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GE Healthcare rabbit polyclonal ab
Rabbit Polyclonal Ab, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rabbit polyclonal ab/product/GE Healthcare
Average 92 stars, based on 1 article reviews
Price from $9.99 to $1999.99
rabbit polyclonal ab - by Bioz Stars, 2021-01
92/100 stars

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Produced:

Article Title: Involvement of Rac1 in Activation of Multicomponent Nox1- and Nox3-Based NADPH Oxidases
Article Snippet: .. Rabbit polyclonal Ab was raised against recombinant glutathione S -transferase (GST) fused to full-length mouse Noxa1, produced in Escherichia coli using pGEX-4T1 (Amersham Biosciences). ..

Recombinant:

Article Title: Involvement of Rac1 in Activation of Multicomponent Nox1- and Nox3-Based NADPH Oxidases
Article Snippet: .. Rabbit polyclonal Ab was raised against recombinant glutathione S -transferase (GST) fused to full-length mouse Noxa1, produced in Escherichia coli using pGEX-4T1 (Amersham Biosciences). ..

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    GE Healthcare rabbit anti gii norovirus polyclonal sera
    Predicted <t>GII.4</t> <t>norovirus</t> evolving blockade epitopes. Bioinformatic approaches predicted five antibody epitopes on the surface of GII.4 noroviruses that appeared to be evolving over time and to correlate with the emergence of new GII.4 outbreak strains. Panel A : Amino acid variation of Epitopes A–E by GII.4 strain. Panel B : Predicted epitopes were expanded to include interacting amino acids within 8A. Epitope A (grey), Epitope B (blue), Epitope C (green), Epitope D (black), Epitope E (teal) and HBGA binding sites (magenta) mapped onto the P domain dimer of GII.4.2002.
    Rabbit Anti Gii Norovirus Polyclonal Sera, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti gii norovirus polyclonal sera/product/GE Healthcare
    Average 85 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    rabbit anti gii norovirus polyclonal sera - by Bioz Stars, 2021-01
    85/100 stars
      Buy from Supplier

    85
    GE Healthcare rabbit polyclonal anti pap iii antibody
    N-terminal proteolytic processing of <t>PAP-III</t> in injured sciatic nerves of rats. A , induction of PAP-III mRNA in injured sciatic nerves. Nerves were collected 0 ( cont ), 1, 3, and 7 days ( d ) after axotomy. Expression of PAP-III mRNA was examined by RT-PCR.
    Rabbit Polyclonal Anti Pap Iii Antibody, supplied by GE Healthcare, 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/rabbit polyclonal anti pap iii antibody/product/GE Healthcare
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal anti pap iii antibody - by Bioz Stars, 2021-01
    85/100 stars
      Buy from Supplier

    85
    GE Healthcare anti mcm2 7 ab
    <t>Mcm2-7</t> ATPase motif mutants are defective for in vitro DNA replication. Replication assays were performed with purified wild-type or Mcm2-7 ATPase motif mutant complexes. Radiolabeled DNA replication products were analyzed by alkaline agarose electrophoresis
    Anti Mcm2 7 Ab, supplied by GE Healthcare, 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/anti mcm2 7 ab/product/GE Healthcare
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti mcm2 7 ab - by Bioz Stars, 2021-01
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    Predicted GII.4 norovirus evolving blockade epitopes. Bioinformatic approaches predicted five antibody epitopes on the surface of GII.4 noroviruses that appeared to be evolving over time and to correlate with the emergence of new GII.4 outbreak strains. Panel A : Amino acid variation of Epitopes A–E by GII.4 strain. Panel B : Predicted epitopes were expanded to include interacting amino acids within 8A. Epitope A (grey), Epitope B (blue), Epitope C (green), Epitope D (black), Epitope E (teal) and HBGA binding sites (magenta) mapped onto the P domain dimer of GII.4.2002.

    Journal: PLoS Pathogens

    Article Title: Immunogenetic Mechanisms Driving Norovirus GII.4 Antigenic Variation

    doi: 10.1371/journal.ppat.1002705

    Figure Lengend Snippet: Predicted GII.4 norovirus evolving blockade epitopes. Bioinformatic approaches predicted five antibody epitopes on the surface of GII.4 noroviruses that appeared to be evolving over time and to correlate with the emergence of new GII.4 outbreak strains. Panel A : Amino acid variation of Epitopes A–E by GII.4 strain. Panel B : Predicted epitopes were expanded to include interacting amino acids within 8A. Epitope A (grey), Epitope B (blue), Epitope C (green), Epitope D (black), Epitope E (teal) and HBGA binding sites (magenta) mapped onto the P domain dimer of GII.4.2002.

