biotinylated goat anti rabbit igg  (Vector Laboratories)


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    Name:
    Biotinylated Goat Anti Rabbit IgG Antibody
    Description:
    Biotinylated Goat Anit Rabbit IgG Antibody is prepared using proprietary immunization schedules that produce high affinity antibodies The antibodies are then purified by affinity chromatography and cross reactivities that are likely to interfere with specific labeling are removed by solid phase adsorption techniques The biotinylated secondary antibodies are conjugated to ensure the maximum degree of labeling without compromising the specificity or affinity of the antibody These antibodies are subjected to rigorous quality control assays and can be used for tissue and cell staining ELISAs and blots Biotinylated Goat Anti Rabbit IgG H L is supplied in liquid format With some exceptions the recommended dilution for most applications is 1 200 H L indicates the antibody recognizes both heavy and light chains This antibody is included in the VECTASTAIN ABC kits
    Catalog Number:
    ba-1000
    Price:
    None
    Host:
    Goat
    Size:
    1 5 mg
    Category:
    Antibodies
    Reactivity:
    Rabbit
    Buy from Supplier


    Structured Review

    Vector Laboratories biotinylated goat anti rabbit igg
    Biotinylated Goat Anti Rabbit IgG Antibody
    Biotinylated Goat Anit Rabbit IgG Antibody is prepared using proprietary immunization schedules that produce high affinity antibodies The antibodies are then purified by affinity chromatography and cross reactivities that are likely to interfere with specific labeling are removed by solid phase adsorption techniques The biotinylated secondary antibodies are conjugated to ensure the maximum degree of labeling without compromising the specificity or affinity of the antibody These antibodies are subjected to rigorous quality control assays and can be used for tissue and cell staining ELISAs and blots Biotinylated Goat Anti Rabbit IgG H L is supplied in liquid format With some exceptions the recommended dilution for most applications is 1 200 H L indicates the antibody recognizes both heavy and light chains This antibody is included in the VECTASTAIN ABC kits
    https://www.bioz.com/result/biotinylated goat anti rabbit igg/product/Vector Laboratories
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    biotinylated goat anti rabbit igg - by Bioz Stars, 2020-07
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    Images

    1) Product Images from "Insertion of Basic Amino Acids in the Hemagglutinin Cleavage Site of H4N2 Avian Influenza Virus (AIV)—Reduced Virus Fitness in Chickens is Restored by Reassortment with Highly Pathogenic H5N1 AIV"

    Article Title: Insertion of Basic Amino Acids in the Hemagglutinin Cleavage Site of H4N2 Avian Influenza Virus (AIV)—Reduced Virus Fitness in Chickens is Restored by Reassortment with Highly Pathogenic H5N1 AIV

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms21072353

    Distribution of avian influenza virus NP in selected organs of inoculated birds. Distribution of influenza NP in brain ( A , E , I , M ), lung ( B , F , J , N ), spleen ( C , G , K , O ) and heart ( D , H , L , P ) of inoculated chickens of selected viruses at 4 dpi (except for H5N1_H4_T 327 K) as detected by immunohistochemistry using primary polyclonal rabbit anti-NP A/FPV/Rostock/34 antibody (1:750) and a secondary biotinylated goat anti-rabbit IgG (Vector Laboratories, Burlingame, CA, USA) antibody (1:200). 3-amino-9-ethyl-carbazol (red-brown); hematoxylin counterstain (blue); Nomarski contrast; bars A,B,D,E,F,H,I,J,L,M,N,P = 20 µm. Bars C,G,K,O = 50 µm.
    Figure Legend Snippet: Distribution of avian influenza virus NP in selected organs of inoculated birds. Distribution of influenza NP in brain ( A , E , I , M ), lung ( B , F , J , N ), spleen ( C , G , K , O ) and heart ( D , H , L , P ) of inoculated chickens of selected viruses at 4 dpi (except for H5N1_H4_T 327 K) as detected by immunohistochemistry using primary polyclonal rabbit anti-NP A/FPV/Rostock/34 antibody (1:750) and a secondary biotinylated goat anti-rabbit IgG (Vector Laboratories, Burlingame, CA, USA) antibody (1:200). 3-amino-9-ethyl-carbazol (red-brown); hematoxylin counterstain (blue); Nomarski contrast; bars A,B,D,E,F,H,I,J,L,M,N,P = 20 µm. Bars C,G,K,O = 50 µm.

