igg fc  (Millipore)


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    Name:
    Anti Human IgG Fc specific antibody
    Description:
    IgG contains four polypeptide chains made of two identical 50 kDa γ heavy H chains and two identical 25 kDa κ or λ light L chains that are associated by inter chain disulfide bonds IgG contains four isotypes IgG1 IgG2 IgG3 and IgG4
    Catalog Number:
    i9135
    Price:
    None
    Applications:
    Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.Immunohistochemistry (1 paper)
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    Structured Review

    Millipore igg fc
    Immunoblot analyses of the Ig-binding capability of recombinant T. pallidum Gpd. Shown are inclusion bodies purified from E. coli BL21 (DE3) pLysS transformed with either the pET-3a-Gpd construct (lanes 1, 3, 5, and 7) or with the pET-3a vector alone (lanes 2, 4, 6, and 8). Molecular mass standards in kilodaltons are indicated on the left of each panel. (A) Specificity of recombinant T. pallidum Gpd for binding various Ig classes. Lanes: 1 and 2, human <t>IgA</t> and goat F(ab′) 2 anti-human IgA (alpha chain specific); 3 and 4, human IgD and goat F(ab′) 2 anti-human IgD (delta chain specific); 5 and 6, human <t>IgG</t> and goat F(ab′) 2 anti-human IgG (gamma chain specific); 7 and 8, human IgM and goat F(ab′) 2 anti-human IgM (mu chain specific). (B) Investigation of the binding specificity of recombinant T. pallidum Gpd for human IgG. In all cases the secondary antibody used was goat F(ab′) 2 anti-human IgG (gamma chain specific). Lanes: 1 and 2, intact human IgG; 3 and 4, human IgG Fc fragment; 5 and 6, human IgG Fab fragment; 7 and 8, no primary Ig.
    IgG contains four polypeptide chains made of two identical 50 kDa γ heavy H chains and two identical 25 kDa κ or λ light L chains that are associated by inter chain disulfide bonds IgG contains four isotypes IgG1 IgG2 IgG3 and IgG4
    https://www.bioz.com/result/igg fc/product/Millipore
    Average 99 stars, based on 504 article reviews
    Price from $9.99 to $1999.99
    igg fc - by Bioz Stars, 2021-01
    99/100 stars

    Images

    1) Product Images from "Function and Protective Capacity of Treponema pallidum subsp. pallidum Glycerophosphodiester Phosphodiesterase"

    Article Title: Function and Protective Capacity of Treponema pallidum subsp. pallidum Glycerophosphodiester Phosphodiesterase

    Journal: Infection and Immunity

    doi:

    Immunoblot analyses of the Ig-binding capability of recombinant T. pallidum Gpd. Shown are inclusion bodies purified from E. coli BL21 (DE3) pLysS transformed with either the pET-3a-Gpd construct (lanes 1, 3, 5, and 7) or with the pET-3a vector alone (lanes 2, 4, 6, and 8). Molecular mass standards in kilodaltons are indicated on the left of each panel. (A) Specificity of recombinant T. pallidum Gpd for binding various Ig classes. Lanes: 1 and 2, human IgA and goat F(ab′) 2 anti-human IgA (alpha chain specific); 3 and 4, human IgD and goat F(ab′) 2 anti-human IgD (delta chain specific); 5 and 6, human IgG and goat F(ab′) 2 anti-human IgG (gamma chain specific); 7 and 8, human IgM and goat F(ab′) 2 anti-human IgM (mu chain specific). (B) Investigation of the binding specificity of recombinant T. pallidum Gpd for human IgG. In all cases the secondary antibody used was goat F(ab′) 2 anti-human IgG (gamma chain specific). Lanes: 1 and 2, intact human IgG; 3 and 4, human IgG Fc fragment; 5 and 6, human IgG Fab fragment; 7 and 8, no primary Ig.
    Figure Legend Snippet: Immunoblot analyses of the Ig-binding capability of recombinant T. pallidum Gpd. Shown are inclusion bodies purified from E. coli BL21 (DE3) pLysS transformed with either the pET-3a-Gpd construct (lanes 1, 3, 5, and 7) or with the pET-3a vector alone (lanes 2, 4, 6, and 8). Molecular mass standards in kilodaltons are indicated on the left of each panel. (A) Specificity of recombinant T. pallidum Gpd for binding various Ig classes. Lanes: 1 and 2, human IgA and goat F(ab′) 2 anti-human IgA (alpha chain specific); 3 and 4, human IgD and goat F(ab′) 2 anti-human IgD (delta chain specific); 5 and 6, human IgG and goat F(ab′) 2 anti-human IgG (gamma chain specific); 7 and 8, human IgM and goat F(ab′) 2 anti-human IgM (mu chain specific). (B) Investigation of the binding specificity of recombinant T. pallidum Gpd for human IgG. In all cases the secondary antibody used was goat F(ab′) 2 anti-human IgG (gamma chain specific). Lanes: 1 and 2, intact human IgG; 3 and 4, human IgG Fc fragment; 5 and 6, human IgG Fab fragment; 7 and 8, no primary Ig.