    Article Snippet: Bound VLP was detected by a rabbit anti-GII norovirus polyclonal sera made from hyperimmunization with either GII.4.2009 or a cocktail of GII.4.1997, GII.3.1999, GII.1.1976, and GII.2.1976 VLPs, followed by anti-rabbit IgG-HRP (GE Healthcare) and color developed with 1-Step Ultra TMB ELISA HRP substrate solution (Thermo-Fisher).

    Techniques: Binding Assay

    Characterization of donor NVB plasma blockade of norovirus VLPs. Panel A : PGM binding blockade activity. Sigmoidal curves were fit to the mean percent control binding calculated by comparing the amount of VLP bound to PGM in the presence of antibody pretreatment to the amount of VLP bound in the absence of antibody pretreatment. Error bars represent the standard error of the mean. Panel B : Mean EC50 (% plasma) for blockade of each VLP. * VLPs with EC50 values significantly different from the EC50 for GII.4.2006.

    Journal: PLoS Pathogens

    Article Title: Immunogenetic Mechanisms Driving Norovirus GII.4 Antigenic Variation

    doi: 10.1371/journal.ppat.1002705

    Figure Lengend Snippet: Characterization of donor NVB plasma blockade of norovirus VLPs. Panel A : PGM binding blockade activity. Sigmoidal curves were fit to the mean percent control binding calculated by comparing the amount of VLP bound to PGM in the presence of antibody pretreatment to the amount of VLP bound in the absence of antibody pretreatment. Error bars represent the standard error of the mean. Panel B : Mean EC50 (% plasma) for blockade of each VLP. * VLPs with EC50 values significantly different from the EC50 for GII.4.2006.

    Article Snippet: Bound VLP was detected by a rabbit anti-GII norovirus polyclonal sera made from hyperimmunization with either GII.4.2009 or a cocktail of GII.4.1997, GII.3.1999, GII.1.1976, and GII.2.1976 VLPs, followed by anti-rabbit IgG-HRP (GE Healthcare) and color developed with 1-Step Ultra TMB ELISA HRP substrate solution (Thermo-Fisher).

    Techniques: Binding Assay, Activity Assay

    Epitope A constitutes ∼40% of the polyclonal blockade antibody response in NoV outbreak human convalescent-phase serum. Convalescent serum samples collected from eight GII.4.2009-infected subjects were assayed for ability to block VLP interaction

    Journal: Journal of Virology

    Article Title: Emergence of a Norovirus GII.4 Strain Correlates with Changes in Evolving Blockade Epitopes

    doi: 10.1128/JVI.03106-12

    Figure Lengend Snippet: Epitope A constitutes ∼40% of the polyclonal blockade antibody response in NoV outbreak human convalescent-phase serum. Convalescent serum samples collected from eight GII.4.2009-infected subjects were assayed for ability to block VLP interaction

    Article Snippet: VLPs (0.5 μg/ml) were pretreated with decreasing concentrations of test MAb or outbreak sera for 1 h at room temperature before being added to the carbohydrate ligand-coated plates for 1 h. Bound VLP were detected by a rabbit anti-GII norovirus polyclonal sera made from hyperimmunization with either GII.4.2009 or a cocktail of GII.4.1997, GII.3.1999, GII.1.1976, and GII.2.1976 VLPs, followed by anti-rabbit IgG-HRP (GE Healthcare) and color developed with 1-Step Ultra TMB ELISA HRP substrate solution (Thermo Fisher).

    Techniques: Infection, Blocking Assay

    N-terminal proteolytic processing of PAP-III in injured sciatic nerves of rats. A , induction of PAP-III mRNA in injured sciatic nerves. Nerves were collected 0 ( cont ), 1, 3, and 7 days ( d ) after axotomy. Expression of PAP-III mRNA was examined by RT-PCR.

