-ICAM mAb modified in mice at 30 min. Tissue uptake is indicated as mean ± SEM. ( h ) Localization ratio of selected organs. Significant differences were determined by t-test with Bonferroni correction to account for multiple comparisons.

    Techniques Used: Conjugation Assay, CRISPR, Modification, Staining, Fluorescence, High Performance Liquid Chromatography, Binding Assay, Labeling, Mouse Assay

    Schematic diagram and characterization of CRISPR/Cas9 genome editing of hybridoma cells for site-specific modification of antibodies. C-terminal end of Ig gamma-2B gene from ( a ) rat chromosome 13q24, ( b ) Fcgr2b locus, was modified by ( c ) homology directed repair to incorporate sortase and flag tags. sgRNAs with best On-Target/Off-Target scores were selected in the region near the IgG2b stop codon. ( d ) Anti-ICAMIgG2b antibodies were generated incorporating Sortase and FLAG tags at their C-terminal end. Confirmation of insert was performed by ( e ) Agarose gel analysis of PCR fragments from positive and negative clones. ( f ) Verification of integration in positive clones by sanger sequencing. ( g ) Coomassie blue stained gel of three positive clones. ( h ) Western blot of a positive clone under reducing and non-reducing conditions, stained with anti-Flag-HRP.
    Figure Legend Snippet: Schematic diagram and characterization of CRISPR/Cas9 genome editing of hybridoma cells for site-specific modification of antibodies. C-terminal end of Ig gamma-2B gene from ( a ) rat chromosome 13q24, ( b ) Fcgr2b locus, was modified by ( c ) homology directed repair to incorporate sortase and flag tags. sgRNAs with best On-Target/Off-Target scores were selected in the region near the IgG2b stop codon. ( d ) Anti-ICAMIgG2b antibodies were generated incorporating Sortase and FLAG tags at their C-terminal end. Confirmation of insert was performed by ( e ) Agarose gel analysis of PCR fragments from positive and negative clones. ( f ) Verification of integration in positive clones by sanger sequencing. ( g ) Coomassie blue stained gel of three positive clones. ( h ) Western blot of a positive clone under reducing and non-reducing conditions, stained with anti-Flag-HRP.

    Techniques Used: CRISPR, Modification, Generated, Agarose Gel Electrophoresis, Polymerase Chain Reaction, Clone Assay, Sequencing, Staining, Western Blot

    Related Articles

    DNA Extraction:

    Article Title: Study on the association of the polymorphism of HLA-II gene with leukemia
    Article Snippet: Main instruments and reagents The main instruments used were PCR, refrigerated centrifuge and gel imaging instrument (all from Bio-Rad Laboratories, Inc., Hercules, CA, USA). .. The main reagents were DNA extraction and enzyme-linked immunosorbent assay (ELISA) kits (both from Qiagen, Hilden, Germany), and HLA goat anti-mouse first antibody (cat. no. ab6789; dilution, 1:1,250; Abcam, Cambridge, MA, USA) and PCR reagents (Takara Bio, Dalian, China), SSO-HLA gene type kit (Dynal, Wirral, UK). ..

    Enzyme-linked Immunosorbent Assay:

    Article Title: Study on the association of the polymorphism of HLA-II gene with leukemia
    Article Snippet: Main instruments and reagents The main instruments used were PCR, refrigerated centrifuge and gel imaging instrument (all from Bio-Rad Laboratories, Inc., Hercules, CA, USA). .. The main reagents were DNA extraction and enzyme-linked immunosorbent assay (ELISA) kits (both from Qiagen, Hilden, Germany), and HLA goat anti-mouse first antibody (cat. no. ab6789; dilution, 1:1,250; Abcam, Cambridge, MA, USA) and PCR reagents (Takara Bio, Dalian, China), SSO-HLA gene type kit (Dynal, Wirral, UK). ..

    Polymerase Chain Reaction:

    Article Title: Study on the association of the polymorphism of HLA-II gene with leukemia
    Article Snippet: Main instruments and reagents The main instruments used were PCR, refrigerated centrifuge and gel imaging instrument (all from Bio-Rad Laboratories, Inc., Hercules, CA, USA). .. The main reagents were DNA extraction and enzyme-linked immunosorbent assay (ELISA) kits (both from Qiagen, Hilden, Germany), and HLA goat anti-mouse first antibody (cat. no. ab6789; dilution, 1:1,250; Abcam, Cambridge, MA, USA) and PCR reagents (Takara Bio, Dalian, China), SSO-HLA gene type kit (Dynal, Wirral, UK). ..