    Techniques Used: Binding Assay, Recombinant, Purification, Transformation Assay, Positron Emission Tomography, Construct, Plasmid Preparation

    2) Product Images from "Function and Protective Capacity of Treponema pallidum subsp. pallidum Glycerophosphodiester Phosphodiesterase"

    Article Title: Function and Protective Capacity of Treponema pallidum subsp. pallidum Glycerophosphodiester Phosphodiesterase

    Journal: Infection and Immunity

    doi:

    Immunoblot analyses of the Ig-binding capability of recombinant T. pallidum Gpd. Shown are inclusion bodies purified from E. coli BL21 (DE3) pLysS transformed with either the pET-3a-Gpd construct (lanes 1, 3, 5, and 7) or with the pET-3a vector alone (lanes 2, 4, 6, and 8). Molecular mass standards in kilodaltons are indicated on the left of each panel. (A) Specificity of recombinant T. pallidum Gpd for binding various Ig classes. Lanes: 1 and 2, human IgA and goat F(ab′) 2 anti-human IgA (alpha chain specific); 3 and 4, human IgD and goat F(ab′) 2 anti-human IgD (delta chain specific); 5 and 6, human IgG and goat F(ab′) 2 anti-human IgG (gamma chain specific); 7 and 8, human IgM and goat F(ab′) 2 anti-human IgM (mu chain specific). (B) Investigation of the binding specificity of recombinant T. pallidum Gpd for human IgG. In all cases the secondary antibody used was goat F(ab′) 2 anti-human IgG (gamma chain specific). Lanes: 1 and 2, intact human IgG; 3 and 4, human IgG Fc fragment; 5 and 6, human IgG Fab fragment; 7 and 8, no primary Ig.
    Figure Legend Snippet: Immunoblot analyses of the Ig-binding capability of recombinant T. pallidum Gpd. Shown are inclusion bodies purified from E. coli BL21 (DE3) pLysS transformed with either the pET-3a-Gpd construct (lanes 1, 3, 5, and 7) or with the pET-3a vector alone (lanes 2, 4, 6, and 8). Molecular mass standards in kilodaltons are indicated on the left of each panel. (A) Specificity of recombinant T. pallidum Gpd for binding various Ig classes. Lanes: 1 and 2, human IgA and goat F(ab′) 2 anti-human IgA (alpha chain specific); 3 and 4, human IgD and goat F(ab′) 2 anti-human IgD (delta chain specific); 5 and 6, human IgG and goat F(ab′) 2 anti-human IgG (gamma chain specific); 7 and 8, human IgM and goat F(ab′) 2 anti-human IgM (mu chain specific). (B) Investigation of the binding specificity of recombinant T. pallidum Gpd for human IgG. In all cases the secondary antibody used was goat F(ab′) 2 anti-human IgG (gamma chain specific). Lanes: 1 and 2, intact human IgG; 3 and 4, human IgG Fc fragment; 5 and 6, human IgG Fab fragment; 7 and 8, no primary Ig.

    Techniques Used: Binding Assay, Recombinant, Purification, Transformation Assay, Positron Emission Tomography, Construct, Plasmid Preparation

    3) Product Images from "Function and Protective Capacity of Treponema pallidum subsp. pallidum Glycerophosphodiester Phosphodiesterase"

    Article Title: Function and Protective Capacity of Treponema pallidum subsp. pallidum Glycerophosphodiester Phosphodiesterase

    Journal: Infection and Immunity

    doi:

    Immunoblot analyses of the Ig-binding capability of recombinant T. pallidum Gpd. Shown are inclusion bodies purified from E. coli BL21 (DE3) pLysS transformed with either the pET-3a-Gpd construct (lanes 1, 3, 5, and 7) or with the pET-3a vector alone (lanes 2, 4, 6, and 8). Molecular mass standards in kilodaltons are indicated on the left of each panel. (A) Specificity of recombinant T. pallidum Gpd for binding various Ig classes. Lanes: 1 and 2, human IgA and goat F(ab′) 2 anti-human IgA (alpha chain specific); 3 and 4, human IgD and goat F(ab′) 2 anti-human IgD (delta chain specific); 5 and 6, human IgG and goat F(ab′) 2 anti-human IgG (gamma chain specific); 7 and 8, human IgM and goat F(ab′) 2 anti-human IgM (mu chain specific). (B) Investigation of the binding specificity of recombinant T. pallidum Gpd for human IgG. In all cases the secondary antibody used was goat F(ab′) 2 anti-human IgG (gamma chain specific). Lanes: 1 and 2, intact human IgG; 3 and 4, human IgG Fc fragment; 5 and 6, human IgG Fab fragment; 7 and 8, no primary Ig.
    Figure Legend Snippet: Immunoblot analyses of the Ig-binding capability of recombinant T. pallidum Gpd. Shown are inclusion bodies purified from E. coli BL21 (DE3) pLysS transformed with either the pET-3a-Gpd construct (lanes 1, 3, 5, and 7) or with the pET-3a vector alone (lanes 2, 4, 6, and 8). Molecular mass standards in kilodaltons are indicated on the left of each panel. (A) Specificity of recombinant T. pallidum Gpd for binding various Ig classes. Lanes: 1 and 2, human IgA and goat F(ab′) 2 anti-human IgA (alpha chain specific); 3 and 4, human IgD and goat F(ab′) 2 anti-human IgD (delta chain specific); 5 and 6, human IgG and goat F(ab′) 2 anti-human IgG (gamma chain specific); 7 and 8, human IgM and goat F(ab′) 2 anti-human IgM (mu chain specific). (B) Investigation of the binding specificity of recombinant T. pallidum Gpd for human IgG. In all cases the secondary antibody used was goat F(ab′) 2 anti-human IgG (gamma chain specific). Lanes: 1 and 2, intact human IgG; 3 and 4, human IgG Fc fragment; 5 and 6, human IgG Fab fragment; 7 and 8, no primary Ig.

    Techniques Used: Binding Assay, Recombinant, Purification, Transformation Assay, Positron Emission Tomography, Construct, Plasmid Preparation

    4) Product Images from "Function and Protective Capacity of Treponema pallidum subsp. pallidum Glycerophosphodiester Phosphodiesterase"

    Article Title: Function and Protective Capacity of Treponema pallidum subsp. pallidum Glycerophosphodiester Phosphodiesterase

    Journal: Infection and Immunity

    doi:

    Immunoblot analyses of the Ig-binding capability of recombinant T. pallidum Gpd. Shown are inclusion bodies purified from E. coli BL21 (DE3) pLysS transformed with either the pET-3a-Gpd construct (lanes 1, 3, 5, and 7) or with the pET-3a vector alone (lanes 2, 4, 6, and 8). Molecular mass standards in kilodaltons are indicated on the left of each panel. (A) Specificity of recombinant T. pallidum Gpd for binding various Ig classes. Lanes: 1 and 2, human IgA and goat F(ab′) 2 anti-human IgA (alpha chain specific); 3 and 4, human IgD and goat F(ab′) 2 anti-human IgD (delta chain specific); 5 and 6, human IgG and goat F(ab′) 2 anti-human IgG (gamma chain specific); 7 and 8, human IgM and goat F(ab′) 2 anti-human IgM (mu chain specific). (B) Investigation of the binding specificity of recombinant T. pallidum Gpd for human IgG. In all cases the secondary antibody used was goat F(ab′) 2 anti-human IgG (gamma chain specific). Lanes: 1 and 2, intact human IgG; 3 and 4, human IgG Fc fragment; 5 and 6, human IgG Fab fragment; 7 and 8, no primary Ig.
    Figure Legend Snippet: Immunoblot analyses of the Ig-binding capability of recombinant T. pallidum Gpd. Shown are inclusion bodies purified from E. coli BL21 (DE3) pLysS transformed with either the pET-3a-Gpd construct (lanes 1, 3, 5, and 7) or with the pET-3a vector alone (lanes 2, 4, 6, and 8). Molecular mass standards in kilodaltons are indicated on the left of each panel. (A) Specificity of recombinant T. pallidum Gpd for binding various Ig classes. Lanes: 1 and 2, human IgA and goat F(ab′) 2 anti-human IgA (alpha chain specific); 3 and 4, human IgD and goat F(ab′) 2 anti-human IgD (delta chain specific); 5 and 6, human IgG and goat F(ab′) 2 anti-human IgG (gamma chain specific); 7 and 8, human IgM and goat F(ab′) 2 anti-human IgM (mu chain specific). (B) Investigation of the binding specificity of recombinant T. pallidum Gpd for human IgG. In all cases the secondary antibody used was goat F(ab′) 2 anti-human IgG (gamma chain specific). Lanes: 1 and 2, intact human IgG; 3 and 4, human IgG Fc fragment; 5 and 6, human IgG Fab fragment; 7 and 8, no primary Ig.

    Techniques Used: Binding Assay, Recombinant, Purification, Transformation Assay, Positron Emission Tomography, Construct, Plasmid Preparation

    5) Product Images from "Function and Protective Capacity of Treponema pallidum subsp. pallidum Glycerophosphodiester Phosphodiesterase"

    Article Title: Function and Protective Capacity of Treponema pallidum subsp. pallidum Glycerophosphodiester Phosphodiesterase

    Journal: Infection and Immunity

    doi:

    Immunoblot analyses of the Ig-binding capability of recombinant T. pallidum Gpd. Shown are inclusion bodies purified from E. coli BL21 (DE3) pLysS transformed with either the pET-3a-Gpd construct (lanes 1, 3, 5, and 7) or with the pET-3a vector alone (lanes 2, 4, 6, and 8). Molecular mass standards in kilodaltons are indicated on the left of each panel. (A) Specificity of recombinant T. pallidum Gpd for binding various Ig classes. Lanes: 1 and 2, human IgA and goat F(ab′) 2 anti-human IgA (alpha chain specific); 3 and 4, human IgD and goat F(ab′) 2 anti-human IgD (delta chain specific); 5 and 6, human IgG and goat F(ab′) 2 anti-human IgG (gamma chain specific); 7 and 8, human IgM and goat F(ab′) 2 anti-human IgM (mu chain specific). (B) Investigation of the binding specificity of recombinant T. pallidum Gpd for human IgG. In all cases the secondary antibody used was goat F(ab′) 2 anti-human IgG (gamma chain specific). Lanes: 1 and 2, intact human IgG; 3 and 4, human IgG Fc fragment; 5 and 6, human IgG Fab fragment; 7 and 8, no primary Ig.
    Figure Legend Snippet: Immunoblot analyses of the Ig-binding capability of recombinant T. pallidum Gpd. Shown are inclusion bodies purified from E. coli BL21 (DE3) pLysS transformed with either the pET-3a-Gpd construct (lanes 1, 3, 5, and 7) or with the pET-3a vector alone (lanes 2, 4, 6, and 8). Molecular mass standards in kilodaltons are indicated on the left of each panel. (A) Specificity of recombinant T. pallidum Gpd for binding various Ig classes. Lanes: 1 and 2, human IgA and goat F(ab′) 2 anti-human IgA (alpha chain specific); 3 and 4, human IgD and goat F(ab′) 2 anti-human IgD (delta chain specific); 5 and 6, human IgG and goat F(ab′) 2 anti-human IgG (gamma chain specific); 7 and 8, human IgM and goat F(ab′) 2 anti-human IgM (mu chain specific). (B) Investigation of the binding specificity of recombinant T. pallidum Gpd for human IgG. In all cases the secondary antibody used was goat F(ab′) 2 anti-human IgG (gamma chain specific). Lanes: 1 and 2, intact human IgG; 3 and 4, human IgG Fc fragment; 5 and 6, human IgG Fab fragment; 7 and 8, no primary Ig.

    Techniques Used: Binding Assay, Recombinant, Purification, Transformation Assay, Positron Emission Tomography, Construct, Plasmid Preparation

    Related Articles

    Amplification:

    Article Title: A canine chimeric monoclonal antibody targeting PD-L1 and its clinical efficacy in canine oral malignant melanoma or undifferentiated sarcoma
    Article Snippet: .. Blocking assay for PD-1/PD-L1 or CD80/PD-L1 binding For the preparation of recombinant canine CD80 protein fused to rabbit IgG Fc (cCD80-Ig), the nucleotide sequence encoding the putative extracellular region of cCD80 was amplified by polymerase chain reaction (PCR) using cDNA obtained from beagle PBMCs stimulated with phorbol 12-myristate 13-acetate (20 ng/mL, Sigma-Aldrich, St. Louis, MO, USA) and ionomycin (1 μg/mL, Sigma-Aldrich) and the gene-specific primers (5′-CGC GGA TAT CAT GGA TTA CAC AGC GAA GTG-3′ and 5′-CGG GGT ACC CCA GAG CTG TTG CTG GTT AT-3′). .. The amplicon was then cloned into the multicloning site of the pCXN-2.1–rabbit IgG Fc vector (kindly provided by Dr T. Yokomizo, Juntendo University; modified) , using EcoRV and KpnI restriction enzyme sites.

    Concentration Assay:

    Article Title: Function and Protective Capacity of Treponema pallidum subsp. pallidum Glycerophosphodiester Phosphodiesterase
    Article Snippet: .. Primary Igs were used at a concentration of 1 μg/ml and included human IgA (Sigma), IgD (The Binding Site, Birmingham, United Kingdom), intact IgG (Sigma), IgG Fc and Fab fragments, and IgM (Sigma). .. Corresponding horseradish peroxidase-conjugated secondary antibodies (Sigma) were used at a concentration of 0.2 μg/ml and included goat F(ab′)2 anti-human IgA (alpha chain specific), goat F(ab′)2 anti-human IgD (delta chain specific), goat F(ab′)2 anti-human IgG (gamma chain specific) and goat F(ab′)2 anti-human IgM (mu chain specific).

    Blocking Assay:

    Article Title: A canine chimeric monoclonal antibody targeting PD-L1 and its clinical efficacy in canine oral malignant melanoma or undifferentiated sarcoma
    Article Snippet: .. Blocking assay for PD-1/PD-L1 or CD80/PD-L1 binding For the preparation of recombinant canine CD80 protein fused to rabbit IgG Fc (cCD80-Ig), the nucleotide sequence encoding the putative extracellular region of cCD80 was amplified by polymerase chain reaction (PCR) using cDNA obtained from beagle PBMCs stimulated with phorbol 12-myristate 13-acetate (20 ng/mL, Sigma-Aldrich, St. Louis, MO, USA) and ionomycin (1 μg/mL, Sigma-Aldrich) and the gene-specific primers (5′-CGC GGA TAT CAT GGA TTA CAC AGC GAA GTG-3′ and 5′-CGG GGT ACC CCA GAG CTG TTG CTG GTT AT-3′). .. The amplicon was then cloned into the multicloning site of the pCXN-2.1–rabbit IgG Fc vector (kindly provided by Dr T. Yokomizo, Juntendo University; modified) , using EcoRV and KpnI restriction enzyme sites.

    Sequencing:

    Article Title: A canine chimeric monoclonal antibody targeting PD-L1 and its clinical efficacy in canine oral malignant melanoma or undifferentiated sarcoma
    Article Snippet: .. Blocking assay for PD-1/PD-L1 or CD80/PD-L1 binding For the preparation of recombinant canine CD80 protein fused to rabbit IgG Fc (cCD80-Ig), the nucleotide sequence encoding the putative extracellular region of cCD80 was amplified by polymerase chain reaction (PCR) using cDNA obtained from beagle PBMCs stimulated with phorbol 12-myristate 13-acetate (20 ng/mL, Sigma-Aldrich, St. Louis, MO, USA) and ionomycin (1 μg/mL, Sigma-Aldrich) and the gene-specific primers (5′-CGC GGA TAT CAT GGA TTA CAC AGC GAA GTG-3′ and 5′-CGG GGT ACC CCA GAG CTG TTG CTG GTT AT-3′). .. The amplicon was then cloned into the multicloning site of the pCXN-2.1–rabbit IgG Fc vector (kindly provided by Dr T. Yokomizo, Juntendo University; modified) , using EcoRV and KpnI restriction enzyme sites.

    CTG Assay:

    Article Title: A canine chimeric monoclonal antibody targeting PD-L1 and its clinical efficacy in canine oral malignant melanoma or undifferentiated sarcoma
    Article Snippet: .. Blocking assay for PD-1/PD-L1 or CD80/PD-L1 binding For the preparation of recombinant canine CD80 protein fused to rabbit IgG Fc (cCD80-Ig), the nucleotide sequence encoding the putative extracellular region of cCD80 was amplified by polymerase chain reaction (PCR) using cDNA obtained from beagle PBMCs stimulated with phorbol 12-myristate 13-acetate (20 ng/mL, Sigma-Aldrich, St. Louis, MO, USA) and ionomycin (1 μg/mL, Sigma-Aldrich) and the gene-specific primers (5′-CGC GGA TAT CAT GGA TTA CAC AGC GAA GTG-3′ and 5′-CGG GGT ACC CCA GAG CTG TTG CTG GTT AT-3′). .. The amplicon was then cloned into the multicloning site of the pCXN-2.1–rabbit IgG Fc vector (kindly provided by Dr T. Yokomizo, Juntendo University; modified) , using EcoRV and KpnI restriction enzyme sites.

    Incubation:

    Article Title: The deubiquitylase Ubp15 couples transcription to mRNA export
    Article Snippet: .. The cleared extract was incubated for 1 hr at 4 °C with 200 µL of pre-washed magnetic Dynabeads M-270 Epoxy (Thermo Fisher Scientific) conjugated to rabbit IgG (Sigma). ..

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    Article Snippet: .. The neurons were incubated in the presence of human IgG-Fc or sAPPα at the indicated concentrations (1.22, 2.44, or 4.88 nM) and/or 200 nM KT5720 (420320, Calbiochem, San Diego, CA, USA) for 24 h. The neurons were then fixed in 4% PFA, and immunostained with polyclonal anti-TuJ1 antibody (1∶1000; PRB-435P, Covance). .. The lengths of the longest neurites were measured by ImageJ software (National Institutes of Health, Bethesda, MD, USA).

    Polymerase Chain Reaction:

    Article Title: A canine chimeric monoclonal antibody targeting PD-L1 and its clinical efficacy in canine oral malignant melanoma or undifferentiated sarcoma
    Article Snippet: .. Blocking assay for PD-1/PD-L1 or CD80/PD-L1 binding For the preparation of recombinant canine CD80 protein fused to rabbit IgG Fc (cCD80-Ig), the nucleotide sequence encoding the putative extracellular region of cCD80 was amplified by polymerase chain reaction (PCR) using cDNA obtained from beagle PBMCs stimulated with phorbol 12-myristate 13-acetate (20 ng/mL, Sigma-Aldrich, St. Louis, MO, USA) and ionomycin (1 μg/mL, Sigma-Aldrich) and the gene-specific primers (5′-CGC GGA TAT CAT GGA TTA CAC AGC GAA GTG-3′ and 5′-CGG GGT ACC CCA GAG CTG TTG CTG GTT AT-3′). .. The amplicon was then cloned into the multicloning site of the pCXN-2.1–rabbit IgG Fc vector (kindly provided by Dr T. Yokomizo, Juntendo University; modified) , using EcoRV and KpnI restriction enzyme sites.

    Recombinant:

    Article Title: A canine chimeric monoclonal antibody targeting PD-L1 and its clinical efficacy in canine oral malignant melanoma or undifferentiated sarcoma
    Article Snippet: .. Blocking assay for PD-1/PD-L1 or CD80/PD-L1 binding For the preparation of recombinant canine CD80 protein fused to rabbit IgG Fc (cCD80-Ig), the nucleotide sequence encoding the putative extracellular region of cCD80 was amplified by polymerase chain reaction (PCR) using cDNA obtained from beagle PBMCs stimulated with phorbol 12-myristate 13-acetate (20 ng/mL, Sigma-Aldrich, St. Louis, MO, USA) and ionomycin (1 μg/mL, Sigma-Aldrich) and the gene-specific primers (5′-CGC GGA TAT CAT GGA TTA CAC AGC GAA GTG-3′ and 5′-CGG GGT ACC CCA GAG CTG TTG CTG GTT AT-3′). .. The amplicon was then cloned into the multicloning site of the pCXN-2.1–rabbit IgG Fc vector (kindly provided by Dr T. Yokomizo, Juntendo University; modified) , using EcoRV and KpnI restriction enzyme sites.

    Article Title: Ephrin-A1-Mediated Dopaminergic Neurogenesis and Angiogenesis in a Rat Model of Parkinson's Disease
    Article Snippet: .. Preparation of Clustered Ephrin-A1-Fc, Clustered IgG(Fc), and FGF2 Recombinant mouse ephrin-A1 fused by means of a polypeptide linker to the Fc portion of human IgG1 (ephrin-A1-Fc) was purchased from Sigma-Aldrich (St. Louis, MO; Cat. #E9902). .. To prepare clustered ephrin-A1-Fc, 20 µg ephrin-A1-Fc was incubated with 48 µg rabbit anti-human IgG(Fc) antibody (Jackson ImmunoResearch Laboratories, West Grove, PA; Cat. #309-005-008) in 30 µl phosphate-buffered saline (PBS) at 4°C for ≥1 hour.

    Chloramphenicol Acetyltransferase Assay:

    Article Title: A canine chimeric monoclonal antibody targeting PD-L1 and its clinical efficacy in canine oral malignant melanoma or undifferentiated sarcoma
    Article Snippet: .. Blocking assay for PD-1/PD-L1 or CD80/PD-L1 binding For the preparation of recombinant canine CD80 protein fused to rabbit IgG Fc (cCD80-Ig), the nucleotide sequence encoding the putative extracellular region of cCD80 was amplified by polymerase chain reaction (PCR) using cDNA obtained from beagle PBMCs stimulated with phorbol 12-myristate 13-acetate (20 ng/mL, Sigma-Aldrich, St. Louis, MO, USA) and ionomycin (1 μg/mL, Sigma-Aldrich) and the gene-specific primers (5′-CGC GGA TAT CAT GGA TTA CAC AGC GAA GTG-3′ and 5′-CGG GGT ACC CCA GAG CTG TTG CTG GTT AT-3′). .. The amplicon was then cloned into the multicloning site of the pCXN-2.1–rabbit IgG Fc vector (kindly provided by Dr T. Yokomizo, Juntendo University; modified) , using EcoRV and KpnI restriction enzyme sites.

    Binding Assay:

    Article Title: Function and Protective Capacity of Treponema pallidum subsp. pallidum Glycerophosphodiester Phosphodiesterase
    Article Snippet: .. Primary Igs were used at a concentration of 1 μg/ml and included human IgA (Sigma), IgD (The Binding Site, Birmingham, United Kingdom), intact IgG (Sigma), IgG Fc and Fab fragments, and IgM (Sigma). .. Corresponding horseradish peroxidase-conjugated secondary antibodies (Sigma) were used at a concentration of 0.2 μg/ml and included goat F(ab′)2 anti-human IgA (alpha chain specific), goat F(ab′)2 anti-human IgD (delta chain specific), goat F(ab′)2 anti-human IgG (gamma chain specific) and goat F(ab′)2 anti-human IgM (mu chain specific).

    Article Title: A canine chimeric monoclonal antibody targeting PD-L1 and its clinical efficacy in canine oral malignant melanoma or undifferentiated sarcoma
    Article Snippet: .. Blocking assay for PD-1/PD-L1 or CD80/PD-L1 binding For the preparation of recombinant canine CD80 protein fused to rabbit IgG Fc (cCD80-Ig), the nucleotide sequence encoding the putative extracellular region of cCD80 was amplified by polymerase chain reaction (PCR) using cDNA obtained from beagle PBMCs stimulated with phorbol 12-myristate 13-acetate (20 ng/mL, Sigma-Aldrich, St. Louis, MO, USA) and ionomycin (1 μg/mL, Sigma-Aldrich) and the gene-specific primers (5′-CGC GGA TAT CAT GGA TTA CAC AGC GAA GTG-3′ and 5′-CGG GGT ACC CCA GAG CTG TTG CTG GTT AT-3′). .. The amplicon was then cloned into the multicloning site of the pCXN-2.1–rabbit IgG Fc vector (kindly provided by Dr T. Yokomizo, Juntendo University; modified) , using EcoRV and KpnI restriction enzyme sites.

    Article Title: Neurexin-Neuroligin Adhesions Capture Surface-Diffusing AMPA Receptors through PSD-95 Scaffolds
    Article Snippet: .. 2 μg of soluble Nrx1β-Fc were mixed with 1 μg of anti-Human-Fc into 100 μl of culture medium or observation medium containing 0.3% globulin-free BSA (Sigma) to avoid nonspecific binding. ..

    Injection:

    Article Title: Intramyocardial administration of chimeric ephrinA1-Fc promotes tissue salvage following myocardial infarction in mice
    Article Snippet: .. Immediately following coronary occlusion, using a Hamilton syringe with a sterile 30 gauge needle, animals received a single intramyocardial injection of either 6 μg IgG-Fc (R & D), or 6 μg ephrinA1-Fc (Sigma) resuspended in 6 μl sterile PBS at the peri-infarct zone. .. Injections occurred within 1 min of coronary ligation.

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    Millipore secondary antibody incubation
    Secondary Antibody Incubation, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 104 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 104 article reviews
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