    Journal: The Journal of Biological Chemistry

    Article Title: N-terminal Cleaved Pancreatitis-associated Protein-III (PAP-III) Serves as a Scaffold for Neurites and Promotes Neurite Outgrowth *

    doi: 10.1074/jbc.M112.395301

    Figure Lengend Snippet: N-terminal proteolytic processing of PAP-III in injured sciatic nerves of rats. A , induction of PAP-III mRNA in injured sciatic nerves. Nerves were collected 0 ( cont ), 1, 3, and 7 days ( d ) after axotomy. Expression of PAP-III mRNA was examined by RT-PCR.

    Article Snippet: The membrane was probed with a mouse monoclonal anti-GAPDH antibody (4300; Ambion, Huntingdon, UK) or a rabbit polyclonal anti-PAP-III antibody produced in our previous study and then with horseradish peroxidase-conjugated secondary antibodies (GE Healthcare) ( ).

    Techniques: Expressing, Reverse Transcription Polymerase Chain Reaction

    Weak interactions of exogenously added ΔN-PAP-III fibers with glial cells. ΔN-PAP-III fibers produced in 25 m m Tris (pH 7.5) containing 150 m m NaCl were added to the culture media of astrocytes, microglia, and Schwann cells, and incubated

    Journal: The Journal of Biological Chemistry

    Article Title: N-terminal Cleaved Pancreatitis-associated Protein-III (PAP-III) Serves as a Scaffold for Neurites and Promotes Neurite Outgrowth *

    doi: 10.1074/jbc.M112.395301

    Figure Lengend Snippet: Weak interactions of exogenously added ΔN-PAP-III fibers with glial cells. ΔN-PAP-III fibers produced in 25 m m Tris (pH 7.5) containing 150 m m NaCl were added to the culture media of astrocytes, microglia, and Schwann cells, and incubated

    Article Snippet: The membrane was probed with a mouse monoclonal anti-GAPDH antibody (4300; Ambion, Huntingdon, UK) or a rabbit polyclonal anti-PAP-III antibody produced in our previous study and then with horseradish peroxidase-conjugated secondary antibodies (GE Healthcare) ( ).

    Techniques: Produced, Incubation

    Association of exogenously added ΔN-PAP-III fibers with neurons. ΔN-PAP-III fibers produced in 25 m m Tris (pH 7.5) containing 150 m m NaCl were added to the culture media of primary cortical neurons precultured for 12–18 h. Twenty-four

    Journal: The Journal of Biological Chemistry

    Article Title: N-terminal Cleaved Pancreatitis-associated Protein-III (PAP-III) Serves as a Scaffold for Neurites and Promotes Neurite Outgrowth *

    doi: 10.1074/jbc.M112.395301

    Figure Lengend Snippet: Association of exogenously added ΔN-PAP-III fibers with neurons. ΔN-PAP-III fibers produced in 25 m m Tris (pH 7.5) containing 150 m m NaCl were added to the culture media of primary cortical neurons precultured for 12–18 h. Twenty-four

    Article Snippet: The membrane was probed with a mouse monoclonal anti-GAPDH antibody (4300; Ambion, Huntingdon, UK) or a rabbit polyclonal anti-PAP-III antibody produced in our previous study and then with horseradish peroxidase-conjugated secondary antibodies (GE Healthcare) ( ).

    Techniques: Produced

    Precipitability of ΔN-PAP-III depends on Na + concentrations. A , PAP-III protein was incubated with (+) or without (−) trypsin in 25 m m Tris (pH 7.5) containing 0 (−), 25, and 150 m m NaCl for 2 h ( hrs ). B , PAP-III protein was treated

    Journal: The Journal of Biological Chemistry

    Article Title: N-terminal Cleaved Pancreatitis-associated Protein-III (PAP-III) Serves as a Scaffold for Neurites and Promotes Neurite Outgrowth *

    doi: 10.1074/jbc.M112.395301

    Figure Lengend Snippet: Precipitability of ΔN-PAP-III depends on Na + concentrations. A , PAP-III protein was incubated with (+) or without (−) trypsin in 25 m m Tris (pH 7.5) containing 0 (−), 25, and 150 m m NaCl for 2 h ( hrs ). B , PAP-III protein was treated

    Article Snippet: The membrane was probed with a mouse monoclonal anti-GAPDH antibody (4300; Ambion, Huntingdon, UK) or a rabbit polyclonal anti-PAP-III antibody produced in our previous study and then with horseradish peroxidase-conjugated secondary antibodies (GE Healthcare) ( ).