    Techniques Used: Immunohistochemistry, Plasmid Preparation

    2) Product Images from "Characterization of G-Protein-Gated K+ Channels Composed of Kir3.2 Subunits in Dopaminergic Neurons of the Substantia Nigra"

    Article Title: Characterization of G-Protein-Gated K+ Channels Composed of Kir3.2 Subunits in Dopaminergic Neurons of the Substantia Nigra

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.19-03-01006.1999

    A , RT-PCR analysis of Kir3.0 mRNAs in rat SN and Cx. Using the Kir3.0-specific primers indicated above each panel, their expression was examined in cDNAs obtained from rat SN ( odd numbers ) and Cx ( even numbers ). PCR products (519, 369, 456, and 574 bp) of Kir3.2a, Kir3.2c, Kir3.3, and Kir3.2b were detected in both SN and Cx, whereas that of Kir3.1 (666 bp) was found in Cx but not in SN. Numbers indicate the standard markers in base pairs. B , Immunoprecipitation analysis of Kir3.2 isoforms in rat SN and Cx. Biotinylated membrane proteins of rat SN ( a ) or Cx ( b ) were incubated with aG2C-3 ( lanes 1 - 3 ) or aG2A-5 antibodies ( lanes 4 , 5 ) as indicated. The immunoprecipitants were detected with streptavidin–HRP ( SA - HRP ; lanes 1 , 4 ), aG2A-5 ( lane 2 ), aG1C-1 ( lane 3 ), or aG2C-3 antibodies ( lane 5 ). The positions of Kir3.2a ( small open arrowheads ) and Kir3.2c ( large arrowheads ) isoforms and Kir3.1 subunits ( arrows ) are indicated. IgG heavy chains or unknown bands are indicated with asterisks and number signs , respectively. Numbers on the left of the panels indicate the molecular weights of the standard markers in kilodaltons. C , Detection of Kir3.3 in the aG2A-5 immunoprecipitant from rat Cx. The lysates of HEK293T cells transfected with the plasmids indicated in each lane were examined for specificity of aG3NC and aG2B-2 with immunoblot analysis ( a ). Both antibodies could specifically detect proteins at 41 kDa of Kir3.3 and 38 kDa of Kir3.2b, respectively. When the PVDF membranes blotted with SA–HRP were overexposed to the films until the bands of Kir3.2a and Kir3.2c were indistinguishable ( b ), a faint signal at 40 kDa ( small arrows ) was detected in the immunocomplex of aG2A-5 obtained from Cx ( lane 2 ), not from SN ( lane 1 ). The 40 kDa protein in the immunoprecipitant has an immunoreactivity to aG3NC. However, signal with aG2B-2 could not be found either in SN or in Cx.
    Figure Legend Snippet: A , RT-PCR analysis of Kir3.0 mRNAs in rat SN and Cx. Using the Kir3.0-specific primers indicated above each panel, their expression was examined in cDNAs obtained from rat SN ( odd numbers ) and Cx ( even numbers ). PCR products (519, 369, 456, and 574 bp) of Kir3.2a, Kir3.2c, Kir3.3, and Kir3.2b were detected in both SN and Cx, whereas that of Kir3.1 (666 bp) was found in Cx but not in SN. Numbers indicate the standard markers in base pairs. B , Immunoprecipitation analysis of Kir3.2 isoforms in rat SN and Cx. Biotinylated membrane proteins of rat SN ( a ) or Cx ( b ) were incubated with aG2C-3 ( lanes 1 - 3 ) or aG2A-5 antibodies ( lanes 4 , 5 ) as indicated. The immunoprecipitants were detected with streptavidin–HRP ( SA - HRP ; lanes 1 , 4 ), aG2A-5 ( lane 2 ), aG1C-1 ( lane 3 ), or aG2C-3 antibodies ( lane 5 ). The positions of Kir3.2a ( small open arrowheads ) and Kir3.2c ( large arrowheads ) isoforms and Kir3.1 subunits ( arrows ) are indicated. IgG heavy chains or unknown bands are indicated with asterisks and number signs , respectively. Numbers on the left of the panels indicate the molecular weights of the standard markers in kilodaltons. C , Detection of Kir3.3 in the aG2A-5 immunoprecipitant from rat Cx. The lysates of HEK293T cells transfected with the plasmids indicated in each lane were examined for specificity of aG3NC and aG2B-2 with immunoblot analysis ( a ). Both antibodies could specifically detect proteins at 41 kDa of Kir3.3 and 38 kDa of Kir3.2b, respectively. When the PVDF membranes blotted with SA–HRP were overexposed to the films until the bands of Kir3.2a and Kir3.2c were indistinguishable ( b ), a faint signal at 40 kDa ( small arrows ) was detected in the immunocomplex of aG2A-5 obtained from Cx ( lane 2 ), not from SN ( lane 1 ). The 40 kDa protein in the immunoprecipitant has an immunoreactivity to aG3NC. However, signal with aG2B-2 could not be found either in SN or in Cx.