    SDS Page:

    Article Title: The plasminogen binding protein PbsP is required for brain invasion by hypervirulent CC17 Group B streptococci
    Article Snippet: Cell wall extracts and immunoblots Cell wall extracts were obtained by mutanolysin extraction in a hypertonic sucrose buffer and used for Western blot analyses as described previously , . .. Briefly, 10 µg of cell wall proteins were run on polyacrylamide gels (SDS-PAGE), transferred to a nitrocellulose membrane and PbsP was visualized by chemi-luminescence after incubation with mouse anti-PbsP serum and horseradish peroxidase conjugated goat anti mouse IgG (Abcam ab6789). .. Mouse meningitis model The CC17 BM110 strain and the deletion mutants were used to induce infection in 8-week-old CD1 female mice, as previously described , .

    Incubation:

    Article Title: The plasminogen binding protein PbsP is required for brain invasion by hypervirulent CC17 Group B streptococci
    Article Snippet: Cell wall extracts and immunoblots Cell wall extracts were obtained by mutanolysin extraction in a hypertonic sucrose buffer and used for Western blot analyses as described previously , . .. Briefly, 10 µg of cell wall proteins were run on polyacrylamide gels (SDS-PAGE), transferred to a nitrocellulose membrane and PbsP was visualized by chemi-luminescence after incubation with mouse anti-PbsP serum and horseradish peroxidase conjugated goat anti mouse IgG (Abcam ab6789). .. Mouse meningitis model The CC17 BM110 strain and the deletion mutants were used to induce infection in 8-week-old CD1 female mice, as previously described , .

    Article Title: Serine/Arginine-rich Splicing Factor 2 Modulates Herpes Simplex Virus Type 1 Replication via Regulating Viral Gene Transcriptional Activity and Pre-mRNA Splicing *
    Article Snippet: The RNA immunoprecipitation assay was performed using the protocol of Peritz et al. ( ). .. Briefly, HSV-1-infected HeLa cell lysates were incubated with the anti-SRSF2 antibody (Abcam, ab11826) and IgG antibody (Abcam, ab205719) at 4 °C overnight. .. RNA enriched from the immunoprecipitation was retro-transcribed for the real-time PCR.

    Article Title: Serine/Arginine-rich Splicing Factor 2 Modulates Herpes Simplex Virus Type 1 Replication via Regulating Viral Gene Transcriptional Activity and Pre-mRNA Splicing *
    Article Snippet: Briefly, the cells were fixed with 1% formaldehyde and sonicated to shear the DNA to an average fragment size of 200–1000 bp. .. After centrifugation, the supernatants were incubated with the SRSF2 antibody (Abcam, ab11826) and IgG antibody (Abcam, ab205719). .. Chromatin DNA was purified with the Dynabeads Protein G kit (Invitrogen, 10004D) and subjected to real-time PCR.

    Centrifugation:

    Article Title: Serine/Arginine-rich Splicing Factor 2 Modulates Herpes Simplex Virus Type 1 Replication via Regulating Viral Gene Transcriptional Activity and Pre-mRNA Splicing *
    Article Snippet: Briefly, the cells were fixed with 1% formaldehyde and sonicated to shear the DNA to an average fragment size of 200–1000 bp. .. After centrifugation, the supernatants were incubated with the SRSF2 antibody (Abcam, ab11826) and IgG antibody (Abcam, ab205719). .. Chromatin DNA was purified with the Dynabeads Protein G kit (Invitrogen, 10004D) and subjected to real-time PCR.

