goat igg1  (Bio-Rad)

 
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  • 95
    Name:
    Goat F ab 2 anti Mouse IgG1 Heavy Chain Human Adsorbed
    Description:

    Catalog Number:
    STAR185
    Price:
    None
    Applications:
    ELISA, Immunofluorescence, Western Blotting
    Format:
    Purified
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    Structured Review

    Bio-Rad goat igg1
    Inhibition of binding of labeled goat <t>IgG1</t> or labeled rabbit IgG to MAL5R-coated surfaces by human Fc fragment. The 100% binding value represents the interaction between labeled IgG and MAL5R in the absence of inhibitors.

    https://www.bioz.com/result/goat igg1/product/Bio-Rad
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    goat igg1 - by Bioz Stars, 2020-09
    95/100 stars

    Images

    1) Product Images from "Five Homologous Repeats of the Protein G-Related Protein MIG Cooperate in Binding to Goat Immunoglobulin G"

    Article Title: Five Homologous Repeats of the Protein G-Related Protein MIG Cooperate in Binding to Goat Immunoglobulin G

    Journal: Infection and Immunity

    doi:

    Inhibition of binding of labeled goat IgG1 or labeled rabbit IgG to MAL5R-coated surfaces by human Fc fragment. The 100% binding value represents the interaction between labeled IgG and MAL5R in the absence of inhibitors.
    Figure Legend Snippet: Inhibition of binding of labeled goat IgG1 or labeled rabbit IgG to MAL5R-coated surfaces by human Fc fragment. The 100% binding value represents the interaction between labeled IgG and MAL5R in the absence of inhibitors.

    Techniques Used: Inhibition, Binding Assay, Labeling

    Schematic representation of the native MIG protein molecule and the fragments and peptides derived from the IgG-binding domain. (A) The numbers 1 through 5 indicate the five repeats of the IgG-binding domain, and the hatched area represents the cell wall-spanning and membrane-anchoring regions of the native molecule. The various fragments were expressed as fusions with the maltose-binding protein (MBP). The molecular masses of the proteins calculated from the amino acid sequences are given in parentheses. (B) Schematic representation of the peptides derived from the first IgG-binding repeat of protein MIG and the C1 domain of protein G. The numbers above the upper bar indicate the amino acid positions in the one repeat of protein MIG. The lower bar represents the truncated form of the repeat (1RCT). The arrows show the sequences of the 11-amino-acid-long peptides derived from the repeat and the corresponding region in the C1 domain of protein G. The identical amino acids in these two peptides are indicated by vertical bars.
    Figure Legend Snippet: Schematic representation of the native MIG protein molecule and the fragments and peptides derived from the IgG-binding domain. (A) The numbers 1 through 5 indicate the five repeats of the IgG-binding domain, and the hatched area represents the cell wall-spanning and membrane-anchoring regions of the native molecule. The various fragments were expressed as fusions with the maltose-binding protein (MBP). The molecular masses of the proteins calculated from the amino acid sequences are given in parentheses. (B) Schematic representation of the peptides derived from the first IgG-binding repeat of protein MIG and the C1 domain of protein G. The numbers above the upper bar indicate the amino acid positions in the one repeat of protein MIG. The lower bar represents the truncated form of the repeat (1RCT). The arrows show the sequences of the 11-amino-acid-long peptides derived from the repeat and the corresponding region in the C1 domain of protein G. The identical amino acids in these two peptides are indicated by vertical bars.

    Techniques Used: Derivative Assay, Binding Assay

    Competition between MAL5R applied to the surfaces of microtiter plates and various protein MIG constructs in solution for binding of labeled goat IgG1. Samples from dilution series of MAL1R (•), MAL2R (□), MAL3R (▵), and MAL5R (○), mixed with an equal volume of 10 5 -diluted alkP-goat IgG1, were incubated in wells of enzyme-linked immunosorbent assay plates coated with MAL5R.
    Figure Legend Snippet: Competition between MAL5R applied to the surfaces of microtiter plates and various protein MIG constructs in solution for binding of labeled goat IgG1. Samples from dilution series of MAL1R (•), MAL2R (□), MAL3R (▵), and MAL5R (○), mixed with an equal volume of 10 5 -diluted alkP-goat IgG1, were incubated in wells of enzyme-linked immunosorbent assay plates coated with MAL5R.