    Techniques Used: Reverse Transcription Polymerase Chain Reaction, Expressing, Polymerase Chain Reaction, Immunoprecipitation, Incubation, Transfection

    3) Product Images from "β-Catenin, a Transcription Factor Activated by Canonical Wnt Signaling, Is Expressed in Sensory Neurons of Calves Latently Infected with Bovine Herpesvirus 1"

    Article Title: β-Catenin, a Transcription Factor Activated by Canonical Wnt Signaling, Is Expressed in Sensory Neurons of Calves Latently Infected with Bovine Herpesvirus 1

    Journal: Journal of Virology

    doi: 10.1128/JVI.02971-15

    Detection of β-catenin during latency. (A) TG were collected from three mock-infected calves or three latently infected calves (at least 60 days postinfection). Thin sections were cut from formalin-fixed paraffin-embedded TG sections. The β-catenin antibody used for this study was purchased from Abcam (ab6302) and was diluted 1:200. Biotinylated goat anti-rabbit IgG (Vector Laboratories) was used as a secondary antibody. Thin sections from mock-infected calves were used as controls. Closed circles denote β-catenin-positive neurons. (B) The number of β-catenin-positive neurons from 750 total neurons was estimated from sections derived from three latently infected calves or three mock-infected calves. An asterisk denotes significant differences ( P
    Figure Legend Snippet: Detection of β-catenin during latency. (A) TG were collected from three mock-infected calves or three latently infected calves (at least 60 days postinfection). Thin sections were cut from formalin-fixed paraffin-embedded TG sections. The β-catenin antibody used for this study was purchased from Abcam (ab6302) and was diluted 1:200. Biotinylated goat anti-rabbit IgG (Vector Laboratories) was used as a secondary antibody. Thin sections from mock-infected calves were used as controls. Closed circles denote β-catenin-positive neurons. (B) The number of β-catenin-positive neurons from 750 total neurons was estimated from sections derived from three latently infected calves or three mock-infected calves. An asterisk denotes significant differences ( P

    Techniques Used: Infection, Formalin-fixed Paraffin-Embedded, Plasmid Preparation, Derivative Assay

    ). The adjacent section was stained with the β-catenin antibody (1:200 dilution). Biotinylated goat anti-rabbit IgG (Vector Laboratories) was used as a secondary antibody. Neurons, indicated by numbers 1 to 9, are ORF2 + and β-catenin + ). Neurons, indicated by numbers 1 to 12, are β-catenin + neurons in one section and are also shown in the section stained with the bICP0 antibody to point out the location of the same neurons numbered in the section stained by the β-catenin antibody. These results are representative of four sections cut from TG of two latently infected calves.
    Figure Legend Snippet: ). The adjacent section was stained with the β-catenin antibody (1:200 dilution). Biotinylated goat anti-rabbit IgG (Vector Laboratories) was used as a secondary antibody. Neurons, indicated by numbers 1 to 9, are ORF2 + and β-catenin + ). Neurons, indicated by numbers 1 to 12, are β-catenin + neurons in one section and are also shown in the section stained with the bICP0 antibody to point out the location of the same neurons numbered in the section stained by the β-catenin antibody. These results are representative of four sections cut from TG of two latently infected calves.

    Techniques Used: Staining, Plasmid Preparation, Infection

    Decreased numbers of β-catenin + neurons during DEX-induced reactivation from latency. (A) A representative TG section collected from a calf that was latently infected (at least 60 days postinfection) or from a latently infected calf treated with DEX for 6 h to induce reactivation from latency. Thin sections were cut from formalin-fixed paraffin-embedded TG sections. The β-catenin antibody used for this study was purchased from Abcam (ab6302) and was diluted 1:200. Biotinylated goat anti-rabbit IgG (Vector laboratories) was used as a secondary antibody. Thin sections from mock-infected calves were used as controls. Closed circles denote β-catenin-positive neurons. (B) The number of β-catenin-positive neurons from 750 total neurons was estimated from TG sections from three latently infected calves and from three latently infected calves treated with DEX for 70 min, 3 h, or 6 h. An asterisk denotes significant differences ( P
    Figure Legend Snippet: Decreased numbers of β-catenin + neurons during DEX-induced reactivation from latency. (A) A representative TG section collected from a calf that was latently infected (at least 60 days postinfection) or from a latently infected calf treated with DEX for 6 h to induce reactivation from latency. Thin sections were cut from formalin-fixed paraffin-embedded TG sections. The β-catenin antibody used for this study was purchased from Abcam (ab6302) and was diluted 1:200. Biotinylated goat anti-rabbit IgG (Vector laboratories) was used as a secondary antibody. Thin sections from mock-infected calves were used as controls. Closed circles denote β-catenin-positive neurons. (B) The number of β-catenin-positive neurons from 750 total neurons was estimated from TG sections from three latently infected calves and from three latently infected calves treated with DEX for 70 min, 3 h, or 6 h. An asterisk denotes significant differences ( P

    Techniques Used: Infection, Formalin-fixed Paraffin-Embedded, Plasmid Preparation

    4) Product Images from "VPAC2 receptor expression in human normal and neoplastic tissues: evaluation of the novel MAB SP235"

    Article Title: VPAC2 receptor expression in human normal and neoplastic tissues: evaluation of the novel MAB SP235

    Journal: Endocrine Connections

    doi: 10.1530/EC-14-0051

    SP235 immunohistochemistry of human normal and neoplastic tissues. Sections were dewaxed, microwaved in citric acid and incubated with the rabbit monoclonal anti-VPAC2 antibody (SP235) at a dilution of 1:500. Sections were then sequentially treated with biotinylated anti-rabbit IgG and AB solution. Sections were then developed in AEC and lightly counterstained with haematoxylin. Insets in A and D, for adsorption controls the SP235 was incubated with 10 μg/ml of the peptide used for immunisations (+ peptide). Scale bar, A=B=C=F=I=250 μm and D=E=G=H=100 μm.
    Figure Legend Snippet: SP235 immunohistochemistry of human normal and neoplastic tissues. Sections were dewaxed, microwaved in citric acid and incubated with the rabbit monoclonal anti-VPAC2 antibody (SP235) at a dilution of 1:500. Sections were then sequentially treated with biotinylated anti-rabbit IgG and AB solution. Sections were then developed in AEC and lightly counterstained with haematoxylin. Insets in A and D, for adsorption controls the SP235 was incubated with 10 μg/ml of the peptide used for immunisations (+ peptide). Scale bar, A=B=C=F=I=250 μm and D=E=G=H=100 μm.

    Techniques Used: Immunohistochemistry, Incubation, Adsorption

    Characterisation of SP235 using mouse, rat and human tissues. (A) Comparision of the carboxyl-terminal sequences of mouse, rat and human VPAC2. The sequence depicted for the human VPAC2 was used for antibody generation. (B) Western blotting analysis of SP235 in various tissues. Tissue extracts from WT mice ( Vpac + / + ) and mice lacking Vpac2 ( Vpac2 −/− ) were separated on 7.5% SDS–polyacrylamide gels and blotted onto PVDF membranes. Membranes were then incubated with the rabbit monoclonal anti-VPAC2 antibody (SP235) at a dilution of 1:500. Membranes were developed using ECL. Ordinate, migration of protein molecular weight markers (kDa). (C) SP235 immunohistochemistry in rat and human tissues. Sections were dewaxed, microwaved in citric acid and incubated with the rabbit monoclonal anti-VPAC2 antibody (SP235) at a dilution of 1:500. Sections were then sequentially treated with biotinylated anti-rabbit IgG and AB solution. Sections were then developed in AEC and lightly counterstained with haematoxylin. Representative photomicrographs from one of five different tissue samples are shown. Scale bar: upper panel=200 μm and lower panel=100 μm.
    Figure Legend Snippet: Characterisation of SP235 using mouse, rat and human tissues. (A) Comparision of the carboxyl-terminal sequences of mouse, rat and human VPAC2. The sequence depicted for the human VPAC2 was used for antibody generation. (B) Western blotting analysis of SP235 in various tissues. Tissue extracts from WT mice ( Vpac + / + ) and mice lacking Vpac2 ( Vpac2 −/− ) were separated on 7.5% SDS–polyacrylamide gels and blotted onto PVDF membranes. Membranes were then incubated with the rabbit monoclonal anti-VPAC2 antibody (SP235) at a dilution of 1:500. Membranes were developed using ECL. Ordinate, migration of protein molecular weight markers (kDa). (C) SP235 immunohistochemistry in rat and human tissues. Sections were dewaxed, microwaved in citric acid and incubated with the rabbit monoclonal anti-VPAC2 antibody (SP235) at a dilution of 1:500. Sections were then sequentially treated with biotinylated anti-rabbit IgG and AB solution. Sections were then developed in AEC and lightly counterstained with haematoxylin. Representative photomicrographs from one of five different tissue samples are shown. Scale bar: upper panel=200 μm and lower panel=100 μm.

    Techniques Used: Sequencing, Western Blot, Mouse Assay, Incubation, Migration, Molecular Weight, Immunohistochemistry

    5) Product Images from "Myocardial protection from ischemia/reperfusion injury by endogenous and exogenous HGF"

    Article Title: Myocardial protection from ischemia/reperfusion injury by endogenous and exogenous HGF

    Journal: Journal of Clinical Investigation

    doi:

    Adverse effects of neutralization of endogenous HGF on the ischemia/reperfusion injury model. ( a ) Specificity of the neutralizing antibody to HGF. Plasma from a rat with ischemia/reperfusion injury was immunoprecipitated with normal IgG (lane 1) or anti–rat HGF IgG (lane 2), and immunoreactive proteins were detected by Western blot, using biotinylated anti–rat HGF IgG. ( b ) Immunohistochemical staining of infarcted hearts with α-sarcomeric actin to depict the infarct area and its quantification. Anti–rat HGF IgG ( n = 10) or normal IgG ( n = 10) was injected 20 minutes before coronary occlusion, and every 12 hours after reperfusion. Forty-eight hours after operation, rats were killed and histological and biochemical analyses were made. Arrowheads indicate the α-sarcomeric actin–negative infarct area (original magnification, ×40). A P
    Figure Legend Snippet: Adverse effects of neutralization of endogenous HGF on the ischemia/reperfusion injury model. ( a ) Specificity of the neutralizing antibody to HGF. Plasma from a rat with ischemia/reperfusion injury was immunoprecipitated with normal IgG (lane 1) or anti–rat HGF IgG (lane 2), and immunoreactive proteins were detected by Western blot, using biotinylated anti–rat HGF IgG. ( b ) Immunohistochemical staining of infarcted hearts with α-sarcomeric actin to depict the infarct area and its quantification. Anti–rat HGF IgG ( n = 10) or normal IgG ( n = 10) was injected 20 minutes before coronary occlusion, and every 12 hours after reperfusion. Forty-eight hours after operation, rats were killed and histological and biochemical analyses were made. Arrowheads indicate the α-sarcomeric actin–negative infarct area (original magnification, ×40). A P

    Techniques Used: Neutralization, Immunoprecipitation, Western Blot, Immunohistochemistry, Staining, Injection

    6) Product Images from "The Wnt Signaling Pathway Is Differentially Expressed during the Bovine Herpesvirus 1 Latency-Reactivation Cycle: Evidence That Two Protein Kinases Associated with Neuronal Survival, Akt3 and BMPR2, Are Expressed at Higher Levels during Latency"

    Article Title: The Wnt Signaling Pathway Is Differentially Expressed during the Bovine Herpesvirus 1 Latency-Reactivation Cycle: Evidence That Two Protein Kinases Associated with Neuronal Survival, Akt3 and BMPR2, Are Expressed at Higher Levels during Latency

    Journal: Journal of Virology

    doi: 10.1128/JVI.01937-17

    Detection of GNAQ in TG neurons during latency-reactivation cycle. TG were collected from 3 uninfected calves (U) (A), latently infected calves (L) (B), or latently infected calves treated with DEX for 6 h to initiate reactivation from latency (DEX) (C). Thin sections were cut from formalin-fixed, paraffin-embedded TG sections. The GNAQ antibody (ab75825; Abcam) was diluted 1:450. Biotinylated goat anti-rabbit IgG (Vector Laboratories) was used as a secondary antibody. Arrows denote GNAQ + neurons in the respective samples. (D) The percentage of GNAQ-positive neurons from 296 uninfected neurons, 241 latently infected neurons, and 209 TG neurons at 6 h after latently infected calves were treated with DEX. An asterisk denotes significant differences ( P
    Figure Legend Snippet: Detection of GNAQ in TG neurons during latency-reactivation cycle. TG were collected from 3 uninfected calves (U) (A), latently infected calves (L) (B), or latently infected calves treated with DEX for 6 h to initiate reactivation from latency (DEX) (C). Thin sections were cut from formalin-fixed, paraffin-embedded TG sections. The GNAQ antibody (ab75825; Abcam) was diluted 1:450. Biotinylated goat anti-rabbit IgG (Vector Laboratories) was used as a secondary antibody. Arrows denote GNAQ + neurons in the respective samples. (D) The percentage of GNAQ-positive neurons from 296 uninfected neurons, 241 latently infected neurons, and 209 TG neurons at 6 h after latently infected calves were treated with DEX. An asterisk denotes significant differences ( P

    Techniques Used: Infection, Formalin-fixed Paraffin-Embedded, Plasmid Preparation

    Akt3 is frequently detected in ORF2 + neurons during latency. Consecutive sections from formalin-fixed paraffin-embedded TG sections from latently infected calves were prepared. One section was stained with the Akt3 antibody (ab152157; Abcam) that was diluted 1:500. A consecutive section was stained with a peptide-specific ORF2 antibody (1:500 dilution). Biotinylated goat anti-rabbit IgG (Vector Laboratories) was used as a secondary antibody for the sections. Areas of sections that contained ORF2 + neurons were subsequently examined for Akt3 staining. Numbers denote the ORF2-positive neurons, and neurons 1, 3, 4, and 5 were also Akt3 + . Magnification is approximately 400×, and these sections are representative of many sections that were examined.
    Figure Legend Snippet: Akt3 is frequently detected in ORF2 + neurons during latency. Consecutive sections from formalin-fixed paraffin-embedded TG sections from latently infected calves were prepared. One section was stained with the Akt3 antibody (ab152157; Abcam) that was diluted 1:500. A consecutive section was stained with a peptide-specific ORF2 antibody (1:500 dilution). Biotinylated goat anti-rabbit IgG (Vector Laboratories) was used as a secondary antibody for the sections. Areas of sections that contained ORF2 + neurons were subsequently examined for Akt3 staining. Numbers denote the ORF2-positive neurons, and neurons 1, 3, 4, and 5 were also Akt3 + . Magnification is approximately 400×, and these sections are representative of many sections that were examined.