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 95
    Abcam goat anti mouse horseradish peroxidase labeled secondary antibodies
    Fluorescent images of HT-29 cells infected with Ad-hITF. The hITF was detected using <t>mouse</t> <t>anti-hITF</t> antibodies and <t>goat</t> anti-mouse <t>TRITC-labeled</t> <t>secondary</t> antibodies. Nuclei were stained with DAPI. A, GFP; B, hITF; C, cell nuclei; D, merged images.
    Goat Anti Mouse Horseradish Peroxidase Labeled Secondary Antibodies, supplied by Abcam, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/goat anti mouse horseradish peroxidase labeled secondary antibodies/product/Abcam
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    goat anti mouse horseradish peroxidase labeled secondary antibodies - by Bioz Stars, 2021-06
    95/100 stars
      Buy from Supplier

    94
    Abcam hrp conjugated anti mouse igg secondary antibody
    Mutation of arginine (R) 424 to serine (S) confers resistance to binding of plasma antibodies. (A) Lysates of cells transfected with Bole1a_R424 and Bole1_S424 E1E2 expression constructs were used in enzyme-linked immunosorbent assays (ELISAs) to assess E1E2 binding by <t>IgG</t> in the same panel of 19 HCV-infected plasma samples. Each of the 19 plasma samples was assayed in duplicate, and antibody binding was detected using <t>HRP-conjugated</t> anti-human IgG secondary antibody. Each point represents the mean of two replicate values, and each line indicates binding by IgG from a unique plasma sample. P values were calculated using a paired two-tailed Student's t test. OD 450 ).
    Hrp Conjugated Anti Mouse Igg Secondary Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hrp conjugated anti mouse igg secondary antibody/product/Abcam
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    hrp conjugated anti mouse igg secondary antibody - by Bioz Stars, 2021-06
    94/100 stars
      Buy from Supplier

    85
    Abcam goat anti mouse hrp conjugate secondary antibody
    Soluble partially purified KMO-FLAG. (A) Western blot using chemiluminescence detection, anti-FLAG M2 antibody and goat anti-mouse <t>HRP</t> secondary antibody, (a) soluble fraction from over-expressed KMO-12His-FLAG (57 kDa) in bacterial cells. (B) SDS-PAGE gel stained with simplyblue showing anti-FLAG conjugated protein A magnetic bead purification of KMO-12His-FLAG, (a) Cell-free extract prior to purification, (b) flowthrough proteins which did not bind to the beads, (c) first magnetic bead wash, (d) second bead wash, (e) purified KMO-12His (57 kDa) (bold arrow) eluted from the beads by TEV protease has precipitated with two contaminant E . coli proteins (indicated using arrows). (C) Cartoon illustrating the <t>flKMO-12His-FLAG</t> construct. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)
    Goat Anti Mouse Hrp Conjugate Secondary Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/goat anti mouse hrp conjugate secondary antibody/product/Abcam
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    goat anti mouse hrp conjugate secondary antibody - by Bioz Stars, 2021-06
    85/100 stars
      Buy from Supplier

    Image Search Results


    Fluorescent images of HT-29 cells infected with Ad-hITF. The hITF was detected using mouse anti-hITF antibodies and goat anti-mouse TRITC-labeled secondary antibodies. Nuclei were stained with DAPI. A, GFP; B, hITF; C, cell nuclei; D, merged images.

    Journal: PLoS ONE

    Article Title: Recombinant Adenovirus-Mediated Intestinal Trefoil Factor Gene Therapy for Burn-Induced Intestinal Mucosal Injury

    doi: 10.1371/journal.pone.0062429

    Figure Lengend Snippet: Fluorescent images of HT-29 cells infected with Ad-hITF. The hITF was detected using mouse anti-hITF antibodies and goat anti-mouse TRITC-labeled secondary antibodies. Nuclei were stained with DAPI. A, GFP; B, hITF; C, cell nuclei; D, merged images.

    Article Snippet: Mouse anti-hITF antibodies and goat anti-mouse horseradish peroxidase-labeled secondary antibodies were purchased from Abcom (Cambridge, MA, USA).

    Techniques: Infection, Labeling, Staining

    Mutation of arginine (R) 424 to serine (S) confers resistance to binding of plasma antibodies. (A) Lysates of cells transfected with Bole1a_R424 and Bole1_S424 E1E2 expression constructs were used in enzyme-linked immunosorbent assays (ELISAs) to assess E1E2 binding by IgG in the same panel of 19 HCV-infected plasma samples. Each of the 19 plasma samples was assayed in duplicate, and antibody binding was detected using HRP-conjugated anti-human IgG secondary antibody. Each point represents the mean of two replicate values, and each line indicates binding by IgG from a unique plasma sample. P values were calculated using a paired two-tailed Student's t test. OD 450 ).