    Techniques Used: Construct, Binding Assay, Labeling, Incubation, Enzyme-linked Immunosorbent Assay

    Inhibition of binding of labeled goat IgG1 to surface-bound MAL5R by MAL1RCT. The 100% binding value represents the interaction between the labeled IgG1 and MAL5R in the absence of inhibitor.
    Figure Legend Snippet: Inhibition of binding of labeled goat IgG1 to surface-bound MAL5R by MAL1RCT. The 100% binding value represents the interaction between the labeled IgG1 and MAL5R in the absence of inhibitor.

    Techniques Used: Inhibition, Binding Assay, Labeling

    Related Articles

    Binding Assay:

    Article Title: Five Homologous Repeats of the Protein G-Related Protein MIG Cooperate in Binding to Goat Immunoglobulin G
    Article Snippet: .. To investigate the influence of an increasing number of IgG-binding repeats on the interaction with goat IgG subclasses, the fusion proteins (MAL1R to MAL5R) were absorbed in wells of microtiter plates and goat IgG1 and IgG2, purified as recently described , were allowed to compete for the binding of the goat IgG1-alkaline phosphatase conjugate (alkP-IgG1; Bio-Rad). .. As shown in Fig. , the avidities of MIG constructs for goat IgG1 increased as the number of IgG-binding repeats increased.

    Blocking Assay:

    Article Title: Differential antibody response to the Anopheles gambiae gSG6 and cE5 salivary proteins in individuals naturally exposed to bites of malaria vectors
    Article Snippet: .. After washing, blocking and washing again as above wells were incubated overnight at 4°C with serial dilutions, from 1 μg/ml to 0.0078 μg/ml (1 → 0.5 → 0.25 → 0.125 → 0.0625 → 0.03125 → 0.0156 → 0.0078), of purified native human IgG1 or IgG4 (ABD Serotec, Kidlington, Oxford, UK) in 50 μl of blocking reagent. .. Incubation with anti-human IgG1/HRP or IgG4/HRP and colorimetric detection were performed as described above.

    Article Title: Salmonella Virchow Infection of the Chicken Elicits Cellular and Humoral Systemic and Mucosal Responses, but Limited Protection to Homologous or Heterologous Re-Challenge
    Article Snippet: .. Specific antibodies were detected by incubating the samples with alkaline phosphatase conjugated to either goat anti-chicken IgA (1:20000), IgM (1:1000), or IgG (1:2000) (Serotec, Oxford, UK) diluted in blocking buffer, for 1 h at 37°C. .. Plates were washed with PBS Tween-20 (0.05%) and incubated with 100 μl per well of p -nitrophenyl phosphate in the dark for 30 min at room temperature.

    Purification:

    Article Title: Five Homologous Repeats of the Protein G-Related Protein MIG Cooperate in Binding to Goat Immunoglobulin G
    Article Snippet: .. To investigate the influence of an increasing number of IgG-binding repeats on the interaction with goat IgG subclasses, the fusion proteins (MAL1R to MAL5R) were absorbed in wells of microtiter plates and goat IgG1 and IgG2, purified as recently described , were allowed to compete for the binding of the goat IgG1-alkaline phosphatase conjugate (alkP-IgG1; Bio-Rad). .. As shown in Fig. , the avidities of MIG constructs for goat IgG1 increased as the number of IgG-binding repeats increased.

    Article Title: Differential antibody response to the Anopheles gambiae gSG6 and cE5 salivary proteins in individuals naturally exposed to bites of malaria vectors
    Article Snippet: .. After washing, blocking and washing again as above wells were incubated overnight at 4°C with serial dilutions, from 1 μg/ml to 0.0078 μg/ml (1 → 0.5 → 0.25 → 0.125 → 0.0625 → 0.03125 → 0.0156 → 0.0078), of purified native human IgG1 or IgG4 (ABD Serotec, Kidlington, Oxford, UK) in 50 μl of blocking reagent. .. Incubation with anti-human IgG1/HRP or IgG4/HRP and colorimetric detection were performed as described above.

    Enzyme-linked Immunosorbent Assay:

    Article Title: Identity and validity of conserved B cell epitopes of filovirus glycoprotein: towards rapid diagnostic testing for Ebola and possibly Marburg virus disease
    Article Snippet: .. Materials and Reagents : Synthetic analogues of the filovirus GP1, 2 peptide epitopes 1, 2 and 3 (denoted UG-Filo-Peptide 1, 2 and 3 respectively, GeneCUST, Luxemburg), New Zealand Rabbit derived anti-UG-Filo-Peptide 1 and anti-UG-Filo-Peptide 3 polyclonal antibodies (denoted PAbs- A005345 and A005346 respectively), plain ELISA plates (flat bottom, Nunc), Bovine Serum Albumin (BSA, In-vitrogen, USA), recombinant EBOV GP1, 2, goat anti-human IgM and IgG (HRP labeled, Bio-Rad, France), Phosphate Buffered Saline (PBS), and the enzymatic substrate tetramethylbenzidine (TMB). .. Interventions (a) Synthetic Epitopes: Amino acid sequences of the epitopes UG-Filo-Peptide 1, 2 and 3 were loaned to GeneCUST, Luxemburg, for biochemical manufacture of synthetic analogues of the same. (b) Cloning and Expression of recombinant EBOV GP1, 2 Protein: Amino acid sequences of Zaire ebolavirus ( EBOV) sp.|Q66798| were loaned to GenSCRIPT, HGK for sub-cloning and expression of the recombinant protein in HEK293-6E cell-lines. (c) Filovirus GP1, 2 host specific IgM or IgG antibodies detection EIA: For detection of Filovirus GP1, 2 host specific IgM and IgG humoral responses in serum of 92 (of 94) EVD survivor serum, we (i) dissolved 1μg (conc: 1 mg/ml) of individual synthetic peptide by adding 100 μl of freshly prepared phosphate buffered saline (PBS was prepared by dissolving ¼ of a 250 mg tablet in 50 ml PCR grade water). (ii) 100 μl (0.001 ng) of individual synthetic peptide (UG-Filo-Peptide-01 & UG-Filo-Peptide-02) was then pipetted into each of the wells of a sterile 96-well microtiter plate (Nunc) and the plate incubated overnight. (iii) The plated wells were then blocked once the following day using 5% BSA in PBS and incubated at 37 °C for 30 mins, after which excess solution was discarded and plate left to dry. (iv) 100μls of PBS was added to each assigned wells, followed by addition of 10 μl (1:100 dilution) of samples into the respective wells; after which the plate was shaken at 15HZ for 16 s, and then incubated for 1 h at 37 °C.

    Incubation:

    Article Title: Differential antibody response to the Anopheles gambiae gSG6 and cE5 salivary proteins in individuals naturally exposed to bites of malaria vectors
    Article Snippet: .. After washing, blocking and washing again as above wells were incubated overnight at 4°C with serial dilutions, from 1 μg/ml to 0.0078 μg/ml (1 → 0.5 → 0.25 → 0.125 → 0.0625 → 0.03125 → 0.0156 → 0.0078), of purified native human IgG1 or IgG4 (ABD Serotec, Kidlington, Oxford, UK) in 50 μl of blocking reagent. .. Incubation with anti-human IgG1/HRP or IgG4/HRP and colorimetric detection were performed as described above.

    Labeling:

    Article Title: Identity and validity of conserved B cell epitopes of filovirus glycoprotein: towards rapid diagnostic testing for Ebola and possibly Marburg virus disease
    Article Snippet: .. Materials and Reagents : Synthetic analogues of the filovirus GP1, 2 peptide epitopes 1, 2 and 3 (denoted UG-Filo-Peptide 1, 2 and 3 respectively, GeneCUST, Luxemburg), New Zealand Rabbit derived anti-UG-Filo-Peptide 1 and anti-UG-Filo-Peptide 3 polyclonal antibodies (denoted PAbs- A005345 and A005346 respectively), plain ELISA plates (flat bottom, Nunc), Bovine Serum Albumin (BSA, In-vitrogen, USA), recombinant EBOV GP1, 2, goat anti-human IgM and IgG (HRP labeled, Bio-Rad, France), Phosphate Buffered Saline (PBS), and the enzymatic substrate tetramethylbenzidine (TMB). .. Interventions (a) Synthetic Epitopes: Amino acid sequences of the epitopes UG-Filo-Peptide 1, 2 and 3 were loaned to GeneCUST, Luxemburg, for biochemical manufacture of synthetic analogues of the same. (b) Cloning and Expression of recombinant EBOV GP1, 2 Protein: Amino acid sequences of Zaire ebolavirus ( EBOV) sp.|Q66798| were loaned to GenSCRIPT, HGK for sub-cloning and expression of the recombinant protein in HEK293-6E cell-lines. (c) Filovirus GP1, 2 host specific IgM or IgG antibodies detection EIA: For detection of Filovirus GP1, 2 host specific IgM and IgG humoral responses in serum of 92 (of 94) EVD survivor serum, we (i) dissolved 1μg (conc: 1 mg/ml) of individual synthetic peptide by adding 100 μl of freshly prepared phosphate buffered saline (PBS was prepared by dissolving ¼ of a 250 mg tablet in 50 ml PCR grade water). (ii) 100 μl (0.001 ng) of individual synthetic peptide (UG-Filo-Peptide-01 & UG-Filo-Peptide-02) was then pipetted into each of the wells of a sterile 96-well microtiter plate (Nunc) and the plate incubated overnight. (iii) The plated wells were then blocked once the following day using 5% BSA in PBS and incubated at 37 °C for 30 mins, after which excess solution was discarded and plate left to dry. (iv) 100μls of PBS was added to each assigned wells, followed by addition of 10 μl (1:100 dilution) of samples into the respective wells; after which the plate was shaken at 15HZ for 16 s, and then incubated for 1 h at 37 °C.

    Recombinant:

    Article Title: Identity and validity of conserved B cell epitopes of filovirus glycoprotein: towards rapid diagnostic testing for Ebola and possibly Marburg virus disease
    Article Snippet: .. Materials and Reagents : Synthetic analogues of the filovirus GP1, 2 peptide epitopes 1, 2 and 3 (denoted UG-Filo-Peptide 1, 2 and 3 respectively, GeneCUST, Luxemburg), New Zealand Rabbit derived anti-UG-Filo-Peptide 1 and anti-UG-Filo-Peptide 3 polyclonal antibodies (denoted PAbs- A005345 and A005346 respectively), plain ELISA plates (flat bottom, Nunc), Bovine Serum Albumin (BSA, In-vitrogen, USA), recombinant EBOV GP1, 2, goat anti-human IgM and IgG (HRP labeled, Bio-Rad, France), Phosphate Buffered Saline (PBS), and the enzymatic substrate tetramethylbenzidine (TMB). .. Interventions (a) Synthetic Epitopes: Amino acid sequences of the epitopes UG-Filo-Peptide 1, 2 and 3 were loaned to GeneCUST, Luxemburg, for biochemical manufacture of synthetic analogues of the same. (b) Cloning and Expression of recombinant EBOV GP1, 2 Protein: Amino acid sequences of Zaire ebolavirus ( EBOV) sp.|Q66798| were loaned to GenSCRIPT, HGK for sub-cloning and expression of the recombinant protein in HEK293-6E cell-lines. (c) Filovirus GP1, 2 host specific IgM or IgG antibodies detection EIA: For detection of Filovirus GP1, 2 host specific IgM and IgG humoral responses in serum of 92 (of 94) EVD survivor serum, we (i) dissolved 1μg (conc: 1 mg/ml) of individual synthetic peptide by adding 100 μl of freshly prepared phosphate buffered saline (PBS was prepared by dissolving ¼ of a 250 mg tablet in 50 ml PCR grade water). (ii) 100 μl (0.001 ng) of individual synthetic peptide (UG-Filo-Peptide-01 & UG-Filo-Peptide-02) was then pipetted into each of the wells of a sterile 96-well microtiter plate (Nunc) and the plate incubated overnight. (iii) The plated wells were then blocked once the following day using 5% BSA in PBS and incubated at 37 °C for 30 mins, after which excess solution was discarded and plate left to dry. (iv) 100μls of PBS was added to each assigned wells, followed by addition of 10 μl (1:100 dilution) of samples into the respective wells; after which the plate was shaken at 15HZ for 16 s, and then incubated for 1 h at 37 °C.

    Derivative Assay:

    Article Title: Identity and validity of conserved B cell epitopes of filovirus glycoprotein: towards rapid diagnostic testing for Ebola and possibly Marburg virus disease
    Article Snippet: .. Materials and Reagents : Synthetic analogues of the filovirus GP1, 2 peptide epitopes 1, 2 and 3 (denoted UG-Filo-Peptide 1, 2 and 3 respectively, GeneCUST, Luxemburg), New Zealand Rabbit derived anti-UG-Filo-Peptide 1 and anti-UG-Filo-Peptide 3 polyclonal antibodies (denoted PAbs- A005345 and A005346 respectively), plain ELISA plates (flat bottom, Nunc), Bovine Serum Albumin (BSA, In-vitrogen, USA), recombinant EBOV GP1, 2, goat anti-human IgM and IgG (HRP labeled, Bio-Rad, France), Phosphate Buffered Saline (PBS), and the enzymatic substrate tetramethylbenzidine (TMB). .. Interventions (a) Synthetic Epitopes: Amino acid sequences of the epitopes UG-Filo-Peptide 1, 2 and 3 were loaned to GeneCUST, Luxemburg, for biochemical manufacture of synthetic analogues of the same. (b) Cloning and Expression of recombinant EBOV GP1, 2 Protein: Amino acid sequences of Zaire ebolavirus ( EBOV) sp.|Q66798| were loaned to GenSCRIPT, HGK for sub-cloning and expression of the recombinant protein in HEK293-6E cell-lines. (c) Filovirus GP1, 2 host specific IgM or IgG antibodies detection EIA: For detection of Filovirus GP1, 2 host specific IgM and IgG humoral responses in serum of 92 (of 94) EVD survivor serum, we (i) dissolved 1μg (conc: 1 mg/ml) of individual synthetic peptide by adding 100 μl of freshly prepared phosphate buffered saline (PBS was prepared by dissolving ¼ of a 250 mg tablet in 50 ml PCR grade water). (ii) 100 μl (0.001 ng) of individual synthetic peptide (UG-Filo-Peptide-01 & UG-Filo-Peptide-02) was then pipetted into each of the wells of a sterile 96-well microtiter plate (Nunc) and the plate incubated overnight. (iii) The plated wells were then blocked once the following day using 5% BSA in PBS and incubated at 37 °C for 30 mins, after which excess solution was discarded and plate left to dry. (iv) 100μls of PBS was added to each assigned wells, followed by addition of 10 μl (1:100 dilution) of samples into the respective wells; after which the plate was shaken at 15HZ for 16 s, and then incubated for 1 h at 37 °C.

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  • 99
    Bio-Rad goat anti human igg horseradish peroxidase conjugate
    CENP-A, CENP-B, and CENP-C were coprecipitated by CHIP using anti-CENP-A and/or anti-CENP-C antibodies. (A) Indirect immunofluorescence microscopy using newly prepared anti-CENP-A (top right) and anti-CENP-C (top left) antibodies. Mitotic chromosomes from HeLa cells were stained with anti-CENP-A or anti-CENP-C antibodies. Second antibodies were anti-mouse <t>IgG-fluorescein</t> isothiocyanate (FITC) conjugate for CENP-A, and anti-guinea pig IgG-rhodamine isothiocyanate (RITC) conjugate for CENP-C. Chromosomes were stained with DAPI (4′,6′-diamidino-3-phenylindole, bottom left). The three panels were merged (bottom right). CENP-A, green; CENP-C, red; DNA, white. (B) CHIP of the solubilized chromatin. Isolated HeLa nuclei were digested with 40 U of MNase per ml for 5 min (lanes 1 and 3) or 80 U/ml for 45 min (lanes 2 and 4), and the soluble fractions were subjected to CHIP using anti-CENP-A (lanes 1 and 2) or anti-CENP-C (lanes 3 and 4) antibodies. The precipitated proteins were separated by SDS-7.5% (for CENP-B and -C) or 12.5% (for CENP-A) PAGE, and the centromere proteins were detected by Western blotting using <t>ACA</t> serum (AK). Lane M shows the positions of CENP-A, CENP-B, and CENP-C. Positions of molecular size markers are indicated at the right.
    Goat Anti Human Igg Horseradish Peroxidase Conjugate, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/goat anti human igg horseradish peroxidase conjugate/product/Bio-Rad
    Average 99 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    goat anti human igg horseradish peroxidase conjugate - by Bioz Stars, 2020-09
    99/100 stars
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    88
    Bio-Rad peroxidase conjugated goat anti human immunoglobulin g igg
    (Left panel) SDS-PAGE and Coomassie staining of H. ducreyi outer membrane proteins and purified recombinant proteins. H. ducreyi strain 35000 was grown under heme-limiting conditions to induce synthesis of HgbA and TdhA. Recombinant His-tagged proteins were purified from E. coli as described in the text. Lanes: OMP, H. ducreyi outer membrane proteins (30 μg); rHgbA, rTdhA, rD15, purified recombinant proteins (2 μg each). Note the larger sizes of the hexahistidine leader-containing recombinant proteins compared to their respective native proteins. (Right panel) Western blots of H. ducreyi outer membrane proteins and recombinant proteins. Blots A, B, and C were probed with affinity-purified antipeptide <t>IgG</t> to HgbA, TdhA, or D15, respectively. In blot A, only 5 μg of outer membrane protein was loaded to visualize the abundant HgbA protein. In blots B and C, 30 μg of outer membrane protein was loaded to visualize the less abundant TdhA and D15 proteins. Each lane of recombinant protein contained 200 to 400 ng of protein.
    Peroxidase Conjugated Goat Anti Human Immunoglobulin G Igg, 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/peroxidase conjugated goat anti human immunoglobulin g igg/product/Bio-Rad
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    88/100 stars
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    91
    Bio-Rad horseradish peroxidase conjugated goat antimonkey immunoglobulin g igg
    Serum antibody responses of BPZE1-inoculated baboons. <t>Immunoglobulin</t> G <t>(IgG)</t> ( A ) and immunoglobulin A (IgA) ( B ) titers were measured against filamentous hemagglutinin (FHA) (upper panels), pertussis toxin (PT) (middle panels), and pertactin (Prn) (lower panels) at the indicated time points after administration of BPZE1. Each symbol represents an individual animal. Blue, red, and green symbols indicate antibody titers of noninfected animals, baboons inoculated with 10 9 colony-forming units (CFU) BPZE1, and baboons inoculated with 10 10 CFU BPZE1, respectively.
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    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.
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    Image Search Results


    CENP-A, CENP-B, and CENP-C were coprecipitated by CHIP using anti-CENP-A and/or anti-CENP-C antibodies. (A) Indirect immunofluorescence microscopy using newly prepared anti-CENP-A (top right) and anti-CENP-C (top left) antibodies. Mitotic chromosomes from HeLa cells were stained with anti-CENP-A or anti-CENP-C antibodies. Second antibodies were anti-mouse IgG-fluorescein isothiocyanate (FITC) conjugate for CENP-A, and anti-guinea pig IgG-rhodamine isothiocyanate (RITC) conjugate for CENP-C. Chromosomes were stained with DAPI (4′,6′-diamidino-3-phenylindole, bottom left). The three panels were merged (bottom right). CENP-A, green; CENP-C, red; DNA, white. (B) CHIP of the solubilized chromatin. Isolated HeLa nuclei were digested with 40 U of MNase per ml for 5 min (lanes 1 and 3) or 80 U/ml for 45 min (lanes 2 and 4), and the soluble fractions were subjected to CHIP using anti-CENP-A (lanes 1 and 2) or anti-CENP-C (lanes 3 and 4) antibodies. The precipitated proteins were separated by SDS-7.5% (for CENP-B and -C) or 12.5% (for CENP-A) PAGE, and the centromere proteins were detected by Western blotting using ACA serum (AK). Lane M shows the positions of CENP-A, CENP-B, and CENP-C. Positions of molecular size markers are indicated at the right.

    Journal: Molecular and Cellular Biology

    Article Title: CENP-A, -B, and -C Chromatin Complex That Contains the I-Type ?-Satellite Array Constitutes the Prekinetochore in HeLa Cells

    doi: 10.1128/MCB.22.7.2229-2241.2002

    Figure Lengend Snippet: CENP-A, CENP-B, and CENP-C were coprecipitated by CHIP using anti-CENP-A and/or anti-CENP-C antibodies. (A) Indirect immunofluorescence microscopy using newly prepared anti-CENP-A (top right) and anti-CENP-C (top left) antibodies. Mitotic chromosomes from HeLa cells were stained with anti-CENP-A or anti-CENP-C antibodies. Second antibodies were anti-mouse IgG-fluorescein isothiocyanate (FITC) conjugate for CENP-A, and anti-guinea pig IgG-rhodamine isothiocyanate (RITC) conjugate for CENP-C. Chromosomes were stained with DAPI (4′,6′-diamidino-3-phenylindole, bottom left). The three panels were merged (bottom right). CENP-A, green; CENP-C, red; DNA, white. (B) CHIP of the solubilized chromatin. Isolated HeLa nuclei were digested with 40 U of MNase per ml for 5 min (lanes 1 and 3) or 80 U/ml for 45 min (lanes 2 and 4), and the soluble fractions were subjected to CHIP using anti-CENP-A (lanes 1 and 2) or anti-CENP-C (lanes 3 and 4) antibodies. The precipitated proteins were separated by SDS-7.5% (for CENP-B and -C) or 12.5% (for CENP-A) PAGE, and the centromere proteins were detected by Western blotting using ACA serum (AK). Lane M shows the positions of CENP-A, CENP-B, and CENP-C. Positions of molecular size markers are indicated at the right.

    Article Snippet: ACA serum (AK, 1:3,000 dilution) and goat anti-human IgG-horseradish peroxidase conjugate (Bio-Rad, 1:3,000 dilution) were used for immunodetection.

    Techniques: Chromatin Immunoprecipitation, Immunofluorescence, Microscopy, Staining, Isolation, Polyacrylamide Gel Electrophoresis, Western Blot

    (Left panel) SDS-PAGE and Coomassie staining of H. ducreyi outer membrane proteins and purified recombinant proteins. H. ducreyi strain 35000 was grown under heme-limiting conditions to induce synthesis of HgbA and TdhA. Recombinant His-tagged proteins were purified from E. coli as described in the text. Lanes: OMP, H. ducreyi outer membrane proteins (30 μg); rHgbA, rTdhA, rD15, purified recombinant proteins (2 μg each). Note the larger sizes of the hexahistidine leader-containing recombinant proteins compared to their respective native proteins. (Right panel) Western blots of H. ducreyi outer membrane proteins and recombinant proteins. Blots A, B, and C were probed with affinity-purified antipeptide IgG to HgbA, TdhA, or D15, respectively. In blot A, only 5 μg of outer membrane protein was loaded to visualize the abundant HgbA protein. In blots B and C, 30 μg of outer membrane protein was loaded to visualize the less abundant TdhA and D15 proteins. Each lane of recombinant protein contained 200 to 400 ng of protein.

    Journal: Journal of Clinical Microbiology

    Article Title: Development of a Serological Test for Haemophilus ducreyi for Seroprevalence Studies

    doi:

    Figure Lengend Snippet: (Left panel) SDS-PAGE and Coomassie staining of H. ducreyi outer membrane proteins and purified recombinant proteins. H. ducreyi strain 35000 was grown under heme-limiting conditions to induce synthesis of HgbA and TdhA. Recombinant His-tagged proteins were purified from E. coli as described in the text. Lanes: OMP, H. ducreyi outer membrane proteins (30 μg); rHgbA, rTdhA, rD15, purified recombinant proteins (2 μg each). Note the larger sizes of the hexahistidine leader-containing recombinant proteins compared to their respective native proteins. (Right panel) Western blots of H. ducreyi outer membrane proteins and recombinant proteins. Blots A, B, and C were probed with affinity-purified antipeptide IgG to HgbA, TdhA, or D15, respectively. In blot A, only 5 μg of outer membrane protein was loaded to visualize the abundant HgbA protein. In blots B and C, 30 μg of outer membrane protein was loaded to visualize the less abundant TdhA and D15 proteins. Each lane of recombinant protein contained 200 to 400 ng of protein.