    Techniques Used: Formalin-fixed Paraffin-Embedded, Infection, Staining, Plasmid Preparation

    Comparison of Akt3 expression during the BoHV-1 latency-reactivation cycle. (A) TG were collected from 3 uninfected calves, 3 latently infected calves, or 3 latently infected calves treated with DEX for 6 h to initiate reactivation from latency. Thin sections were cut from formalin-fixed paraffin-embedded TG sections. The Akt3 antibody (ab152157; Abcam) was diluted 1:500. Biotinylated goat anti-rabbit IgG (Vector Laboratories) was used as a secondary antibody. Blue arrows denote Akt3-positive TG neurons that contained an Akt3-positive nucleus and a counterstained nucleolus. Black arrows denote TG neurons in which the nucleus was not visible, but they were Akt3 + . Closed circles denote TG neurons that contain a nucleus in which the nucleolus is counterstained but was not stained by the Akt3 antibody. These images are representative of many sections stained with the Akt3 antibody. Magnification is approximately 400×. (B) The percentage of Akt3-positive TG neurons from 500 total neurons was estimated from sections derived from 3 latently infected calves, 3 mock-infected calves, and 3 latently infected calves treated with DEX for 6 h. An asterisk denotes significant differences ( P
    Figure Legend Snippet: Comparison of Akt3 expression during the BoHV-1 latency-reactivation cycle. (A) TG were collected from 3 uninfected calves, 3 latently infected calves, or 3 latently infected calves treated with DEX for 6 h to initiate reactivation from latency. Thin sections were cut from formalin-fixed paraffin-embedded TG sections. The Akt3 antibody (ab152157; Abcam) was diluted 1:500. Biotinylated goat anti-rabbit IgG (Vector Laboratories) was used as a secondary antibody. Blue arrows denote Akt3-positive TG neurons that contained an Akt3-positive nucleus and a counterstained nucleolus. Black arrows denote TG neurons in which the nucleus was not visible, but they were Akt3 + . Closed circles denote TG neurons that contain a nucleus in which the nucleolus is counterstained but was not stained by the Akt3 antibody. These images are representative of many sections stained with the Akt3 antibody. Magnification is approximately 400×. (B) The percentage of Akt3-positive TG neurons from 500 total neurons was estimated from sections derived from 3 latently infected calves, 3 mock-infected calves, and 3 latently infected calves treated with DEX for 6 h. An asterisk denotes significant differences ( P

    Techniques Used: Expressing, Infection, Formalin-fixed Paraffin-Embedded, Plasmid Preparation, Staining, Derivative Assay

    7) Product Images from "New perspectives on the renal slit diaphragm protein podocin"

    Article Title: New perspectives on the renal slit diaphragm protein podocin

    Journal: Modern Pathology

    doi: 10.1038/modpathol.2011.58

    Immunohistochemical detection suggests Sertoli cells to be the origin of testicular podocin. ( a , b ) Detection of WT-1 in nuclei of Sertoli cells ( b ) and podocin ( a ) within the membranes of sertoli cell extensions within a seminiferous tubule (APAAP, × 400). ( c ) The same primary antibody, but a biotinylated goat anti-rabbit IgG was used to detect podocin in a Sertoli cell tumor. ( d ) Podocin expression in renal glomeruli served as a positive control. Original magnification is shown in the lower right-hand corner of each image.
    Figure Legend Snippet: Immunohistochemical detection suggests Sertoli cells to be the origin of testicular podocin. ( a , b ) Detection of WT-1 in nuclei of Sertoli cells ( b ) and podocin ( a ) within the membranes of sertoli cell extensions within a seminiferous tubule (APAAP, × 400). ( c ) The same primary antibody, but a biotinylated goat anti-rabbit IgG was used to detect podocin in a Sertoli cell tumor. ( d ) Podocin expression in renal glomeruli served as a positive control. Original magnification is shown in the lower right-hand corner of each image.

    Techniques Used: Immunohistochemistry, Expressing, Positive Control

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    Incubation:

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    Article Title: Characterization of G-Protein-Gated K+ Channels Composed of Kir3.2 Subunits in Dopaminergic Neurons of the Substantia Nigra
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    Article Title: Characterization of G-Protein-Gated K+ Channels Composed of Kir3.2 Subunits in Dopaminergic Neurons of the Substantia Nigra
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    Generated:

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    Mouse Assay:

    Article Title: Selective Restoration of Pomc Expression in Glutamatergic POMC Neurons: Evidence for a Dynamic Hypothalamic Neurotransmitter Network
    Article Snippet: .. Following triplicate washes, one set of the sections from control and restored mice was incubated with a biotinylated goat anti-rabbit secondary antisera (1:500, Vector Labs; catalog #BA-1000 ROS23) followed by treatment with a Vectastain ABC HRP kit (Vector Labs; catalog #PK-4000) and development of a colorimetric stain with diaminobenzidine (250 μg/ml in TBS with 0.1% H2 O2 ). .. A second set of sections from control and restored mice was incubated with Alexa Fluor 568 (A568) goat anti-rabbit secondary antibody (1:500; ThermoFisher Scientific; catalog #A-11036).

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    Vector Laboratories biotinylated goat anti rabbit immunoglobulin g igg
    Bar graph shows a comparison of the mean area of <t>IgG</t> immunostaining among groups. It must be noted that neither hypothermic intervention nor FK506 administration prevented the spatial extravasation of endogenous IgG. In addition, even the combination
    Biotinylated Goat Anti Rabbit Immunoglobulin G Igg, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 99/100, based on 865 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bar graph shows a comparison of the mean area of IgG immunostaining among groups. It must be noted that neither hypothermic intervention nor FK506 administration prevented the spatial extravasation of endogenous IgG. In addition, even the combination

    Journal: Journal of Cerebral Blood Flow & Metabolism

    Article Title: Combinational therapy using hypothermia and the immunophilin ligand FK506 to target altered pial arteriolar reactivity, axonal damage, and blood-brain barrier dysfunction after traumatic brain injury in rat

    doi: 10.1038/jcbfm.2010.208

    Figure Lengend Snippet: Bar graph shows a comparison of the mean area of IgG immunostaining among groups. It must be noted that neither hypothermic intervention nor FK506 administration prevented the spatial extravasation of endogenous IgG. In addition, even the combination

    Article Snippet: Next, the sections were incubated for 1 hour with biotinylated goat anti-rabbit immunoglobulin G (IgG) (Vector Laboratories Inc., Burlingame, CA, USA) diluted 1:1,000 in 1% normal goat serum in PBS.

    Techniques: Immunostaining

    CD47 Quantification. (A) The modification chemistry summarized in was utilized to facilitate quantification. Following PEI-PDT addition, primary amines were acetylated using sulfo-NHS-Acetate. recCD47 and pepCD47 were biotinylated using Sulfo-NHS-LC-LC-Biotin.

    Journal: Biomaterials

    Article Title: Enhanced biocompatibility of CD47-functionalized vascular stents

    doi: 10.1016/j.biomaterials.2016.02.008

    Figure Lengend Snippet: CD47 Quantification. (A) The modification chemistry summarized in was utilized to facilitate quantification. Following PEI-PDT addition, primary amines were acetylated using sulfo-NHS-Acetate. recCD47 and pepCD47 were biotinylated using Sulfo-NHS-LC-LC-Biotin.

    Article Snippet: The absolute values of CD47 immobilization density were obtained by plotting the OD data generated with the sets of foil samples to a standard OD curve obtained with escalating amounts of biotinylated goat anti-rabbit antibody (Vector Lab), disclosed to contain an average of 10 biotin groups per a 150 kDa molecule.

    Techniques: Modification

    Sodium/iodide symporter (NIS) expression is primarily restricted to striated ducts in human salivary glands. (A) NIS is expressed at a high level along basolateral membranes of striated duct cells (S), with fewer intercalated (rectangle) and excretory (E) duct cells demonstrating lower NIS levels. Acinar (A) cells do not express NIS. Anti-human NIS antibody, avidin-biotin complex, DAB chromogen, hematoxylin counterstain, bar=25 μm. (B) Distribution and intensity of NIS immunoreactivity among intercalated (ID), striated (SD), and excretory (ED) ductal cells in normal human submandibular, parotid, and minor salivary glands. NIS expression is greater and more frequent in striated ducts, regardless of gland type.

    Journal: Thyroid

    Article Title: Modulation of Sodium/Iodide Symporter Expression in the Salivary Gland

    doi: 10.1089/thy.2012.0571

    Figure Lengend Snippet: Sodium/iodide symporter (NIS) expression is primarily restricted to striated ducts in human salivary glands. (A) NIS is expressed at a high level along basolateral membranes of striated duct cells (S), with fewer intercalated (rectangle) and excretory (E) duct cells demonstrating lower NIS levels. Acinar (A) cells do not express NIS. Anti-human NIS antibody, avidin-biotin complex, DAB chromogen, hematoxylin counterstain, bar=25 μm. (B) Distribution and intensity of NIS immunoreactivity among intercalated (ID), striated (SD), and excretory (ED) ductal cells in normal human submandibular, parotid, and minor salivary glands. NIS expression is greater and more frequent in striated ducts, regardless of gland type.

    Article Snippet: The secondary antibody used was a biotinylated goat anti-rabbit antibody (1:200, BA-1000, Vector Laboratories, Inc., Burlingame, CA) that was incubated for 20 minutes at room temperature.

    Techniques: Expressing, Avidin-Biotin Assay

    NIS expression is reduced in inflamed and neoplastic human salivary glands. (A) NIS expression in striated ducts is decreased in inflammatory salivary glands, as well as in benign and malignant neoplasms of ductal origin. (B) NIS immunoreactivity in inflamed (i, ii) and neoplastic (iii, iv) salivary tissue. NIS expression is variably decreased in striated ducts (S) of chronically inflamed salivary glands (i, ii) , particularly in ducts demonstrating goblet metaplasia (arrows). Neoplastic cells of Warthin's tumor (iii) and mucoepidermoid carcinoma (iv) demonstrate lower NIS level, with immunostaining intensity of 2+ and 1+, respectively. Anti-human NIS antibody, avidin-biotin complex, DAB chromogen, hematoxylin counterstain, bars=25 μm. F, periductal fibrosis; L, lymphocytic inflammation.

    Journal: Thyroid

    Article Title: Modulation of Sodium/Iodide Symporter Expression in the Salivary Gland

    doi: 10.1089/thy.2012.0571

    Figure Lengend Snippet: NIS expression is reduced in inflamed and neoplastic human salivary glands. (A) NIS expression in striated ducts is decreased in inflammatory salivary glands, as well as in benign and malignant neoplasms of ductal origin. (B) NIS immunoreactivity in inflamed (i, ii) and neoplastic (iii, iv) salivary tissue. NIS expression is variably decreased in striated ducts (S) of chronically inflamed salivary glands (i, ii) , particularly in ducts demonstrating goblet metaplasia (arrows). Neoplastic cells of Warthin's tumor (iii) and mucoepidermoid carcinoma (iv) demonstrate lower NIS level, with immunostaining intensity of 2+ and 1+, respectively. Anti-human NIS antibody, avidin-biotin complex, DAB chromogen, hematoxylin counterstain, bars=25 μm. F, periductal fibrosis; L, lymphocytic inflammation.

    Article Snippet: The secondary antibody used was a biotinylated goat anti-rabbit antibody (1:200, BA-1000, Vector Laboratories, Inc., Burlingame, CA) that was incubated for 20 minutes at room temperature.

    Techniques: Expressing, Immunostaining, Avidin-Biotin Assay

    Immunoperoxidase staining of B-lymphoma cells after overnight incubation with anti-CD20 (1F5). Cells were deposited on cytocentrifuge slides, fixed with formaldehyde, permeabilised with saponin, and stained with a biotinylated horse anti-mouse IgG, followed by a complex of streptavidin and peroxidase. Observation was with an × 40 objective, except as noted. ( A ) Raji cells, showing prominent staining of JN spots. ( B ) RL cells, showing dark staining of apparently extracellular objects, referred to as CFs. ( C ) A lower-power photograph of RL cells (× 10), to show the general staining pattern. ( D ) RL cells stained in the absence of saponin, to show antigen that is accessible without permeabilisation. Control Abs of the same subclass produced no brown staining.

    Journal: British Journal of Cancer

    Article Title: Antibodies to CD20 and MHC class II antigen bound to B-lymphoma cells accumulate in shed cytoplasmic fragments

    doi: 10.1038/sj.bjc.6602131

    Figure Lengend Snippet: Immunoperoxidase staining of B-lymphoma cells after overnight incubation with anti-CD20 (1F5). Cells were deposited on cytocentrifuge slides, fixed with formaldehyde, permeabilised with saponin, and stained with a biotinylated horse anti-mouse IgG, followed by a complex of streptavidin and peroxidase. Observation was with an × 40 objective, except as noted. ( A ) Raji cells, showing prominent staining of JN spots. ( B ) RL cells, showing dark staining of apparently extracellular objects, referred to as CFs. ( C ) A lower-power photograph of RL cells (× 10), to show the general staining pattern. ( D ) RL cells stained in the absence of saponin, to show antigen that is accessible without permeabilisation. Control Abs of the same subclass produced no brown staining.

    Article Snippet: For use with the rabbit anti-human IgM antisera, we used a biotinylated anti-rabbit IgG from Vector Labs.

    Techniques: Immunoperoxidase Staining, Incubation, Staining, Produced