    Techniques: Incubation

    No significant effects of exogenously added full-length PAP-III or PAP-III (N) on neurite extension. Primary cortical neurons were seeded on PDL-coated glass coverslips and cultured for 36 h in media containing no PAP-III ( control ), full-length PAP-III,

    Journal: The Journal of Biological Chemistry

    Article Title: N-terminal Cleaved Pancreatitis-associated Protein-III (PAP-III) Serves as a Scaffold for Neurites and Promotes Neurite Outgrowth *

    doi: 10.1074/jbc.M112.395301

    Figure Lengend Snippet: No significant effects of exogenously added full-length PAP-III or PAP-III (N) on neurite extension. Primary cortical neurons were seeded on PDL-coated glass coverslips and cultured for 36 h in media containing no PAP-III ( control ), full-length PAP-III,

    Article Snippet: The membrane was probed with a mouse monoclonal anti-GAPDH antibody (4300; Ambion, Huntingdon, UK) or a rabbit polyclonal anti-PAP-III antibody produced in our previous study and then with horseradish peroxidase-conjugated secondary antibodies (GE Healthcare) ( ).

    Techniques: Cell Culture

    Neurite extension on ΔN-PAP-III fibers immobilized on glass coverslips. Dense matrices of ΔN-PAP-III fibers were prepared on PDL-coated glass coverslips by digesting ΔN-PAP-III without NaCl. Primary cortical neurons were seeded

    Journal: The Journal of Biological Chemistry

    Article Title: N-terminal Cleaved Pancreatitis-associated Protein-III (PAP-III) Serves as a Scaffold for Neurites and Promotes Neurite Outgrowth *

    doi: 10.1074/jbc.M112.395301

    Figure Lengend Snippet: Neurite extension on ΔN-PAP-III fibers immobilized on glass coverslips. Dense matrices of ΔN-PAP-III fibers were prepared on PDL-coated glass coverslips by digesting ΔN-PAP-III without NaCl. Primary cortical neurons were seeded

    Article Snippet: The membrane was probed with a mouse monoclonal anti-GAPDH antibody (4300; Ambion, Huntingdon, UK) or a rabbit polyclonal anti-PAP-III antibody produced in our previous study and then with horseradish peroxidase-conjugated secondary antibodies (GE Healthcare) ( ).

    Techniques:

    Fibrillar structure of ΔN-PAP-III. A , PAP-III treated with trypsin in 25 m m Tris (pH 7.5) containing 0 (−), 25, and 150 m m NaCl was attached to PDL-coated coverslips and visualized by immunofluorescence using anti-PAP-III antibody. Scale

    Journal: The Journal of Biological Chemistry

    Article Title: N-terminal Cleaved Pancreatitis-associated Protein-III (PAP-III) Serves as a Scaffold for Neurites and Promotes Neurite Outgrowth *

    doi: 10.1074/jbc.M112.395301

    Figure Lengend Snippet: Fibrillar structure of ΔN-PAP-III. A , PAP-III treated with trypsin in 25 m m Tris (pH 7.5) containing 0 (−), 25, and 150 m m NaCl was attached to PDL-coated coverslips and visualized by immunofluorescence using anti-PAP-III antibody. Scale

    Article Snippet: The membrane was probed with a mouse monoclonal anti-GAPDH antibody (4300; Ambion, Huntingdon, UK) or a rabbit polyclonal anti-PAP-III antibody produced in our previous study and then with horseradish peroxidase-conjugated secondary antibodies (GE Healthcare) ( ).

    Techniques: Immunofluorescence

    Mcm2-7 ATPase motif mutants are defective for in vitro DNA replication. Replication assays were performed with purified wild-type or Mcm2-7 ATPase motif mutant complexes. Radiolabeled DNA replication products were analyzed by alkaline agarose electrophoresis

    Journal: Molecular cell

    Article Title: Multiple Functions for Mcm2-7 ATPase Motifs During Replication Initiation

    doi: 10.1016/j.molcel.2014.06.033

    Figure Lengend Snippet: Mcm2-7 ATPase motif mutants are defective for in vitro DNA replication. Replication assays were performed with purified wild-type or Mcm2-7 ATPase motif mutant complexes. Radiolabeled DNA replication products were analyzed by alkaline agarose electrophoresis

    Article Snippet: Eluted proteins were incubated with 30 µl anti-Mcm2-7 Ab (UM174, rabbit polyclonal) bound to Gammabind G Sepharose (GE) in 400 µl Buffer H containing 0.3 M KGlu for 90 minutes.