    Article Snippet: One hundred microliters of a 1:1,000 dilution of horseradish peroxidase-conjugated goat anti-human immunoglobulin G (IgG) (EIA grade; Bio-Rad Laboratories, Hercules, Calif.) was added to each well.

    Techniques: SDS Page, Staining, Purification, Recombinant, Western Blot, Affinity Purification

    Serum antibody responses of BPZE1-inoculated baboons. Immunoglobulin G (IgG) ( A ) and immunoglobulin A (IgA) ( B ) titers were measured against filamentous hemagglutinin (FHA) (upper panels), pertussis toxin (PT) (middle panels), and pertactin (Prn) (lower panels) at the indicated time points after administration of BPZE1. Each symbol represents an individual animal. Blue, red, and green symbols indicate antibody titers of noninfected animals, baboons inoculated with 10 9 colony-forming units (CFU) BPZE1, and baboons inoculated with 10 10 CFU BPZE1, respectively.

    Journal: The Journal of Infectious Diseases

    Article Title: Live Attenuated Pertussis Vaccine BPZE1 Protects Baboons Against Bordetella pertussis Disease and Infection

    doi: 10.1093/infdis/jix254

    Figure Lengend Snippet: Serum antibody responses of BPZE1-inoculated baboons. Immunoglobulin G (IgG) ( A ) and immunoglobulin A (IgA) ( B ) titers were measured against filamentous hemagglutinin (FHA) (upper panels), pertussis toxin (PT) (middle panels), and pertactin (Prn) (lower panels) at the indicated time points after administration of BPZE1. Each symbol represents an individual animal. Blue, red, and green symbols indicate antibody titers of noninfected animals, baboons inoculated with 10 9 colony-forming units (CFU) BPZE1, and baboons inoculated with 10 10 CFU BPZE1, respectively.

    Article Snippet: After 6 washes with PBS, 100 µL/well of horseradish peroxidase–conjugated goat antimonkey immunoglobulin G (IgG) (BioRad) or antimonkey immunoglobulin A (IgA) (Sigma-Aldrich), diluted 1:10000 in PBS, was added.

    Techniques:

    Booster effect of Bordetella pertussis D420 challenge in BPZE1-vaccinated baboons. Immunoglobulin G (IgG) ( A ) and immunoglobulin A (IgA) ( B ) titers were measured against filamentous hemagglutinin (FHA) (upper panels), pertussis toxin (PT) (middle panels), and pertactin (Prn) (lower panels) at the indicated time points after challenge with B. pertussis D420. Each symbol represents an individual animal. Blue, red, and green symbols indicate antibody titers of nonvaccinated animals, baboons vaccinated with 10 9 colony-forming units (CFU) BPZE1, and baboons vaccinated with 10 10 CFU BPZE1, respectively.

    Journal: The Journal of Infectious Diseases

    Article Title: Live Attenuated Pertussis Vaccine BPZE1 Protects Baboons Against Bordetella pertussis Disease and Infection

    doi: 10.1093/infdis/jix254

    Figure Lengend Snippet: Booster effect of Bordetella pertussis D420 challenge in BPZE1-vaccinated baboons. Immunoglobulin G (IgG) ( A ) and immunoglobulin A (IgA) ( B ) titers were measured against filamentous hemagglutinin (FHA) (upper panels), pertussis toxin (PT) (middle panels), and pertactin (Prn) (lower panels) at the indicated time points after challenge with B. pertussis D420. Each symbol represents an individual animal. Blue, red, and green symbols indicate antibody titers of nonvaccinated animals, baboons vaccinated with 10 9 colony-forming units (CFU) BPZE1, and baboons vaccinated with 10 10 CFU BPZE1, respectively.

    Article Snippet: After 6 washes with PBS, 100 µL/well of horseradish peroxidase–conjugated goat antimonkey immunoglobulin G (IgG) (BioRad) or antimonkey immunoglobulin A (IgA) (Sigma-Aldrich), diluted 1:10000 in PBS, was added.

    Techniques:

    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