    Journal: Journal of Virology

    Article Title: A Hepatitis C Virus Envelope Polymorphism Confers Resistance to Neutralization by Polyclonal Sera and Broadly Neutralizing Monoclonal Antibodies

    doi: 10.1128/JVI.02837-15

    Figure Lengend Snippet: Mutation of arginine (R) 424 to serine (S) confers resistance to binding of plasma antibodies. (A) Lysates of cells transfected with Bole1a_R424 and Bole1_S424 E1E2 expression constructs were used in enzyme-linked immunosorbent assays (ELISAs) to assess E1E2 binding by IgG in the same panel of 19 HCV-infected plasma samples. Each of the 19 plasma samples was assayed in duplicate, and antibody binding was detected using HRP-conjugated anti-human IgG secondary antibody. Each point represents the mean of two replicate values, and each line indicates binding by IgG from a unique plasma sample. P values were calculated using a paired two-tailed Student's t test. OD 450 ).

    Article Snippet: HCVpp Western blots were also probed with mouse anti-HIV1 p24 (ab9044; Abcam) followed by HRP-conjugated anti-mouse IgG secondary antibody (ab97265; Abcam).

    Techniques: Mutagenesis, Binding Assay, Transfection, Expressing, Construct, Infection, Two Tailed Test

    Mutation of arginine 424 to serine confers resistance to binding of broadly neutralizing monoclonal antibodies. (A) Binding of MAbs AR3A, CBH-5, HC84.22, and AR4A to Bole1a_R424 and Bole1a_S424 E1E2 lysates was measured by ELISA. MAbs were assayed in duplicate with 2.5-fold serial dilutions, starting at 10 μg/ml, and binding was detected using HRP-conjugated anti-human IgG secondary antibody. Values shown represent the means of the results determined with two replicates, and error bars indicate standard deviations. P values were determined by two-way ANOVA (****, P

    Journal: Journal of Virology

    Article Title: A Hepatitis C Virus Envelope Polymorphism Confers Resistance to Neutralization by Polyclonal Sera and Broadly Neutralizing Monoclonal Antibodies

    doi: 10.1128/JVI.02837-15

    Figure Lengend Snippet: Mutation of arginine 424 to serine confers resistance to binding of broadly neutralizing monoclonal antibodies. (A) Binding of MAbs AR3A, CBH-5, HC84.22, and AR4A to Bole1a_R424 and Bole1a_S424 E1E2 lysates was measured by ELISA. MAbs were assayed in duplicate with 2.5-fold serial dilutions, starting at 10 μg/ml, and binding was detected using HRP-conjugated anti-human IgG secondary antibody. Values shown represent the means of the results determined with two replicates, and error bars indicate standard deviations. P values were determined by two-way ANOVA (****, P

    Article Snippet: HCVpp Western blots were also probed with mouse anti-HIV1 p24 (ab9044; Abcam) followed by HRP-conjugated anti-mouse IgG secondary antibody (ab97265; Abcam).

    Techniques: Mutagenesis, Binding Assay, Enzyme-linked Immunosorbent Assay

    Mice immunized intranasally with the yersiniabactin receptor FyuA produce FyuA-specific urinary antibodies. Urine collected from mice immunized with FyuA-CT (FyuA) or CT was plated on FyuA-coated plates and probed for FyuA-specific IgA (A) or IgG (B)

    Journal: Infection and Immunity

    Article Title: Immunization with the Yersiniabactin Receptor, FyuA, Protects against Pyelonephritis in a Murine Model of Urinary Tract Infection

    doi: 10.1128/IAI.00470-13

    Figure Lengend Snippet: Mice immunized intranasally with the yersiniabactin receptor FyuA produce FyuA-specific urinary antibodies. Urine collected from mice immunized with FyuA-CT (FyuA) or CT was plated on FyuA-coated plates and probed for FyuA-specific IgA (A) or IgG (B)

    Article Snippet: The plates were washed with wash buffer and coated with the secondary antibody, goat anti-mouse IgG (ab97265; Abcam) or goat anti-mouse IgA (ab97235; Abcam), diluted 1:10,000 in blocking buffer, and allowed to incubate at 23°C for 1 h. The plates were washed, and 50 μl of the substrate, 1-Step ultra TMB (3,3′,5,5′-tetramethylbenzidine)-ELISA (catalog number 34018; Thermo Scientific), was added and allowed to incubate at 23°C until color developed (≤20 min).

    Techniques: Mouse Assay

    Soluble partially purified KMO-FLAG. (A) Western blot using chemiluminescence detection, anti-FLAG M2 antibody and goat anti-mouse HRP secondary antibody, (a) soluble fraction from over-expressed KMO-12His-FLAG (57 kDa) in bacterial cells. (B) SDS-PAGE gel stained with simplyblue showing anti-FLAG conjugated protein A magnetic bead purification of KMO-12His-FLAG, (a) Cell-free extract prior to purification, (b) flowthrough proteins which did not bind to the beads, (c) first magnetic bead wash, (d) second bead wash, (e) purified KMO-12His (57 kDa) (bold arrow) eluted from the beads by TEV protease has precipitated with two contaminant E . coli proteins (indicated using arrows). (C) Cartoon illustrating the flKMO-12His-FLAG construct. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Journal: Protein Expression and Purification

    Article Title: Bacterial expression of human kynurenine 3-monooxygenase: Solubility, activity, purification

    doi: 10.1016/j.pep.2013.11.015

    Figure Lengend Snippet: Soluble partially purified KMO-FLAG. (A) Western blot using chemiluminescence detection, anti-FLAG M2 antibody and goat anti-mouse HRP secondary antibody, (a) soluble fraction from over-expressed KMO-12His-FLAG (57 kDa) in bacterial cells. (B) SDS-PAGE gel stained with simplyblue showing anti-FLAG conjugated protein A magnetic bead purification of KMO-12His-FLAG, (a) Cell-free extract prior to purification, (b) flowthrough proteins which did not bind to the beads, (c) first magnetic bead wash, (d) second bead wash, (e) purified KMO-12His (57 kDa) (bold arrow) eluted from the beads by TEV protease has precipitated with two contaminant E . coli proteins (indicated using arrows). (C) Cartoon illustrating the flKMO-12His-FLAG construct. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Article Snippet: Anti-His(C-term)-HRP antibody (Invitrogen, R931-25) (1:2000 dilution) was used to detect the truncate and flKMO proteins, and anti-FLAG M2 antibody (Sigma Aldrich, F1804) (1:1000) with goat anti-mouse HRP conjugate secondary antibody (Abcam, ab6832) (1:10 000) was used to detect KMO-FLAG protein.

    Techniques: Purification, Western Blot, SDS Page, Staining, Construct

    Insoluble flKMO. (A) SDS-PAGE protein gel stained with simplyblue. Lane 1. Soluble fraction following over-expression of full length KMO in bacterial cells. Lane 2. Insoluble fraction, KMO protein (55 kDa) highlighted by arrow. (B) Western blot of the same samples, chemiluminescence detection using Anti-His(c-term)-HRP antibody. Lanes as before. The majority of the KMO protein is present in the insoluble fraction. (C) Cartoon illustrating the flKMO-6His construct. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Journal: Protein Expression and Purification

    Article Title: Bacterial expression of human kynurenine 3-monooxygenase: Solubility, activity, purification

    doi: 10.1016/j.pep.2013.11.015

    Figure Lengend Snippet: Insoluble flKMO. (A) SDS-PAGE protein gel stained with simplyblue. Lane 1. Soluble fraction following over-expression of full length KMO in bacterial cells. Lane 2. Insoluble fraction, KMO protein (55 kDa) highlighted by arrow. (B) Western blot of the same samples, chemiluminescence detection using Anti-His(c-term)-HRP antibody. Lanes as before. The majority of the KMO protein is present in the insoluble fraction. (C) Cartoon illustrating the flKMO-6His construct. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Article Snippet: Anti-His(C-term)-HRP antibody (Invitrogen, R931-25) (1:2000 dilution) was used to detect the truncate and flKMO proteins, and anti-FLAG M2 antibody (Sigma Aldrich, F1804) (1:1000) with goat anti-mouse HRP conjugate secondary antibody (Abcam, ab6832) (1:10 000) was used to detect KMO-FLAG protein.

    Techniques: SDS Page, Staining, Over Expression, Western Blot, Construct