    Techniques: In Vitro, Purification, Mutagenesis, Electrophoresis

    Initial association of ATPase motif mutant Mcm2-7/Cdt1 complexes. Helicaseloading assays were performed in the presence of ATPγS followed by a low-salt wash allowing detection of the initial DNA association of Mcm2-7 and helicase loading proteins

    Journal: Molecular cell

    Article Title: Multiple Functions for Mcm2-7 ATPase Motifs During Replication Initiation

    doi: 10.1016/j.molcel.2014.06.033

    Figure Lengend Snippet: Initial association of ATPase motif mutant Mcm2-7/Cdt1 complexes. Helicaseloading assays were performed in the presence of ATPγS followed by a low-salt wash allowing detection of the initial DNA association of Mcm2-7 and helicase loading proteins

    Article Snippet: Eluted proteins were incubated with 30 µl anti-Mcm2-7 Ab (UM174, rabbit polyclonal) bound to Gammabind G Sepharose (GE) in 400 µl Buffer H containing 0.3 M KGlu for 90 minutes.

    Techniques: Mutagenesis

    Loaded Mcm2-7 ATPase motif mutants form double hexamers that are DDK substrates. (A) Double hexamer formation by ATPase motif mutant Mcm2-7 complexes. After a helicase-loading reaction and high-salt wash, loaded wild-type or mutant Mcm2-7 complexes were

    Journal: Molecular cell

    Article Title: Multiple Functions for Mcm2-7 ATPase Motifs During Replication Initiation

    doi: 10.1016/j.molcel.2014.06.033

    Figure Lengend Snippet: Loaded Mcm2-7 ATPase motif mutants form double hexamers that are DDK substrates. (A) Double hexamer formation by ATPase motif mutant Mcm2-7 complexes. After a helicase-loading reaction and high-salt wash, loaded wild-type or mutant Mcm2-7 complexes were

    Article Snippet: Eluted proteins were incubated with 30 µl anti-Mcm2-7 Ab (UM174, rabbit polyclonal) bound to Gammabind G Sepharose (GE) in 400 µl Buffer H containing 0.3 M KGlu for 90 minutes.

    Techniques: Mutagenesis

    Mcm2-7 ATPase motif mutants exhibit defects in multiple steps during helicase activation. (A) Mcm2-7 ATPase mutants are defective in DNA retention during helicase activation. The amount of the indicated Mcm2-7 complexes (Flag-Mcm3) retained on DNA was

    Journal: Molecular cell

    Article Title: Multiple Functions for Mcm2-7 ATPase Motifs During Replication Initiation

    doi: 10.1016/j.molcel.2014.06.033

    Figure Lengend Snippet: Mcm2-7 ATPase motif mutants exhibit defects in multiple steps during helicase activation. (A) Mcm2-7 ATPase mutants are defective in DNA retention during helicase activation. The amount of the indicated Mcm2-7 complexes (Flag-Mcm3) retained on DNA was

    Article Snippet: Eluted proteins were incubated with 30 µl anti-Mcm2-7 Ab (UM174, rabbit polyclonal) bound to Gammabind G Sepharose (GE) in 400 µl Buffer H containing 0.3 M KGlu for 90 minutes.

    Techniques: Activation Assay

    Mcm2-7 ATPase motif mutants are defective in helicase loading. (A) Helicase loading of MCM ATPase motif mutants was monitored by incubating loading proteins with ATP and origin-DNA-beads followed by a high-salt wash. The associated graph shows the relative

    Journal: Molecular cell

    Article Title: Multiple Functions for Mcm2-7 ATPase Motifs During Replication Initiation

    doi: 10.1016/j.molcel.2014.06.033

    Figure Lengend Snippet: Mcm2-7 ATPase motif mutants are defective in helicase loading. (A) Helicase loading of MCM ATPase motif mutants was monitored by incubating loading proteins with ATP and origin-DNA-beads followed by a high-salt wash. The associated graph shows the relative

    Article Snippet: Eluted proteins were incubated with 30 µl anti-Mcm2-7 Ab (UM174, rabbit polyclonal) bound to Gammabind G Sepharose (GE) in 400 µl Buffer H containing 0.3 M KGlu for 90 minutes.

    Techniques: