biotinylated secondary antibody reagent  (Vector Laboratories)


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    Biotinylated Anti Avidin Antibody
    Description:
    Biotinylated Anti Avidin has been widely used as an amplifying reagent in immunohistochemistry in situ hybridization microarray assays ELISAs blots and many other applications The capability of binding avidin via either biotin binding sites or through antigen binding sites makes this biotinylated antibody unique Our antibodies to avidin are produced in goats using our highly purified avidin and isolated by affinity chromatography Anti Avidin does not bind streptavidin and Anti Streptavidin does not recognize avidin These antibodies provide opportunities to significantly amplify signals in many applications
    Catalog Number:
    ba-0300
    Price:
    None
    Category:
    Antibodies
    Size:
    0 5 mg
    Host:
    Goat
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    Structured Review

    Vector Laboratories biotinylated secondary antibody reagent
    Biotinylated Anti Avidin Antibody
    Biotinylated Anti Avidin has been widely used as an amplifying reagent in immunohistochemistry in situ hybridization microarray assays ELISAs blots and many other applications The capability of binding avidin via either biotin binding sites or through antigen binding sites makes this biotinylated antibody unique Our antibodies to avidin are produced in goats using our highly purified avidin and isolated by affinity chromatography Anti Avidin does not bind streptavidin and Anti Streptavidin does not recognize avidin These antibodies provide opportunities to significantly amplify signals in many applications
    https://www.bioz.com/result/biotinylated secondary antibody reagent/product/Vector Laboratories
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    Images

    1) Product Images from "gC1qR/p33 Blockade Reduces Staphylococcus aureus Colonization of Target Tissues in an Animal Model of Infective Endocarditis "

    Article Title: gC1qR/p33 Blockade Reduces Staphylococcus aureus Colonization of Target Tissues in an Animal Model of Infective Endocarditis

    Journal:

    doi: 10.1128/IAI.01794-05

    Functional activities of gC1qR MAbs 74.5.2 and 60.11 in rat serum. Biotinylated, clfA -positive bacteria were suspended (10% cell suspension) in selected serum samples from animals treated with gC1qR MAbs. Samples were applied to fibrinogen-coated microtiter
    Figure Legend Snippet: Functional activities of gC1qR MAbs 74.5.2 and 60.11 in rat serum. Biotinylated, clfA -positive bacteria were suspended (10% cell suspension) in selected serum samples from animals treated with gC1qR MAbs. Samples were applied to fibrinogen-coated microtiter

    Techniques Used: Functional Assay

    2) Product Images from "Y-cell receptive field and collicular projection of parasol ganglion cells in macaque monkey retina"

    Article Title: Y-cell receptive field and collicular projection of parasol ganglion cells in macaque monkey retina

    Journal:

    doi: 10.1523/JNEUROSCI.2982-08.2008

    Photomicrograph of ~1 mm 2 area of a macaque retina that was retrogradely tracer labeled from injections of biotinylated rhodamine dextran in the superior colliculus and photostained in the in vitro retina. Following fixation the retina was processed for
    Figure Legend Snippet: Photomicrograph of ~1 mm 2 area of a macaque retina that was retrogradely tracer labeled from injections of biotinylated rhodamine dextran in the superior colliculus and photostained in the in vitro retina. Following fixation the retina was processed for

    Techniques Used: Labeling, In Vitro

    Parasol cells project to the superior colliculus. A–E , Photomicrographs of parasol cells from the retinal periphery (eccentricity range: 10 – 11.5 mm) retrogradely labeled by injection of biotinylated rhodamine-dextran into the superior
    Figure Legend Snippet: Parasol cells project to the superior colliculus. A–E , Photomicrographs of parasol cells from the retinal periphery (eccentricity range: 10 – 11.5 mm) retrogradely labeled by injection of biotinylated rhodamine-dextran into the superior

    Techniques Used: Labeling, Injection

    Mosaic of neighboring parasol cells retrogradely stained from injections of biotinylated rhodamine dextran injections into the superior colliculus. A , Photomicrograph of two pairs of inner parasol cells with overlapping dendritic fields, at an eccentricity
    Figure Legend Snippet: Mosaic of neighboring parasol cells retrogradely stained from injections of biotinylated rhodamine dextran injections into the superior colliculus. A , Photomicrograph of two pairs of inner parasol cells with overlapping dendritic fields, at an eccentricity

    Techniques Used: Staining

    Photomicrographs of macaque brain sections showing injection of biotinylated rhodamine dextran confined to the superior colliculus. Sections are shown stacked consecutively from lower right to upper left covering ~1.2 mm distance. Orientation of stacked
    Figure Legend Snippet: Photomicrographs of macaque brain sections showing injection of biotinylated rhodamine dextran confined to the superior colliculus. Sections are shown stacked consecutively from lower right to upper left covering ~1.2 mm distance. Orientation of stacked

    Techniques Used: Injection

    3) Product Images from "Inflammatory Responses Are Not Sufficient to Cause Delayed Neuronal Death in ATP-Induced Acute Brain Injury"

    Article Title: Inflammatory Responses Are Not Sufficient to Cause Delayed Neuronal Death in ATP-Induced Acute Brain Injury

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0013756

    Death of dopaminergic neurons and microglia in the SNpc induced by ATP. ( A ) ATP (100 nmol in 2 µl PBS) or PBS (2 µl) was unilaterally injected into SNpc (*, injection sites), and brains were obtained after 3 h. Brain sections (30 µm thickness) of the midbrain including the entire SN were prepared, every sixth serial section selected and stained with TH (upper panel) and Iba-1 (lower panel) antibodies, and visualized with biotin-conjugated secondary antibodies and enzymatic detection with the avidin/biotin system unless indicated. At 100 nmol, mild neuronal and microglial damage occurred, thus, 100 nmol ATP was employed for in vivo experiments in this study. Photographs of the most damaged sections were obtained. The contralateral side (contra) and PBS-injected rat brain sections were used as control. ( B ) Serial sections obtained at 3 h were labeled with TH (left panel), Iba-1 (middle panel), and TH/Iba-1 (right panel) antibodies. For visualization of the double-labeling, color reactions using DAB (for TH) and DAB/nickel sulfate (for Iba-1) were applied. Dotted lines indicated damage areas. ( C ) Brain tissue obtained 3 h post ATP treatment was subjected to electron microscopy, as described in “ Materials and Methods ”. Nuclei of neuron (N, white arrow), astrocytes (A, white arrowhead), and microglia (M, black arrow) were shown in intact rat brain whereas cellular structures were severely disrupted in ATP-injected brain. Data in this study are representative of at least 5 animals. Scale bars, 200 µm (A); 100 µm (B); 5 µm (C).
    Figure Legend Snippet: Death of dopaminergic neurons and microglia in the SNpc induced by ATP. ( A ) ATP (100 nmol in 2 µl PBS) or PBS (2 µl) was unilaterally injected into SNpc (*, injection sites), and brains were obtained after 3 h. Brain sections (30 µm thickness) of the midbrain including the entire SN were prepared, every sixth serial section selected and stained with TH (upper panel) and Iba-1 (lower panel) antibodies, and visualized with biotin-conjugated secondary antibodies and enzymatic detection with the avidin/biotin system unless indicated. At 100 nmol, mild neuronal and microglial damage occurred, thus, 100 nmol ATP was employed for in vivo experiments in this study. Photographs of the most damaged sections were obtained. The contralateral side (contra) and PBS-injected rat brain sections were used as control. ( B ) Serial sections obtained at 3 h were labeled with TH (left panel), Iba-1 (middle panel), and TH/Iba-1 (right panel) antibodies. For visualization of the double-labeling, color reactions using DAB (for TH) and DAB/nickel sulfate (for Iba-1) were applied. Dotted lines indicated damage areas. ( C ) Brain tissue obtained 3 h post ATP treatment was subjected to electron microscopy, as described in “ Materials and Methods ”. Nuclei of neuron (N, white arrow), astrocytes (A, white arrowhead), and microglia (M, black arrow) were shown in intact rat brain whereas cellular structures were severely disrupted in ATP-injected brain. Data in this study are representative of at least 5 animals. Scale bars, 200 µm (A); 100 µm (B); 5 µm (C).

    Techniques Used: Injection, Staining, Avidin-Biotin Assay, In Vivo, Labeling, Electron Microscopy

    4) Product Images from "Physiological Modulation of Intestinal Motility by Enteric Dopaminergic Neurons and the D2 Receptor: Analysis of Dopamine Receptor Expression, Location, Development, and Function in Wild-Type and Knock-Out Mice"

    Article Title: Physiological Modulation of Intestinal Motility by Enteric Dopaminergic Neurons and the D2 Receptor: Analysis of Dopamine Receptor Expression, Location, Development, and Function in Wild-Type and Knock-Out Mice

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.4720-05.2006

    D 2 and D 3 immunocytochemistry were performed on the submucosal plexus of the ileum of CD-1 mice. The same tissue preparation from D 2 and D 3 KO mice was used as control. D 2 receptor immunoreactivity (IR) was revealed by a D 2 rabbit antibody and a donkey anti-rabbit Alexa 594 secondary antibody. D 3 receptor immunoreactivity was revealed by a D 3 goat antibody, a biotinylated donkey anti-goat secondary antibody, and streptavidin FITC. On the tissue of CD-1 mice, D 2 -immunoreactive products were present in the enteric neurons ( A ), and D 3 -immunoreactive products were also present in the enteric neurons ( B ). D 2 and D 3 immunoreactivities were colocalized in the same cell ( C ). However, D 2 immunoreactivity was not detected on the tissue of D 2 knock-out (KO) mice ( D ); no D 3 immunoreactivity was detected on the tissue of D 3 knock-out mouse ( E ). The arrows indicate the immunoreactive neurons. Scale bar: (in C ) 25 μm.
    Figure Legend Snippet: D 2 and D 3 immunocytochemistry were performed on the submucosal plexus of the ileum of CD-1 mice. The same tissue preparation from D 2 and D 3 KO mice was used as control. D 2 receptor immunoreactivity (IR) was revealed by a D 2 rabbit antibody and a donkey anti-rabbit Alexa 594 secondary antibody. D 3 receptor immunoreactivity was revealed by a D 3 goat antibody, a biotinylated donkey anti-goat secondary antibody, and streptavidin FITC. On the tissue of CD-1 mice, D 2 -immunoreactive products were present in the enteric neurons ( A ), and D 3 -immunoreactive products were also present in the enteric neurons ( B ). D 2 and D 3 immunoreactivities were colocalized in the same cell ( C ). However, D 2 immunoreactivity was not detected on the tissue of D 2 knock-out (KO) mice ( D ); no D 3 immunoreactivity was detected on the tissue of D 3 knock-out mouse ( E ). The arrows indicate the immunoreactive neurons. Scale bar: (in C ) 25 μm.

    Techniques Used: Immunocytochemistry, Mouse Assay, Knock-Out

    5) Product Images from "A regulated PNUTS mRNA to lncRNA splice switch mediates EMT and tumor progression"

    Article Title: A regulated PNUTS mRNA to lncRNA splice switch mediates EMT and tumor progression

    Journal: Nature cell biology

    doi: 10.1038/ncb3595

    PNUTS alternative splicing product is non-coding and interacts with miR-205 (a) Polysome fractionation experiment of A549 cells followed by RT-PCR analysis of PNUTS mRNA and lncRNA-PNUTS expression in each fraction. (b) RT-PCR analysis of PNUTS mRNA and lncRNA-PNUTS expression after the use of oligo-(dT) or random hexanucleotides as primers for initial reverse transcription reaction. (c) RT-PCR analysis of lncRNA-PNUTS expression in A549 cells. The total, cytoplasmic (Cyto.) and nuclear fractions are shown. PNUTS pre-RNA and PNUTS mRNA were used as endogenous controls to monitor the fractions purity. (d) Confocal microscopy imaging of subcellular localization of lncRNA-PNUTS using co-transfection of a MS2-tagged-RNA construct of lncRNA-PNUTS and a fused MS2-GFP protein construct. Scale bar: 5µM. (e) The exact copy numbers of lncRNA-PNUTS (basal levels or levels following activation by Actinomycin D treatment for 3h) and miR-205 were quantified with limiting-dilution qRT-PCR. Data are shown as mean ± s.d., n= 3 independent experiments per condition. Source data are available in Supplementary table 2 . (f) In silico prediction of MiR-205 binding sites located on lncRNA-PNUTS, obtained using the DIANA-microT web server. (g) Selective pull-down of either endogenous lncRNA-PNUTS or PNUTS-mRNA isoforms by using antisense biotinylated probes followed by miRNA-specific RT-PCR analysis to detect endogenously associated miR-205 with lncRNA-PNUTS in A549 cells. (h) MS2-RIP followed by miRNA-specific RT-PCR analysis to detect the association of miR-205 with lncRNA-PNUTS in NMuMG cells. LncRNA-PNUTS and GAPDH expression were used as internal controls. (i) A549 and NMUMG cell lysates incubated with in vitro transcribed biotin-labeled lncRNA-PNUTS were subjected to pull-down followed by miRNA extraction and analysis by RT-PCR. (j) A549 cells overexpressing lncRNA-PNUTS were transfected with an increasing concentration of a synthetic miR-205 mimic and the lncRNA expression was assessed by RT-PCR. ZEB-1 and CDH1 were used to monitor the efficiency of miR-205 overexpression on mesenchymal-epithelial transition (MET) process. (k) Time course experiment by using RT-PCR analysis of lncRNA-PNUTS levels upon addition of 10µg.mL −1 cycloheximide in A549 cells. GAPDH was used as a loading control.
    Figure Legend Snippet: PNUTS alternative splicing product is non-coding and interacts with miR-205 (a) Polysome fractionation experiment of A549 cells followed by RT-PCR analysis of PNUTS mRNA and lncRNA-PNUTS expression in each fraction. (b) RT-PCR analysis of PNUTS mRNA and lncRNA-PNUTS expression after the use of oligo-(dT) or random hexanucleotides as primers for initial reverse transcription reaction. (c) RT-PCR analysis of lncRNA-PNUTS expression in A549 cells. The total, cytoplasmic (Cyto.) and nuclear fractions are shown. PNUTS pre-RNA and PNUTS mRNA were used as endogenous controls to monitor the fractions purity. (d) Confocal microscopy imaging of subcellular localization of lncRNA-PNUTS using co-transfection of a MS2-tagged-RNA construct of lncRNA-PNUTS and a fused MS2-GFP protein construct. Scale bar: 5µM. (e) The exact copy numbers of lncRNA-PNUTS (basal levels or levels following activation by Actinomycin D treatment for 3h) and miR-205 were quantified with limiting-dilution qRT-PCR. Data are shown as mean ± s.d., n= 3 independent experiments per condition. Source data are available in Supplementary table 2 . (f) In silico prediction of MiR-205 binding sites located on lncRNA-PNUTS, obtained using the DIANA-microT web server. (g) Selective pull-down of either endogenous lncRNA-PNUTS or PNUTS-mRNA isoforms by using antisense biotinylated probes followed by miRNA-specific RT-PCR analysis to detect endogenously associated miR-205 with lncRNA-PNUTS in A549 cells. (h) MS2-RIP followed by miRNA-specific RT-PCR analysis to detect the association of miR-205 with lncRNA-PNUTS in NMuMG cells. LncRNA-PNUTS and GAPDH expression were used as internal controls. (i) A549 and NMUMG cell lysates incubated with in vitro transcribed biotin-labeled lncRNA-PNUTS were subjected to pull-down followed by miRNA extraction and analysis by RT-PCR. (j) A549 cells overexpressing lncRNA-PNUTS were transfected with an increasing concentration of a synthetic miR-205 mimic and the lncRNA expression was assessed by RT-PCR. ZEB-1 and CDH1 were used to monitor the efficiency of miR-205 overexpression on mesenchymal-epithelial transition (MET) process. (k) Time course experiment by using RT-PCR analysis of lncRNA-PNUTS levels upon addition of 10µg.mL −1 cycloheximide in A549 cells. GAPDH was used as a loading control.

    Techniques Used: Fractionation, Reverse Transcription Polymerase Chain Reaction, Expressing, Confocal Microscopy, Imaging, Cotransfection, Construct, Activation Assay, Quantitative RT-PCR, In Silico, Binding Assay, Incubation, In Vitro, Labeling, Transfection, Concentration Assay, Over Expression

    6) Product Images from "Increased Epitope-Specific CD8+ T Cells Prevent Murine Coronavirus Spread to the Spinal Cord and Subsequent Demyelination"

    Article Title: Increased Epitope-Specific CD8+ T Cells Prevent Murine Coronavirus Spread to the Spinal Cord and Subsequent Demyelination

    Journal:

    doi: 10.1128/JVI.79.6.3370-3381.2005

    Antigen spread in brains of RA59-gfp/gp33-infected mice receiving virus-specific CD8 + T cells. Brain samples from mice were preserved in formalin, embedded in paraffin, and sectioned sagittally. Sections were stained by an avidin-biotin immunoperoxidase
    Figure Legend Snippet: Antigen spread in brains of RA59-gfp/gp33-infected mice receiving virus-specific CD8 + T cells. Brain samples from mice were preserved in formalin, embedded in paraffin, and sectioned sagittally. Sections were stained by an avidin-biotin immunoperoxidase

    Techniques Used: Infection, Mouse Assay, Staining, Avidin-Biotin Assay

    7) Product Images from "Anti-GRP78 autoantibodies induce endothelial cell activation and accelerate the development of atherosclerotic lesions"

    Article Title: Anti-GRP78 autoantibodies induce endothelial cell activation and accelerate the development of atherosclerotic lesions

    Journal: JCI Insight

    doi: 10.1172/jci.insight.99363

    ER stress causes an increase in csGRP78 levels on ECs. HAECs were treated with ( A ) 2.5 μg/ml Tm or ( B ) 300 nM Tg for the indicated time period or with ( C ) 7-ketocholesterol (7KC), Sin-1, 4-hydroxynonenal (4HNE), or peroxynitrite (Peroxy) for 8 hours, after which surface proteins were biotinylated and separated by streptavidin pull down. Total cell lysates (tGRP78) and surface protein fractions (sGRP78) were subjected to Western blotting for detection of GRP78, the EC marker CD31, IRE1α, or phospho-eIF1α. Blots were also immunostained for β actin as a protein loading control. Densitometry quantification is indicated under each band relative to untreated cells and normalized to β-actin.
    Figure Legend Snippet: ER stress causes an increase in csGRP78 levels on ECs. HAECs were treated with ( A ) 2.5 μg/ml Tm or ( B ) 300 nM Tg for the indicated time period or with ( C ) 7-ketocholesterol (7KC), Sin-1, 4-hydroxynonenal (4HNE), or peroxynitrite (Peroxy) for 8 hours, after which surface proteins were biotinylated and separated by streptavidin pull down. Total cell lysates (tGRP78) and surface protein fractions (sGRP78) were subjected to Western blotting for detection of GRP78, the EC marker CD31, IRE1α, or phospho-eIF1α. Blots were also immunostained for β actin as a protein loading control. Densitometry quantification is indicated under each band relative to untreated cells and normalized to β-actin.

    Techniques Used: Western Blot, Marker

    8) Product Images from "Region-specific astrogliosis: differential vessel formation contributes to different patterns of astrogliosis in the cortex and striatum"

    Article Title: Region-specific astrogliosis: differential vessel formation contributes to different patterns of astrogliosis in the cortex and striatum

    Journal: Molecular Brain

    doi: 10.1186/s13041-020-00642-0

    Avastin attenuates astrogliosis and blood vessel formation in the injured cortex. a, c Cortical sections were obtained from mice in which Avastin or PBS was infused into the ventricle 14 d post-ATP injection. GFAP and CoL1A1 were visualized with Alexa-488 and Alexa-594 conjugated secondary antibodies ( a ) or biotinylated secondary antibodies and DAB-based color reaction ( c ). b Relative fluorescence intensity of GFAP and CoL1A1 were measured using ZEN software and plotted. Values are means ± SEMs for animals treated with saline ( n = 4) or Avastin ( n = 3) (*, p
    Figure Legend Snippet: Avastin attenuates astrogliosis and blood vessel formation in the injured cortex. a, c Cortical sections were obtained from mice in which Avastin or PBS was infused into the ventricle 14 d post-ATP injection. GFAP and CoL1A1 were visualized with Alexa-488 and Alexa-594 conjugated secondary antibodies ( a ) or biotinylated secondary antibodies and DAB-based color reaction ( c ). b Relative fluorescence intensity of GFAP and CoL1A1 were measured using ZEN software and plotted. Values are means ± SEMs for animals treated with saline ( n = 4) or Avastin ( n = 3) (*, p

    Techniques Used: Mouse Assay, Injection, Fluorescence, Software

    9) Product Images from "Application of protein lysate microarrays to molecular marker verification and quantification"

    Article Title: Application of protein lysate microarrays to molecular marker verification and quantification

    Journal: Proteome Science

    doi: 10.1186/1477-5956-3-9

    Schematic of the different binding steps on LMA. F9 lysates or purified p53 protein, purified primary p53 antibody, biotinylated secondary antibody, and Cy3-labeled streptavidin were printed on spots i, ii, iii and iv on the LMA, respectively. A diagrammatic representation of the different binding steps performed for signal detection on LMA is shown.
    Figure Legend Snippet: Schematic of the different binding steps on LMA. F9 lysates or purified p53 protein, purified primary p53 antibody, biotinylated secondary antibody, and Cy3-labeled streptavidin were printed on spots i, ii, iii and iv on the LMA, respectively. A diagrammatic representation of the different binding steps performed for signal detection on LMA is shown.

    Techniques Used: Binding Assay, Purification, Labeling

    Linearity of different binding steps on LMA. LMA containing serially diluted F9 protein lysates (0.055, 0.11, 0.23, 0.46, 0.92, 1.84, 3.68 and 7.36 ng), purified p53 protein (1.5, 3, 6, 12, 24, 48, 96 and 192 pg), purified primary antibody (1.5, 3, 6, 12, 24, 48, 96 and 192 pg), biotinylated secondary antibody (11.5, 23, 46, 92, 184, 368, 736 and 1472 pg) and Cy3-labeled streptavidin (1.95, 3.9, 7.8, 15.6, 31.2, 62.4, 124.8 and 249.6 ng) were printed. Arrays were probed with p53 antibody followed by binding and labeling steps as described in the Methods. Log transformed (base 2) spotted lysate amount was plotted against log transformed (base 2) signal intensity.
    Figure Legend Snippet: Linearity of different binding steps on LMA. LMA containing serially diluted F9 protein lysates (0.055, 0.11, 0.23, 0.46, 0.92, 1.84, 3.68 and 7.36 ng), purified p53 protein (1.5, 3, 6, 12, 24, 48, 96 and 192 pg), purified primary antibody (1.5, 3, 6, 12, 24, 48, 96 and 192 pg), biotinylated secondary antibody (11.5, 23, 46, 92, 184, 368, 736 and 1472 pg) and Cy3-labeled streptavidin (1.95, 3.9, 7.8, 15.6, 31.2, 62.4, 124.8 and 249.6 ng) were printed. Arrays were probed with p53 antibody followed by binding and labeling steps as described in the Methods. Log transformed (base 2) spotted lysate amount was plotted against log transformed (base 2) signal intensity.

    Techniques Used: Binding Assay, Purification, Labeling, Transformation Assay

    10) Product Images from "Age-related increases in ozone-induced injury and altered pulmonary mechanics in mice with progressive lung inflammation"

    Article Title: Age-related increases in ozone-induced injury and altered pulmonary mechanics in mice with progressive lung inflammation

    Journal: American Journal of Physiology - Lung Cellular and Molecular Physiology

    doi: 10.1152/ajplung.00027.2013

    Expression of heme oxygenase-1 (HO-1) in WT and Sftpd −/− mice. Lung sections, prepared 72 h after exposure of 8-, 27-, and 80-wk-old WT and Sftpd −/− mice to air or ozone, were stained with antibody to HO-1 or IgG control followed by biotinylated secondary antibody. Binding was visualized by use of a peroxidase substrate DAB kit. One representative section from 3 separate experiments is shown ( n = 3 mice/treatment group). Original magnification, ×600.
    Figure Legend Snippet: Expression of heme oxygenase-1 (HO-1) in WT and Sftpd −/− mice. Lung sections, prepared 72 h after exposure of 8-, 27-, and 80-wk-old WT and Sftpd −/− mice to air or ozone, were stained with antibody to HO-1 or IgG control followed by biotinylated secondary antibody. Binding was visualized by use of a peroxidase substrate DAB kit. One representative section from 3 separate experiments is shown ( n = 3 mice/treatment group). Original magnification, ×600.

    Techniques Used: Expressing, Mouse Assay, Staining, Binding Assay

    Expression of mannose receptor in WT and Sftpd −/− mice. Lung sections, prepared 72 h after exposure of 8-, 27-, and 80-wk-old WT and Sftpd −/− mice to air or ozone, were stained with antibody to mannose receptor or IgG control followed by biotinylated secondary antibody. Binding was visualized by use of a peroxidase substrate DAB kit. One representative section from 3 separate experiments is shown ( n = 3 mice/treatment group). Original magnification, ×600.
    Figure Legend Snippet: Expression of mannose receptor in WT and Sftpd −/− mice. Lung sections, prepared 72 h after exposure of 8-, 27-, and 80-wk-old WT and Sftpd −/− mice to air or ozone, were stained with antibody to mannose receptor or IgG control followed by biotinylated secondary antibody. Binding was visualized by use of a peroxidase substrate DAB kit. One representative section from 3 separate experiments is shown ( n = 3 mice/treatment group). Original magnification, ×600.

    Techniques Used: Expressing, Mouse Assay, Staining, Binding Assay

    Expression of YM-1 in WT and Sftpd −/− mice. Lung sections, prepared 72 h after exposure of 8-, 27-, and 80-wk-old WT and Sftpd −/− mice to air or ozone, were stained with antibody to YM-1 or IgG control followed by biotinylated secondary antibody. Binding was visualized by use of a peroxidase substrate DAB kit. One representative section from 3 separate experiments is shown ( n = 3 mice/treatment group). Original magnification, ×600.
    Figure Legend Snippet: Expression of YM-1 in WT and Sftpd −/− mice. Lung sections, prepared 72 h after exposure of 8-, 27-, and 80-wk-old WT and Sftpd −/− mice to air or ozone, were stained with antibody to YM-1 or IgG control followed by biotinylated secondary antibody. Binding was visualized by use of a peroxidase substrate DAB kit. One representative section from 3 separate experiments is shown ( n = 3 mice/treatment group). Original magnification, ×600.

    Techniques Used: Expressing, Mouse Assay, Staining, Binding Assay

    Expression of galectin-3 in WT and Sftpd −/− mice. Lung sections, prepared 72 h after exposure of 8-, 27-, and 80-wk-old WT and Sftpd −/− mice to air or ozone, were stained with antibody to galectin-3 or IgG control followed by biotinylated secondary antibody. Binding was visualized by use of a peroxidase substrate DAB kit. One representative section from 3 separate experiments is shown ( n = 3 mice/treatment group). Original magnification, ×600.
    Figure Legend Snippet: Expression of galectin-3 in WT and Sftpd −/− mice. Lung sections, prepared 72 h after exposure of 8-, 27-, and 80-wk-old WT and Sftpd −/− mice to air or ozone, were stained with antibody to galectin-3 or IgG control followed by biotinylated secondary antibody. Binding was visualized by use of a peroxidase substrate DAB kit. One representative section from 3 separate experiments is shown ( n = 3 mice/treatment group). Original magnification, ×600.

    Techniques Used: Expressing, Mouse Assay, Staining, Binding Assay

    Expression of pro-surfactant protein C (SP-C) in WT and Sftpd −/− mice. Lung sections, prepared 72 h after exposure of 8-, 27-, and 80-wk-old WT and Sftpd −/− mice to air or ozone, were stained with antibody to pro-SP-C or IgG control followed by biotinylated secondary antibody. Binding was visualized by use of a peroxidase substrate DAB kit. One representative section from 3 separate experiments is shown ( n = 3 mice/treatment group). Arrowheads indicate insets. Original magnification, ×600; inset, ×1,000.
    Figure Legend Snippet: Expression of pro-surfactant protein C (SP-C) in WT and Sftpd −/− mice. Lung sections, prepared 72 h after exposure of 8-, 27-, and 80-wk-old WT and Sftpd −/− mice to air or ozone, were stained with antibody to pro-SP-C or IgG control followed by biotinylated secondary antibody. Binding was visualized by use of a peroxidase substrate DAB kit. One representative section from 3 separate experiments is shown ( n = 3 mice/treatment group). Arrowheads indicate insets. Original magnification, ×600; inset, ×1,000.

    Techniques Used: Expressing, Mouse Assay, Staining, Binding Assay

    Expression of inducible nitric oxide synthase (iNOS) in WT and Sftpd −/− mice. Lung sections, prepared 72 h after exposure of 8-, 27-, and 80-wk-old WT and Sftpd −/− mice to air or ozone, were stained with antibody to iNOS or IgG control followed by biotinylated secondary antibody. Binding was visualized by use of a peroxidase substrate DAB kit. One representative section from 3 separate experiments is shown ( n = 3 mice/treatment group). Original magnification, ×600.
    Figure Legend Snippet: Expression of inducible nitric oxide synthase (iNOS) in WT and Sftpd −/− mice. Lung sections, prepared 72 h after exposure of 8-, 27-, and 80-wk-old WT and Sftpd −/− mice to air or ozone, were stained with antibody to iNOS or IgG control followed by biotinylated secondary antibody. Binding was visualized by use of a peroxidase substrate DAB kit. One representative section from 3 separate experiments is shown ( n = 3 mice/treatment group). Original magnification, ×600.

    Techniques Used: Expressing, Mouse Assay, Staining, Binding Assay

    11) Product Images from "Altered expression of claudin family proteins in Alzheimer’s disease and vascular dementia brains"

    Article Title: Altered expression of claudin family proteins in Alzheimer’s disease and vascular dementia brains

    Journal: Journal of Cellular and Molecular Medicine

    doi: 10.1111/j.1582-4934.2009.00999.x

    Expression of Cl-2, Cl-5 and Cl-11 in astrocytes in control (CON), AD and VaD brains, in the frontal cortex, Brodmann area 46/9. Cl-expressing cells are brownish, as a result of the immunohistochemical staining method with anti-Cl sera detected with avidin–biotin-peroxidase complex kit and DAB substrate. Astrocytes are indicated by arrows. Bars: 5 μm.
    Figure Legend Snippet: Expression of Cl-2, Cl-5 and Cl-11 in astrocytes in control (CON), AD and VaD brains, in the frontal cortex, Brodmann area 46/9. Cl-expressing cells are brownish, as a result of the immunohistochemical staining method with anti-Cl sera detected with avidin–biotin-peroxidase complex kit and DAB substrate. Astrocytes are indicated by arrows. Bars: 5 μm.

    Techniques Used: Expressing, Immunohistochemistry, Staining, Avidin-Biotin Assay

    Expression of Cl-2, Cl-5 and Cl-11 in control (CON), AD and VaD brains, in the frontal cortex, Brodmann area 46/9. Cl-expressing cells are brownish, as a result of the immunohistochemical staining method with anti-Cl sera detected with avidin–biotin-peroxidase complex kit and DAB substrate. Expression of Cl-2, Cl-5 and Cl-11 was increased in neurons and neuronal fibres in AD and VaD brains, as compared to control brains. Expression of Cls was noticed mainly in the pyramidal neurons in CON, AD and VaD. Arrows are indicating Cl-expressing neurons. Bars: 30 μm.
    Figure Legend Snippet: Expression of Cl-2, Cl-5 and Cl-11 in control (CON), AD and VaD brains, in the frontal cortex, Brodmann area 46/9. Cl-expressing cells are brownish, as a result of the immunohistochemical staining method with anti-Cl sera detected with avidin–biotin-peroxidase complex kit and DAB substrate. Expression of Cl-2, Cl-5 and Cl-11 was increased in neurons and neuronal fibres in AD and VaD brains, as compared to control brains. Expression of Cls was noticed mainly in the pyramidal neurons in CON, AD and VaD. Arrows are indicating Cl-expressing neurons. Bars: 30 μm.

    Techniques Used: Expressing, Immunohistochemistry, Staining, Avidin-Biotin Assay

    Expression of Cl-2, Cl-5 and Cl-11 in oligodendrocytes in control (CON), AD and VaD brains, in the frontal cortex, Brodmann area 46/9. Cl-expressing cells are brownish, as a result of the immunohistochemical staining method with anti-Cl sera detected with avidin–biotin-peroxidase complex kit and DAB substrate. Oligodendrocytes are indicated by arrows. Bars: 5 μm.
    Figure Legend Snippet: Expression of Cl-2, Cl-5 and Cl-11 in oligodendrocytes in control (CON), AD and VaD brains, in the frontal cortex, Brodmann area 46/9. Cl-expressing cells are brownish, as a result of the immunohistochemical staining method with anti-Cl sera detected with avidin–biotin-peroxidase complex kit and DAB substrate. Oligodendrocytes are indicated by arrows. Bars: 5 μm.

    Techniques Used: Expressing, Immunohistochemistry, Staining, Avidin-Biotin Assay

    Expression of Cl-2, Cl-5 and Cl-11 in brain microvessels in control (CON), AD and VaD brains, in the frontal cortex, Brodmann area 46/9. Cl-expressing cells are brownish, as a result of the immunohistochemical staining method with anti-Cl sera detected with avidin–biotin-peroxidase complex kit and DAB substrate. Endothelial cells expressing Cl-2, Cl-5 or Cl-11 are indicated by arrows. Bars: 5 μm.
    Figure Legend Snippet: Expression of Cl-2, Cl-5 and Cl-11 in brain microvessels in control (CON), AD and VaD brains, in the frontal cortex, Brodmann area 46/9. Cl-expressing cells are brownish, as a result of the immunohistochemical staining method with anti-Cl sera detected with avidin–biotin-peroxidase complex kit and DAB substrate. Endothelial cells expressing Cl-2, Cl-5 or Cl-11 are indicated by arrows. Bars: 5 μm.

    Techniques Used: Expressing, Immunohistochemistry, Staining, Avidin-Biotin Assay

    12) Product Images from "Canine adenovirus type 1 causing neurological signs in a 5-week-old puppy"

    Article Title: Canine adenovirus type 1 causing neurological signs in a 5-week-old puppy

    Journal: BMC Veterinary Research

    doi: 10.1186/s12917-019-2173-5

    Endothelial cells in the brain with positive immunoreactivity for adenovirus. Strong intracytoplasmic and intranuclear staining. Avidin-Biotin immunoperoxidase. Bar = 50.0 μm
    Figure Legend Snippet: Endothelial cells in the brain with positive immunoreactivity for adenovirus. Strong intracytoplasmic and intranuclear staining. Avidin-Biotin immunoperoxidase. Bar = 50.0 μm

    Techniques Used: Staining, Avidin-Biotin Assay

    13) Product Images from "p75NTR Mediates Neurotrophin-Induced Apoptosis of Vascular Smooth Muscle Cells"

    Article Title: p75NTR Mediates Neurotrophin-Induced Apoptosis of Vascular Smooth Muscle Cells

    Journal: The American Journal of Pathology

    doi:

    Immunohistochemical analysis of p75 NTR in vascular lesions of the rat thoracic aorta 2 weeks after balloon de-endothelialization. Sections of rat thoracic aorta from either control animals ( A and B ), or 5 ( C and D ) and 14 days ( E and F ) after balloon de-endothelialization were incubated with the indicated antibodies. Immunoreactive proteins were visualized using avidin-biotin-based horseradish peroxidase kit using Vector VIP as a chromogenic substrate; the sections were counterstained with hematoxylin. Original magnification, ×90.
    Figure Legend Snippet: Immunohistochemical analysis of p75 NTR in vascular lesions of the rat thoracic aorta 2 weeks after balloon de-endothelialization. Sections of rat thoracic aorta from either control animals ( A and B ), or 5 ( C and D ) and 14 days ( E and F ) after balloon de-endothelialization were incubated with the indicated antibodies. Immunoreactive proteins were visualized using avidin-biotin-based horseradish peroxidase kit using Vector VIP as a chromogenic substrate; the sections were counterstained with hematoxylin. Original magnification, ×90.

    Techniques Used: Immunohistochemistry, Incubation, Avidin-Biotin Assay, Plasmid Preparation

    14) Product Images from "Effects of hepatitis B virus infection on human sperm chromosomes"

    Article Title: Effects of hepatitis B virus infection on human sperm chromosomes

    Journal: World Journal of Gastroenterology : WJG

    doi: 10.3748/wjg.v9.i4.736

    Detection of HBV DNA sequences in sperm chromo-somes by FISH with biotinylated whole length HBV DNA probe: (A) a well separated chromosome plate from one pa-tient (subject 6) with chronic persistent hepatitis, with three fluorescent signals on different chromosomes; (B) a poorly sepa-rated chromosome plate from the same patient with five fluo-rescent signals.
    Figure Legend Snippet: Detection of HBV DNA sequences in sperm chromo-somes by FISH with biotinylated whole length HBV DNA probe: (A) a well separated chromosome plate from one pa-tient (subject 6) with chronic persistent hepatitis, with three fluorescent signals on different chromosomes; (B) a poorly sepa-rated chromosome plate from the same patient with five fluo-rescent signals.

    Techniques Used: Fluorescence In Situ Hybridization

    15) Product Images from "Callosal connections of dorsal versus ventral premotor areas in the macaque monkey: a multiple retrograde tracing study"

    Article Title: Callosal connections of dorsal versus ventral premotor areas in the macaque monkey: a multiple retrograde tracing study

    Journal: BMC Neuroscience

    doi: 10.1186/1471-2202-6-67

    Frontal sections of the right hemisphere of Mk1, arranged from rostral to caudal with increasing ID# (10 to 54), showing the distribution of retrogradely labelled neurons as a result of tracers injections in the opposite PMd-r (red dots), PMv-r (grey dots), PMd-c (blue dots) and PMv-c (green dots). The tracers used are indicated in the bottom right. Tracers : biotinylated dextran amine (BDA), diamidino yellow (DY), fast blue (FB), cholera-toxin B subunit (CB). See list of abbreviations.
    Figure Legend Snippet: Frontal sections of the right hemisphere of Mk1, arranged from rostral to caudal with increasing ID# (10 to 54), showing the distribution of retrogradely labelled neurons as a result of tracers injections in the opposite PMd-r (red dots), PMv-r (grey dots), PMd-c (blue dots) and PMv-c (green dots). The tracers used are indicated in the bottom right. Tracers : biotinylated dextran amine (BDA), diamidino yellow (DY), fast blue (FB), cholera-toxin B subunit (CB). See list of abbreviations.

    Techniques Used:

    Reconstruction of the injection sites on a lateral view of the left hemisphere of the 8 monkeys included in the present study. Tracers : biotinylated dextran amine (BDA), diamidino yellow (DY), fast blue (FB), fluoro ruby (FR), cholera-toxin B subunit (CB). For other abbreviations, see Fig. 1.
    Figure Legend Snippet: Reconstruction of the injection sites on a lateral view of the left hemisphere of the 8 monkeys included in the present study. Tracers : biotinylated dextran amine (BDA), diamidino yellow (DY), fast blue (FB), fluoro ruby (FR), cholera-toxin B subunit (CB). For other abbreviations, see Fig. 1.

    Techniques Used: Injection

    16) Product Images from "Taurine Attenuates Carcinogenicity in Ulcerative Colitis-Colorectal Cancer Mouse Model"

    Article Title: Taurine Attenuates Carcinogenicity in Ulcerative Colitis-Colorectal Cancer Mouse Model

    Journal: Oxidative Medicine and Cellular Longevity

    doi: 10.1155/2020/7935917

    Immunohistochemistry of (a) Ki-67 and (b) PTEN and western blot analysis of (c) cleaved caspase-9. The expression of Ki-67 and PTEN was assessed by avidin-biotin kits with peroxidase-based detection (brown). Nuclei were counterstained with hematoxylin. Original magnifications 100x. (c) Western blot image and relative intensity of cleaved caspase-9 adjusted by β -actin. Graphs represent the average score (bar; SD) of (a) Ki-67 score, (b) PTEN score, (c) cleaved caspase-9. # P
    Figure Legend Snippet: Immunohistochemistry of (a) Ki-67 and (b) PTEN and western blot analysis of (c) cleaved caspase-9. The expression of Ki-67 and PTEN was assessed by avidin-biotin kits with peroxidase-based detection (brown). Nuclei were counterstained with hematoxylin. Original magnifications 100x. (c) Western blot image and relative intensity of cleaved caspase-9 adjusted by β -actin. Graphs represent the average score (bar; SD) of (a) Ki-67 score, (b) PTEN score, (c) cleaved caspase-9. # P

    Techniques Used: Immunohistochemistry, Western Blot, Expressing, Avidin-Biotin Assay

    17) Product Images from "Resistin decreases expression of endothelial nitric oxide synthase through oxidative stress in human coronary artery endothelial cells"

    Article Title: Resistin decreases expression of endothelial nitric oxide synthase through oxidative stress in human coronary artery endothelial cells

    Journal: American Journal of Physiology - Heart and Circulatory Physiology

    doi: 10.1152/ajpheart.00431.2009

    Resistin immunoreactivity of human atherosclerotic and nonatherosclerotic arteries. Human aorta and carotid arteries were fixed in formalin and embedded in paraffin. Immunostaining was performed by using the anti-human resistin antibody (1:200), biotinylated
    Figure Legend Snippet: Resistin immunoreactivity of human atherosclerotic and nonatherosclerotic arteries. Human aorta and carotid arteries were fixed in formalin and embedded in paraffin. Immunostaining was performed by using the anti-human resistin antibody (1:200), biotinylated

    Techniques Used: Immunostaining

    18) Product Images from "Synergistic effect of therapeutic stem cells expressing cytosine deaminase and interferon-beta via apoptotic pathway in the metastatic mouse model of breast cancer"

    Article Title: Synergistic effect of therapeutic stem cells expressing cytosine deaminase and interferon-beta via apoptotic pathway in the metastatic mouse model of breast cancer

    Journal: Oncotarget

    doi: 10.18632/oncotarget.6719

    Hematoxylin and eosin (H E) staining and PCNA expression level in metastatic breast cancer models Excised brains were fixed in 4% normal formalin and embedded in paraffin. After being cut with a microtome, slides were deparaffined and rehydrated with xylene, ethanol, and tap water. ( A ) H E staining. ( B ) Immunohistochemistry (IHC) staining for PCNA. To confirm the proliferation rate of tumor cells, brain sections were treated with the primary antibody, anti-mouse PCNA. Next, the slide was incubated with biotinylated anti-mouse secondary antibody and stained protein (brown color) was observed following DAB and hematoxylin staining. Dotted line: necrosis or apoptosis area of tumor cells in the brain section. Magnification ×100, ×200.
    Figure Legend Snippet: Hematoxylin and eosin (H E) staining and PCNA expression level in metastatic breast cancer models Excised brains were fixed in 4% normal formalin and embedded in paraffin. After being cut with a microtome, slides were deparaffined and rehydrated with xylene, ethanol, and tap water. ( A ) H E staining. ( B ) Immunohistochemistry (IHC) staining for PCNA. To confirm the proliferation rate of tumor cells, brain sections were treated with the primary antibody, anti-mouse PCNA. Next, the slide was incubated with biotinylated anti-mouse secondary antibody and stained protein (brown color) was observed following DAB and hematoxylin staining. Dotted line: necrosis or apoptosis area of tumor cells in the brain section. Magnification ×100, ×200.

    Techniques Used: Staining, Expressing, Immunohistochemistry, Incubation

    19) Product Images from "New insights into saccular development and vascular formation in lung allografts under the renal capsule"

    Article Title: New insights into saccular development and vascular formation in lung allografts under the renal capsule

    Journal: Mechanisms of development

    doi:

    Lung graft vessels are endogenous to the grafts but are connected to host vessels. (A,B) β-Galactosidase staining of lung graft (A) and kidney (B) sections from wild-type lung rudiments that were grafted into KDR.LacZ mice for 8 days. Host endothelial cells in the glomerular tufts (arrow) and between the tubules (arrowhead) in the host kidney stain positive (blue) for β-galactosidase activity (B), but there are no host endothelial cells in the graft (A). (C) Intravenous perfusion of biotinylated lectin into the host shows that vessels in the 8-day lung grafts are connected to the host circulation, as evidenced by lectin staining of both large vessel (arrow) and capillaries (arrowhead) in the grafts. (D,E) Intravenous perfusion of biotinylated lectin into the host after 4 days (D) and 6 days (E) of grafting shows dot-like areas of lectin staining (arrows) within the mesenchyme of the lung grafts at 4 days, and lectin staining of larger caliber vessels (arrows), but no staining of capillaries in the mesenchyme (arrowheads) at 6 days. Bar: 50 μm.
    Figure Legend Snippet: Lung graft vessels are endogenous to the grafts but are connected to host vessels. (A,B) β-Galactosidase staining of lung graft (A) and kidney (B) sections from wild-type lung rudiments that were grafted into KDR.LacZ mice for 8 days. Host endothelial cells in the glomerular tufts (arrow) and between the tubules (arrowhead) in the host kidney stain positive (blue) for β-galactosidase activity (B), but there are no host endothelial cells in the graft (A). (C) Intravenous perfusion of biotinylated lectin into the host shows that vessels in the 8-day lung grafts are connected to the host circulation, as evidenced by lectin staining of both large vessel (arrow) and capillaries (arrowhead) in the grafts. (D,E) Intravenous perfusion of biotinylated lectin into the host after 4 days (D) and 6 days (E) of grafting shows dot-like areas of lectin staining (arrows) within the mesenchyme of the lung grafts at 4 days, and lectin staining of larger caliber vessels (arrows), but no staining of capillaries in the mesenchyme (arrowheads) at 6 days. Bar: 50 μm.

    Techniques Used: Staining, Mouse Assay, Activity Assay

    20) Product Images from "Machine-based method for multiplex in situ molecular characterization of tissues by immunofluorescence detection"

    Article Title: Machine-based method for multiplex in situ molecular characterization of tissues by immunofluorescence detection

    Journal: Scientific Reports

    doi: 10.1038/srep09534

    CD31 expression detected with different detection systems. Paraformaldehyde fixed, paraffin embedded 5 μm sections of E13.5 mouse embryo were stained with CD31 primary antibody (see Methods for details) and nuclei were stained with DAPI. Panel A shows detection with biotinylated goat anti-rat secondary antibodies followed by Streptavidin-HRP and TSA- Alexa488 amplification. Panel B shows detection with goat anti-rat secondary antibodies directly conjugated with Alexa488. Panel C shows detection with biotinylated goat anti-rat antibodies followed by Streptavidin-Alexa488. Panel D shows staining with isotype control IgG detected with biotinylated goat anti-rat antibodies, followed by Streptavidin-HRP and TSA-Alexa488. The inset in each panel represents a closer view of the indicated region, with CD31 signal showing in grayscale. White arrows point to autofluorescence emitted by the eurethrocytes, which persists in all staining methods.
    Figure Legend Snippet: CD31 expression detected with different detection systems. Paraformaldehyde fixed, paraffin embedded 5 μm sections of E13.5 mouse embryo were stained with CD31 primary antibody (see Methods for details) and nuclei were stained with DAPI. Panel A shows detection with biotinylated goat anti-rat secondary antibodies followed by Streptavidin-HRP and TSA- Alexa488 amplification. Panel B shows detection with goat anti-rat secondary antibodies directly conjugated with Alexa488. Panel C shows detection with biotinylated goat anti-rat antibodies followed by Streptavidin-Alexa488. Panel D shows staining with isotype control IgG detected with biotinylated goat anti-rat antibodies, followed by Streptavidin-HRP and TSA-Alexa488. The inset in each panel represents a closer view of the indicated region, with CD31 signal showing in grayscale. White arrows point to autofluorescence emitted by the eurethrocytes, which persists in all staining methods.

    Techniques Used: Expressing, Staining, Amplification

    21) Product Images from "Expression of Fas (CD95/APO-1) Ligand by Human Breast Cancers: Significance for Tumor Immune Privilege"

    Article Title: Expression of Fas (CD95/APO-1) Ligand by Human Breast Cancers: Significance for Tumor Immune Privilege

    Journal: Clinical and Diagnostic Laboratory Immunology

    doi:

    Human breast carcinomas express FasL. Immunoperoxidase staining with a FasL-specific rabbit polyclonal IgG antibody (FasL Ab) was performed with paraffin-embedded breast carcinoma sections. Slides were counterstained with hematoxylin. FasL-positive immunohistochemical staining (brown) is shown in a representative breast carcinoma (magnification, ×80). In addition to positive staining of the tumor island (open arrow), positive staining is also observed among isolated cells of lymphoid morphology (solid arrow), possibly representing FasL-expressing, activated T and NK cells. As a control for specificity of antibody detection, the FasL-immunizing peptide was included during primary antibody incubation (Ab control). Competitive displacement of staining by the soluble peptide immunogen confirms FasL specificity. Breast tumor expression of FasL mRNA was detected by in situ hybridization with a biotinylated FasL-specific riboprobe (FasL ISH). A positive brown hybridization signal is seen within a representative tumor island (open arrow) (magnification, ×80). FasL mRNA was also detected in cells within a lymphoid aggregate (solid arrow). In control sections for in situ hybridization (ISH control), the biotinylated sense control probe failed to hybridize, confirming the specificity of the FasL hybridization. These results are representative of 17 breast carcinomas.
    Figure Legend Snippet: Human breast carcinomas express FasL. Immunoperoxidase staining with a FasL-specific rabbit polyclonal IgG antibody (FasL Ab) was performed with paraffin-embedded breast carcinoma sections. Slides were counterstained with hematoxylin. FasL-positive immunohistochemical staining (brown) is shown in a representative breast carcinoma (magnification, ×80). In addition to positive staining of the tumor island (open arrow), positive staining is also observed among isolated cells of lymphoid morphology (solid arrow), possibly representing FasL-expressing, activated T and NK cells. As a control for specificity of antibody detection, the FasL-immunizing peptide was included during primary antibody incubation (Ab control). Competitive displacement of staining by the soluble peptide immunogen confirms FasL specificity. Breast tumor expression of FasL mRNA was detected by in situ hybridization with a biotinylated FasL-specific riboprobe (FasL ISH). A positive brown hybridization signal is seen within a representative tumor island (open arrow) (magnification, ×80). FasL mRNA was also detected in cells within a lymphoid aggregate (solid arrow). In control sections for in situ hybridization (ISH control), the biotinylated sense control probe failed to hybridize, confirming the specificity of the FasL hybridization. These results are representative of 17 breast carcinomas.

    Techniques Used: Immunoperoxidase Staining, Immunohistochemistry, Staining, Isolation, Expressing, Incubation, In Situ Hybridization, Hybridization

    22) Product Images from "Expression of Insulin-Like Growth Factor 2 Receptor in Corneal Keratocytes During Differentiation and in Response to Wound Healing"

    Article Title: Expression of Insulin-Like Growth Factor 2 Receptor in Corneal Keratocytes During Differentiation and in Response to Wound Healing

    Journal: Investigative Ophthalmology & Visual Science

    doi: 10.1167/iovs.14-15179

    Immunodetection of IGF2R in tissue sections from human cornea. Normal human donor corneas ( A , B ), were formalin-fixed, paraffin-embedded, and sections incubated with IGF2R-specific polyclonal antibody ( A ) or the corresponding pre-immune serum ( B ). Biotinylated
    Figure Legend Snippet: Immunodetection of IGF2R in tissue sections from human cornea. Normal human donor corneas ( A , B ), were formalin-fixed, paraffin-embedded, and sections incubated with IGF2R-specific polyclonal antibody ( A ) or the corresponding pre-immune serum ( B ). Biotinylated

    Techniques Used: Immunodetection, Formalin-fixed Paraffin-Embedded, Incubation

    23) Product Images from "Novel A? peptide immunogens modulate plaque pathology and inflammation in a murine model of Alzheimer's disease"

    Article Title: Novel A? peptide immunogens modulate plaque pathology and inflammation in a murine model of Alzheimer's disease

    Journal: Journal of Neuroinflammation

    doi: 10.1186/1742-2094-2-28

    IgG is deposited at detectable levels in Tg 2576 animals immunized at 12 months with fAβ . Representative pictures of cortex sections of mice immunized from 12–16 months with CFA, Oligo Aβ and fAβ. A. Direct immunoperoxidase labeling of mouse IgG using a biotinylated anti mouse IgG and streptavidin-HRP. B. Fluorescent double labeling with horse biotinylated anti mouse IgG (Vector) detected with streptavidin-CY-3 (red) and polyclonal anti Aβ antibody (M-16) detected with FITC conjugated anti rabbit antibody (green). Arrowheads show colocalization of reactivity in some of the plaques. Scale bars: 50 microns.
    Figure Legend Snippet: IgG is deposited at detectable levels in Tg 2576 animals immunized at 12 months with fAβ . Representative pictures of cortex sections of mice immunized from 12–16 months with CFA, Oligo Aβ and fAβ. A. Direct immunoperoxidase labeling of mouse IgG using a biotinylated anti mouse IgG and streptavidin-HRP. B. Fluorescent double labeling with horse biotinylated anti mouse IgG (Vector) detected with streptavidin-CY-3 (red) and polyclonal anti Aβ antibody (M-16) detected with FITC conjugated anti rabbit antibody (green). Arrowheads show colocalization of reactivity in some of the plaques. Scale bars: 50 microns.

    Techniques Used: Mouse Assay, Labeling, Plasmid Preparation

    24) Product Images from "Atherogenesis in the carotid artery with and without interrupted blood flow of two hyperlipidemic mouse strains"

    Article Title: Atherogenesis in the carotid artery with and without interrupted blood flow of two hyperlipidemic mouse strains

    Journal: Journal of vascular research

    doi: 10.1159/000502691

    Immunohistochemical detection of neutrophils (A), macrophages (B, C), CD4+ (D), CD8+ T cells (E), and smooth muscle cells (F) in ligated carotid arteries of B6-Apoe −/− and C3H-Apoe −/− mice fed a Western diet at different time points after ligation. A , Section stained with the standard Avidin-Biotin Complex (ABC) method using an anti-Ly6G antibody. Arrows point to stained neutrophils. B , Sections stained with rat monoclonal macrophage antibody MOMA-2. Arrows point to stained macrophages. C , Fluorescence double immunostaining showing the presence of macrophages in ligated arterial wall of B6-Apoe −/− mice 1 week after ligation. Macrophages were stained with antibodies against Mac3 and FPR1 antigens. Nuclei were stained with DAPI. D , Note the presence of CD4+ cells in intimal lesions of C3H-Apoe −/− mice but not B6-Apoe −/− mice. E , Immunostaining for CD8+ T cells: No CD8+ cells were detectable in the lesions. F , Immunostaining for α-smooth muscle actin. Black arrows point at smooth muscle in the caps and white arrows point at disorganized smooth muscle at the bottom of the lesion. Note the low immunoreactivity to α-smooth muscle actin of the medial arterial wall in B6-Apoe −/− mouse 4 weeks after ligation.
    Figure Legend Snippet: Immunohistochemical detection of neutrophils (A), macrophages (B, C), CD4+ (D), CD8+ T cells (E), and smooth muscle cells (F) in ligated carotid arteries of B6-Apoe −/− and C3H-Apoe −/− mice fed a Western diet at different time points after ligation. A , Section stained with the standard Avidin-Biotin Complex (ABC) method using an anti-Ly6G antibody. Arrows point to stained neutrophils. B , Sections stained with rat monoclonal macrophage antibody MOMA-2. Arrows point to stained macrophages. C , Fluorescence double immunostaining showing the presence of macrophages in ligated arterial wall of B6-Apoe −/− mice 1 week after ligation. Macrophages were stained with antibodies against Mac3 and FPR1 antigens. Nuclei were stained with DAPI. D , Note the presence of CD4+ cells in intimal lesions of C3H-Apoe −/− mice but not B6-Apoe −/− mice. E , Immunostaining for CD8+ T cells: No CD8+ cells were detectable in the lesions. F , Immunostaining for α-smooth muscle actin. Black arrows point at smooth muscle in the caps and white arrows point at disorganized smooth muscle at the bottom of the lesion. Note the low immunoreactivity to α-smooth muscle actin of the medial arterial wall in B6-Apoe −/− mouse 4 weeks after ligation.

    Techniques Used: Immunohistochemistry, Mouse Assay, Western Blot, Ligation, Staining, Avidin-Biotin Assay, Fluorescence, Double Immunostaining, Immunostaining

    25) Product Images from "Control of the Nigrostriatal Dopamine Neuron Activity and Motor Function by the Tail of the Ventral Tegmental Area"

    Article Title: Control of the Nigrostriatal Dopamine Neuron Activity and Motor Function by the Tail of the Ventral Tegmental Area

    Journal: Neuropsychopharmacology

    doi: 10.1038/npp.2014.129

    The tVTA neurons project to the nigrostriatal system. (a) Injection of the anterograde tracer BDA into the tVTA and of the retrograde tracer CTb into the dorsolateral striatum ( n =5). (b and c) tVTA terminals (arrows) contact dendrites and cell soma of striatum-projecting SNc neurons. (d) Injection of the anterograde tracer PhaL into the tVTA ( n =4). (e and f) Electron micrographs showing tVTA axon terminals (tVTA-a) forming synapses (arrow) onto SNc dendrites labeled for tyrosine hydroxylase (TH-d) and contacted by additional unlabeled axons (ua) (f), larger view; (e), details of boxed area). (g) Quantitative analysis of the electron microscopy experiment. Most of the tVTA terminals synapse onto dendrites in the SNc that are immunoreactive for TH. BDA, biotinylated dextran amine; cc, corpus callosum; CTb, cholera toxin β -subunit; DLS, dorsolateral striatum; PhaL, Phaseolus vulgaris leucoagglutinin. Scale bars, 500 μm (a), 20 μm (b, c), 0.25 μm (e), 0.5 μm (f).
    Figure Legend Snippet: The tVTA neurons project to the nigrostriatal system. (a) Injection of the anterograde tracer BDA into the tVTA and of the retrograde tracer CTb into the dorsolateral striatum ( n =5). (b and c) tVTA terminals (arrows) contact dendrites and cell soma of striatum-projecting SNc neurons. (d) Injection of the anterograde tracer PhaL into the tVTA ( n =4). (e and f) Electron micrographs showing tVTA axon terminals (tVTA-a) forming synapses (arrow) onto SNc dendrites labeled for tyrosine hydroxylase (TH-d) and contacted by additional unlabeled axons (ua) (f), larger view; (e), details of boxed area). (g) Quantitative analysis of the electron microscopy experiment. Most of the tVTA terminals synapse onto dendrites in the SNc that are immunoreactive for TH. BDA, biotinylated dextran amine; cc, corpus callosum; CTb, cholera toxin β -subunit; DLS, dorsolateral striatum; PhaL, Phaseolus vulgaris leucoagglutinin. Scale bars, 500 μm (a), 20 μm (b, c), 0.25 μm (e), 0.5 μm (f).

    Techniques Used: Injection, CtB Assay, Labeling, Electron Microscopy

    26) Product Images from "Establishment and characterization of an immortalized Z310 choroidal epithelial cell line from murine choroid plexus"

    Article Title: Establishment and characterization of an immortalized Z310 choroidal epithelial cell line from murine choroid plexus

    Journal: Brain research

    doi:

    Immunocytochemical staining of SV40 large T antigen in cultured Z310 cells. The cells were cultured on a glass coverslip and incubated with monoclonal anti-SV40 large T antigen antibody, followed by reaction with biotinylated goat anti-mouse IgG secondary antibody. The positively stain of SV40 large T was seen in nuclei (×200) at the 52nd passage.
    Figure Legend Snippet: Immunocytochemical staining of SV40 large T antigen in cultured Z310 cells. The cells were cultured on a glass coverslip and incubated with monoclonal anti-SV40 large T antigen antibody, followed by reaction with biotinylated goat anti-mouse IgG secondary antibody. The positively stain of SV40 large T was seen in nuclei (×200) at the 52nd passage.

    Techniques Used: Staining, Cell Culture, Incubation

    Immortalized choroidal Z310 cells possess cytosolic TTR by immunocytochemical staining. The cells were cultured on a glass coverslip and incubated with rabbit anti-rat TTR antiserum, followed by reaction with biotinylated secondary antibody. (A) Cultured Z310 cells show the positive stain for cytosolic TTR (×250). (B) Primary culture of rat choroidal epithelial cells was used as the positive control (×250).
    Figure Legend Snippet: Immortalized choroidal Z310 cells possess cytosolic TTR by immunocytochemical staining. The cells were cultured on a glass coverslip and incubated with rabbit anti-rat TTR antiserum, followed by reaction with biotinylated secondary antibody. (A) Cultured Z310 cells show the positive stain for cytosolic TTR (×250). (B) Primary culture of rat choroidal epithelial cells was used as the positive control (×250).

    Techniques Used: Staining, Cell Culture, Incubation, Positive Control

    27) Product Images from "Epsin is required for Dishevelled stability and Wnt signaling activation in colon cancer development"

    Article Title: Epsin is required for Dishevelled stability and Wnt signaling activation in colon cancer development

    Journal: Nature communications

    doi: 10.1038/ncomms7380

    Epsin interacted with Dvl2 to regulate Wnt receptor signaling independent of receptor-mediated endocytosis (a) Co-immunoprecipitation of endogenous Dvl2, LRP6 and Fzd7 by anti-epsin 1 antibody in Wnt3a-stimulated (100 ng mL −1 , 5 min) HT-29 cells analyzed by Western blotting. (b) Quantification of a , n=8. (c) WT and DKO CECs were stimulated with Wnt3a (100 ng mL −1 ) as indicated then Wnt signaling was analyzed by Western blotting with LRP6 and phospho-LRP6 antibodies. (d) Quantification of phospho-to-total LRP6 fold change in c , n=8. (e) Cell surface of WT and DKO CECs were labeled with cleavable biotin, incubated with Wnt3a at 37°C as indicated then surface biotin was cleaved. Internalized biotinylated-LRP6 was determined by streptavidin bead pull-down and Western blotting. (f) Quantification of e , n=8. All statistical values were calculated using a Student’s t test; P values are indicated. Error bars indicate the mean ± s.e.m.
    Figure Legend Snippet: Epsin interacted with Dvl2 to regulate Wnt receptor signaling independent of receptor-mediated endocytosis (a) Co-immunoprecipitation of endogenous Dvl2, LRP6 and Fzd7 by anti-epsin 1 antibody in Wnt3a-stimulated (100 ng mL −1 , 5 min) HT-29 cells analyzed by Western blotting. (b) Quantification of a , n=8. (c) WT and DKO CECs were stimulated with Wnt3a (100 ng mL −1 ) as indicated then Wnt signaling was analyzed by Western blotting with LRP6 and phospho-LRP6 antibodies. (d) Quantification of phospho-to-total LRP6 fold change in c , n=8. (e) Cell surface of WT and DKO CECs were labeled with cleavable biotin, incubated with Wnt3a at 37°C as indicated then surface biotin was cleaved. Internalized biotinylated-LRP6 was determined by streptavidin bead pull-down and Western blotting. (f) Quantification of e , n=8. All statistical values were calculated using a Student’s t test; P values are indicated. Error bars indicate the mean ± s.e.m.

    Techniques Used: Immunoprecipitation, Western Blot, Labeling, Incubation

    28) Product Images from "Reducing AD-Like Pathology in 3xTg-AD Mouse Model by DNA Epitope Vaccine -- A Novel Immunotherapeutic Strategy"

    Article Title: Reducing AD-Like Pathology in 3xTg-AD Mouse Model by DNA Epitope Vaccine -- A Novel Immunotherapeutic Strategy

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0002124

    The level of oligomeric forms of Aβ detected in hemibrain homogenates by combination of IP with WB using biotinylated anti-Aβ 20.1 monoclonal antibody. Densitometric quantification of bands (relative optical density) revealed significant reduction in the level of Aβ oligomers (3-mers and 6-mers) in brain extracts from immune mice in comparison to control animals (*P
    Figure Legend Snippet: The level of oligomeric forms of Aβ detected in hemibrain homogenates by combination of IP with WB using biotinylated anti-Aβ 20.1 monoclonal antibody. Densitometric quantification of bands (relative optical density) revealed significant reduction in the level of Aβ oligomers (3-mers and 6-mers) in brain extracts from immune mice in comparison to control animals (*P

    Techniques Used: Western Blot, Mouse Assay

    29) Product Images from "A translational continuum of model systems for evaluating treatment strategies in Alzheimer's disease: isradipine as a candidate drug"

    Article Title: A translational continuum of model systems for evaluating treatment strategies in Alzheimer's disease: isradipine as a candidate drug

    Journal: Disease Models & Mechanisms

    doi: 10.1242/dmm.006841

    Chronic treatment with isradipine inhibits the accumulation of tau- P in 3×TgAD mice. (A) Western blot of tau- P levels (detected with the AT8 antibody) in brain lysates from vehicle-treated versus isradipine-treated AD mice. Lower gel shows β-tubulin levels. (B) Quantification of tau- P levels in western blots (normalized to β-tubulin) shows that isradipine treatments reduced overall tau- P levels, although this difference was not significant. (C) Representative brain section from a vehicle-treated AD mouse, immunostained for tau- P (using biotinylated AT8); (D) immunostained brain section from an isradipine-treated AD mouse; C,D illustrate the most dramatic differences seen between vehicle- and isradipine-treated animals. Arrowheads indicate hippocampus; arrow indicates cortex. Scale bar: 400 μm. (E) Quantification of tau- P burden, as detected by immunohistochemistry. Isradipine treatments caused a reduction in tau- P levels in the hippocampus but not the cortex.
    Figure Legend Snippet: Chronic treatment with isradipine inhibits the accumulation of tau- P in 3×TgAD mice. (A) Western blot of tau- P levels (detected with the AT8 antibody) in brain lysates from vehicle-treated versus isradipine-treated AD mice. Lower gel shows β-tubulin levels. (B) Quantification of tau- P levels in western blots (normalized to β-tubulin) shows that isradipine treatments reduced overall tau- P levels, although this difference was not significant. (C) Representative brain section from a vehicle-treated AD mouse, immunostained for tau- P (using biotinylated AT8); (D) immunostained brain section from an isradipine-treated AD mouse; C,D illustrate the most dramatic differences seen between vehicle- and isradipine-treated animals. Arrowheads indicate hippocampus; arrow indicates cortex. Scale bar: 400 μm. (E) Quantification of tau- P burden, as detected by immunohistochemistry. Isradipine treatments caused a reduction in tau- P levels in the hippocampus but not the cortex.

    Techniques Used: Mouse Assay, Western Blot, Immunohistochemistry

    30) Product Images from "Novel Role for Matricellular Proteins in the Regulation of Islet β Cell Survival"

    Article Title: Novel Role for Matricellular Proteins in the Regulation of Islet β Cell Survival

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M114.573980

    SPARC is detected in stromal PS1 cells but not INS-1 β cells by immunocytochemistry. INS-1 and PS1 cells were grown on coverslips, fixed using 10% NBF and stained using anti-SPARC antibody ( panels a–d ) or with biotinylated secondary antibody
    Figure Legend Snippet: SPARC is detected in stromal PS1 cells but not INS-1 β cells by immunocytochemistry. INS-1 and PS1 cells were grown on coverslips, fixed using 10% NBF and stained using anti-SPARC antibody ( panels a–d ) or with biotinylated secondary antibody

    Techniques Used: Immunocytochemistry, Staining

    31) Product Images from "Functional Glycomic Analysis of Human Milk Glycans Reveals the Presence of Virus Receptors and Embryonic Stem Cell Biomarkers *"

    Article Title: Functional Glycomic Analysis of Human Milk Glycans Reveals the Presence of Virus Receptors and Embryonic Stem Cell Biomarkers *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M112.425819

    Plant lectins binding to human milk SGM. The human milk SGM microarray was characterized with biotinylated lectins AAL (0.1 μg/ml; A ), UEA-I (10 μg/ml; B ), LTL (10 μg/ml; C ), SNA (5 μg/ml; D ), RCA-I (10 μg/ml;
    Figure Legend Snippet: Plant lectins binding to human milk SGM. The human milk SGM microarray was characterized with biotinylated lectins AAL (0.1 μg/ml; A ), UEA-I (10 μg/ml; B ), LTL (10 μg/ml; C ), SNA (5 μg/ml; D ), RCA-I (10 μg/ml;

    Techniques Used: Binding Assay, Microarray

    32) Product Images from "Alternative lengthening of telomeres in normal mammalian somatic cells"

    Article Title: Alternative lengthening of telomeres in normal mammalian somatic cells

    Journal: Genes & Development

    doi: 10.1101/gad.205062.112

    Copying of the Tel tag from chromosome 15 onto other telomeres in mouse tissues. ( A – C ) Splenocytes were grown for 48 h ex vivo followed by chromosome harvest and cohybridization of biotinylated plasmid pSXneo (green) and a digoxigenin-labeled
    Figure Legend Snippet: Copying of the Tel tag from chromosome 15 onto other telomeres in mouse tissues. ( A – C ) Splenocytes were grown for 48 h ex vivo followed by chromosome harvest and cohybridization of biotinylated plasmid pSXneo (green) and a digoxigenin-labeled

    Techniques Used: Ex Vivo, Plasmid Preparation, Labeling

    33) Product Images from "SIRF: Quantitative in situ analysis of protein interactions at DNA replication forks"

    Article Title: SIRF: Quantitative in situ analysis of protein interactions at DNA replication forks

    Journal: The Journal of Cell Biology

    doi: 10.1083/jcb.201709121

    EdU incorporation frequency necessary for productive SIRF. (A) Graphical sketch of EdU-incorporated DNA fibers. The distances between EdU nucleotides varies with EdU concentration and is measured (blue line). (B) Representative Airyscan images of single-molecule DNA fibers at 1, 25, and 125 µM EdU in HAP-1 cells using anti-biotin antibodies against biotinylated EdU. (C) Scatter plot of distances between EdU signals in DNA fibers obtained using Airyscan superresolution microscopy in HAP-1 cells at varying EdU concentrations as indicated. (D) Graphical sketch of productive PLA-EdU-DNA fiber signal dependence on EdU concentrations. (E) Representative Airyscan images of single-molecule DNA fibers at 1, 25, and 125 µM EdU in HAP-1 cells using PLA against biotinylated EdU. (F) Graphical sketch of productive PLA-SIRF signal dependence on EdU concentration. (G) Representative images of HAP-1 cells treated with 0, 1, 25, and 125 µM EdU. (H) Scatter plot of EdU-SIRF signals in HAP-1 cells with 1, 25, and 125 µM EdU. Bars represent the mean and SD of combined data from repeated experiments. The significance values are derived from Mann-Whitney statistical analysis.
    Figure Legend Snippet: EdU incorporation frequency necessary for productive SIRF. (A) Graphical sketch of EdU-incorporated DNA fibers. The distances between EdU nucleotides varies with EdU concentration and is measured (blue line). (B) Representative Airyscan images of single-molecule DNA fibers at 1, 25, and 125 µM EdU in HAP-1 cells using anti-biotin antibodies against biotinylated EdU. (C) Scatter plot of distances between EdU signals in DNA fibers obtained using Airyscan superresolution microscopy in HAP-1 cells at varying EdU concentrations as indicated. (D) Graphical sketch of productive PLA-EdU-DNA fiber signal dependence on EdU concentrations. (E) Representative Airyscan images of single-molecule DNA fibers at 1, 25, and 125 µM EdU in HAP-1 cells using PLA against biotinylated EdU. (F) Graphical sketch of productive PLA-SIRF signal dependence on EdU concentration. (G) Representative images of HAP-1 cells treated with 0, 1, 25, and 125 µM EdU. (H) Scatter plot of EdU-SIRF signals in HAP-1 cells with 1, 25, and 125 µM EdU. Bars represent the mean and SD of combined data from repeated experiments. The significance values are derived from Mann-Whitney statistical analysis.

    Techniques Used: Concentration Assay, Microscopy, Proximity Ligation Assay, Derivative Assay, MANN-WHITNEY

    Schematic representation outlining SIRF assay. (A) Cells are grown in microscope chamber-slides and pulsed with EdU. (B) EdU is biotinylated using click chemistry. (C) Slides are incubated with primary antibody (AB) against protein of interest and against biotin, followed by incubation with secondary PLA antibodies containing a DNA-oligomers. (D) A linker DNA binds to the antibody-oligomers allowing T7-mediated ligation for rolling circle amplification by PHI29 polymerase. (E) A fluorescent DNA probe anneals in a sequence specific fashion to the amplification product, thus producing many red fluorescent signals per one antibody interaction, which results in robust and detectable fluorescence. (F) Unproductive reaction occurs when the PLA antibodies are not in close proximity, thus inhibiting formation of circular template and consequent fluorescent probe annealing of the amplified circle.
    Figure Legend Snippet: Schematic representation outlining SIRF assay. (A) Cells are grown in microscope chamber-slides and pulsed with EdU. (B) EdU is biotinylated using click chemistry. (C) Slides are incubated with primary antibody (AB) against protein of interest and against biotin, followed by incubation with secondary PLA antibodies containing a DNA-oligomers. (D) A linker DNA binds to the antibody-oligomers allowing T7-mediated ligation for rolling circle amplification by PHI29 polymerase. (E) A fluorescent DNA probe anneals in a sequence specific fashion to the amplification product, thus producing many red fluorescent signals per one antibody interaction, which results in robust and detectable fluorescence. (F) Unproductive reaction occurs when the PLA antibodies are not in close proximity, thus inhibiting formation of circular template and consequent fluorescent probe annealing of the amplified circle.

    Techniques Used: Microscopy, Incubation, Proximity Ligation Assay, Ligation, Amplification, Sequencing, Fluorescence

    34) Product Images from "Galectin-3 expression is prognostic in diffuse type gastric adenocarcinoma, confers aggressive phenotype, and can be targeted by YAP1/BET inhibitors"

    Article Title: Galectin-3 expression is prognostic in diffuse type gastric adenocarcinoma, confers aggressive phenotype, and can be targeted by YAP1/BET inhibitors

    Journal: British Journal of Cancer

    doi: 10.1038/bjc.2017.388

    Gal-3 is highly up-regulated in human GAC tissues and associated with poor survival in North American GAC patients. ( A ) Human gastric tissue microarray slides consisting of 215 Gastric adenocarcinomas and non-neoplastic gastric tissue samples were immunohistochemically stained using a monoclonal Gal-3 antibody as described in Materials and Methods. Gal-3 expression was increased in both diffused and intestinal GAC tissues compared to normal stomach. Representative images show IHC staining for Gal-3 in tissues of normal, intestinal and diffused type GAC tissues. ( B ) Cumulative Survival Probability was analysed in All GAC patients by specialised statisticians (A.C) using Kaplan–Meier methods; Gal-3 expression high ( > 3.5) or low (
    Figure Legend Snippet: Gal-3 is highly up-regulated in human GAC tissues and associated with poor survival in North American GAC patients. ( A ) Human gastric tissue microarray slides consisting of 215 Gastric adenocarcinomas and non-neoplastic gastric tissue samples were immunohistochemically stained using a monoclonal Gal-3 antibody as described in Materials and Methods. Gal-3 expression was increased in both diffused and intestinal GAC tissues compared to normal stomach. Representative images show IHC staining for Gal-3 in tissues of normal, intestinal and diffused type GAC tissues. ( B ) Cumulative Survival Probability was analysed in All GAC patients by specialised statisticians (A.C) using Kaplan–Meier methods; Gal-3 expression high ( > 3.5) or low (

    Techniques Used: Microarray, Staining, Expressing, Immunohistochemistry

    35) Product Images from "Prevalent Overexpression of Prolyl Isomerase Pin1 in Human Cancers"

    Article Title: Prevalent Overexpression of Prolyl Isomerase Pin1 in Human Cancers

    Journal: The American Journal of Pathology

    doi:

    Immunocytochemical staining of Pin1 in cultured cells. Cells were incubated with anti-Pin1 antibodies, followed by secondary biotinylated antibody and ABC (avidin and biotinylated horseradish peroxidase complex)-diaminobenzidine reaction. A: WI38 (normal
    Figure Legend Snippet: Immunocytochemical staining of Pin1 in cultured cells. Cells were incubated with anti-Pin1 antibodies, followed by secondary biotinylated antibody and ABC (avidin and biotinylated horseradish peroxidase complex)-diaminobenzidine reaction. A: WI38 (normal

    Techniques Used: Staining, Cell Culture, Incubation, Avidin-Biotin Assay

    36) Product Images from "A New Nerve Growth Factor-Mimetic Peptide Active on Neuropathic Pain in Rats"

    Article Title: A New Nerve Growth Factor-Mimetic Peptide Active on Neuropathic Pain in Rats

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.5201-07.2008

    Immunocytochemistry of dorsal horn of the lumbar spinal cord. Sham- (CTR) and CCI-operated animals treated for 7 d by intrathecal infusion of NGF (125 ng/μl/hr) or peptide L1L4 (37.5 μg/μl/hr) were killed on day 14 as described in Materials and Methods. Sections of dorsal horn of the lumbar spinal cord were immunostained for Sub P, CGRP, Cb, GFAP, and ED1 by incubation with the primary antibody followed by the appropriate biotinylated secondary antibody. Samples were then processed by the Vectastain avidin-biotin peroxidase kit (Vector Laboratories) and reaction with DAB and 0.01% hydrogen peroxide. Sections were mounted on chrome-alume gelatin coated slides and imaged with a Zeiss Axioskope 2 light microscope equipped with high-resolution digital camera (C4742–95; Hamamatsu Photonics). Scale bar, 50 μm. Adjacent sections were Nissl-stained.
    Figure Legend Snippet: Immunocytochemistry of dorsal horn of the lumbar spinal cord. Sham- (CTR) and CCI-operated animals treated for 7 d by intrathecal infusion of NGF (125 ng/μl/hr) or peptide L1L4 (37.5 μg/μl/hr) were killed on day 14 as described in Materials and Methods. Sections of dorsal horn of the lumbar spinal cord were immunostained for Sub P, CGRP, Cb, GFAP, and ED1 by incubation with the primary antibody followed by the appropriate biotinylated secondary antibody. Samples were then processed by the Vectastain avidin-biotin peroxidase kit (Vector Laboratories) and reaction with DAB and 0.01% hydrogen peroxide. Sections were mounted on chrome-alume gelatin coated slides and imaged with a Zeiss Axioskope 2 light microscope equipped with high-resolution digital camera (C4742–95; Hamamatsu Photonics). Scale bar, 50 μm. Adjacent sections were Nissl-stained.

    Techniques Used: Immunocytochemistry, Incubation, Avidin-Biotin Assay, Plasmid Preparation, Light Microscopy, Staining

    37) Product Images from "Transforming single DNA molecules into fluorescent magnetic particles for detection and enumeration of genetic variations"

    Article Title: Transforming single DNA molecules into fluorescent magnetic particles for detection and enumeration of genetic variations

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    doi: 10.1073/pnas.1133470100

    Schematic of BEAMing. Step 1: Magnetic beads covalently coated with streptavidin are bound to biotinylated oligonucleotides (oligos). Step 2: An aqueous mix containing all the necessary components for PCR plus primer-bound beads and template DNA are stirred together with an oil/detergent mix to create microemulsions. The aqueous compartments (white circles in the gray oil layer) contain an average of less than one template molecule and less than one bead. Red and green templates represent two template molecules, the sequences of which differ by one or many nucleotides. Step 3: The microemulsions are temperature-cycled as in a conventional PCR. If a DNA template and a bead are present together in a single aqueous compartment, the bead-bound oligonucleotides act as primers for amplification. The straight red and green lines connected to the beads represent extension products from the two different kinds of templates. Step 4: The emulsions are broken, and the beads are purified with a magnet. Step 5: After denaturation, the beads are incubated with oligonucleotides that can distinguish between the sequences of the different kinds of templates. Fluorescently labeled antibodies then are used to label the bound hybridization probes, which renders the beads containing PCR product as red or green after appropriate laser excitation. Step 6: Flow cytometry is used to count the red and green beads.
    Figure Legend Snippet: Schematic of BEAMing. Step 1: Magnetic beads covalently coated with streptavidin are bound to biotinylated oligonucleotides (oligos). Step 2: An aqueous mix containing all the necessary components for PCR plus primer-bound beads and template DNA are stirred together with an oil/detergent mix to create microemulsions. The aqueous compartments (white circles in the gray oil layer) contain an average of less than one template molecule and less than one bead. Red and green templates represent two template molecules, the sequences of which differ by one or many nucleotides. Step 3: The microemulsions are temperature-cycled as in a conventional PCR. If a DNA template and a bead are present together in a single aqueous compartment, the bead-bound oligonucleotides act as primers for amplification. The straight red and green lines connected to the beads represent extension products from the two different kinds of templates. Step 4: The emulsions are broken, and the beads are purified with a magnet. Step 5: After denaturation, the beads are incubated with oligonucleotides that can distinguish between the sequences of the different kinds of templates. Fluorescently labeled antibodies then are used to label the bound hybridization probes, which renders the beads containing PCR product as red or green after appropriate laser excitation. Step 6: Flow cytometry is used to count the red and green beads.

    Techniques Used: Magnetic Beads, Polymerase Chain Reaction, Activated Clotting Time Assay, Amplification, Purification, Incubation, Labeling, Hybridization, Flow Cytometry, Cytometry

    38) Product Images from "Detection of Anthrax Toxin by an Ultrasensitive Immunoassay Using Europium Nanoparticles ▿"

    Article Title: Detection of Anthrax Toxin by an Ultrasensitive Immunoassay Using Europium Nanoparticles ▿

    Journal: Clinical and Vaccine Immunology : CVI

    doi: 10.1128/CVI.00412-08

    Scheme of ENIA for detection of anthrax toxin (PA). ENIA uses monoclonal anti-PA antibody-coated microtiter wells to capture the anthrax PA in the samples. The PA protein is then sandwiched with secondary rabbit anti-PA antibody and biotinylated goat anti-rabbit antibody. The Eu + NPs modified with SA recognize and bind to this biotinylated antigen-antibody complex. The addition of biotinylated anti-SA antibody and Eu + -labeled SA molecules enhances the signal intensity of the binding event. After extensive washing of the complex, the fluorescence signal released from the sandwiched complex is then recorded and quantified with a Vector fluorometer.
    Figure Legend Snippet: Scheme of ENIA for detection of anthrax toxin (PA). ENIA uses monoclonal anti-PA antibody-coated microtiter wells to capture the anthrax PA in the samples. The PA protein is then sandwiched with secondary rabbit anti-PA antibody and biotinylated goat anti-rabbit antibody. The Eu + NPs modified with SA recognize and bind to this biotinylated antigen-antibody complex. The addition of biotinylated anti-SA antibody and Eu + -labeled SA molecules enhances the signal intensity of the binding event. After extensive washing of the complex, the fluorescence signal released from the sandwiched complex is then recorded and quantified with a Vector fluorometer.

    Techniques Used: Modification, Labeling, Binding Assay, Fluorescence, Plasmid Preparation

    39) Product Images from "Mice Lacking Expression of Secondary Lymphoid Organ Chemokine Have Defects in Lymphocyte Homing and Dendritic Cell Localization "

    Article Title: Mice Lacking Expression of Secondary Lymphoid Organ Chemokine Have Defects in Lymphocyte Homing and Dendritic Cell Localization

    Journal: The Journal of Experimental Medicine

    doi:

    (A) The number of DCs is decreased in LNs of plt mice. LNs of +/+ and plt mice were collected and centrifuged over metrizamide gradients. Cells at the interface were collected, stained with FITC-conjugated anti–mouse I-Ad, normalized to the total number of cells per LN, and analyzed by FACS ® to detect I-A + DCs (top right quadrant). One representative experiment of three is shown. (B) The number of DCs is normal in spleens of plt mice. Spleens of +/+ and plt mice were collected, dissociated with collagenase, and stained with FITC-anti–I-Ad, biotinylated anti-B220, and biotinylated anti-CD3 followed by SA-PerCP, normalized to the total number of cells per spleen, and analyzed by flow cytometry. CD3 − , B220 − gated cells in one representative experiment of three are shown.
    Figure Legend Snippet: (A) The number of DCs is decreased in LNs of plt mice. LNs of +/+ and plt mice were collected and centrifuged over metrizamide gradients. Cells at the interface were collected, stained with FITC-conjugated anti–mouse I-Ad, normalized to the total number of cells per LN, and analyzed by FACS ® to detect I-A + DCs (top right quadrant). One representative experiment of three is shown. (B) The number of DCs is normal in spleens of plt mice. Spleens of +/+ and plt mice were collected, dissociated with collagenase, and stained with FITC-anti–I-Ad, biotinylated anti-B220, and biotinylated anti-CD3 followed by SA-PerCP, normalized to the total number of cells per spleen, and analyzed by flow cytometry. CD3 − , B220 − gated cells in one representative experiment of three are shown.

    Techniques Used: Mouse Assay, Staining, FACS, Flow Cytometry, Cytometry

    Decreased migration of skin DCs to LNs in plt mice after contact sensitization with FITC. (A) The shaved abdomens of +/+ and plt mice were painted with 2 mg FITC. After 24 h draining LNs were removed, dissociated, normalized to the total number of cells per LN, and analyzed by flow cytometry. A decreased number of large FITC + cells (boxed area) can be seen in plt mice. One of eight representative experiments is shown. (B) Representative FACS ® profile showing a marked decrease of CD11c + FITC + cells in plt mice after FITC skin painting. (C) Draining LN cells from FITC-painted mice were partially purified on metrizamide gradients, stained with biotinylated anti–I-Ad followed by SA-PerCP, and analyzed by flow cytometry. Only large FITC + cells (boxed areas in A) are shown. (D) The number of FITC + DCs (boxed areas in A) that accumulate in LNs after skin painting with 2 mg FITC is reduced in plt mice. Numbers represent mean ± SD ( n = 8). (E) Comparison of DC content in contralateral (CLN) and draining (DLN) inguinal LNs in mice painted on one flank with 0.2 mg FITC. Single cell suspensions were prepared from individual LNs, stained with anti–I-Ad and anti-B220, and analyzed by flow cytometry gated on I-A + B220 − cells.
    Figure Legend Snippet: Decreased migration of skin DCs to LNs in plt mice after contact sensitization with FITC. (A) The shaved abdomens of +/+ and plt mice were painted with 2 mg FITC. After 24 h draining LNs were removed, dissociated, normalized to the total number of cells per LN, and analyzed by flow cytometry. A decreased number of large FITC + cells (boxed area) can be seen in plt mice. One of eight representative experiments is shown. (B) Representative FACS ® profile showing a marked decrease of CD11c + FITC + cells in plt mice after FITC skin painting. (C) Draining LN cells from FITC-painted mice were partially purified on metrizamide gradients, stained with biotinylated anti–I-Ad followed by SA-PerCP, and analyzed by flow cytometry. Only large FITC + cells (boxed areas in A) are shown. (D) The number of FITC + DCs (boxed areas in A) that accumulate in LNs after skin painting with 2 mg FITC is reduced in plt mice. Numbers represent mean ± SD ( n = 8). (E) Comparison of DC content in contralateral (CLN) and draining (DLN) inguinal LNs in mice painted on one flank with 0.2 mg FITC. Single cell suspensions were prepared from individual LNs, stained with anti–I-Ad and anti-B220, and analyzed by flow cytometry gated on I-A + B220 − cells.

    Techniques Used: Migration, Mouse Assay, Flow Cytometry, Cytometry, FACS, Purification, Staining

    40) Product Images from "HMG-CoA Reductase Inhibition Promotes Neurological Recovery, Peri-Lesional Tissue Remodeling, and Contralesional Pyramidal Tract Plasticity after Focal Cerebral Ischemia"

    Article Title: HMG-CoA Reductase Inhibition Promotes Neurological Recovery, Peri-Lesional Tissue Remodeling, and Contralesional Pyramidal Tract Plasticity after Focal Cerebral Ischemia

    Journal: Frontiers in Cellular Neuroscience

    doi: 10.3389/fncel.2014.00422

    Rosuvastatin promotes contralesional corticorubral plasticity . Tract tracing analysis of corticorubral projections ipsilateral and contralateral to the stroke in mice receiving cascade blue (CB) and biotinylated dextran amine (BDA) injections into the lesion-sided and contralesional motor cortex [for experimental procedures see (A) ]. Percent of midline-crossing fibers to (B) the contralesional red nucleus (RN) traced by CB and (C) ipsilesional red nucleus traced by BDA. Note that the percentage of midline-crossing fibers after ipsilesional CB injection increases in response to stroke (though not significantly) (B) . Importantly, rosuvastatin, delivered at a dose of 2 mg/kg/day, does not further elevate the percentage of midline-crossing fibers originating from the ipsilesional pyramidal tract (B) , but increases the percentage of contralesional pyramidal tract fibers growing out across the midline in direction to the ipsilesional red nucleus (C) . (D) Microphotographs of representative vehicle-treated and rosuvastatin-treated ischemic mice illustrating BDA traced corticorubral fibers crossing the midline in between both red nuclei. Note that the ipsilesional (left) red nucleus receives more BDA traced fibers after rosuvastatin than vehicle delivery. Data are mean values ± SD ( n = 10 animals/group). § p
    Figure Legend Snippet: Rosuvastatin promotes contralesional corticorubral plasticity . Tract tracing analysis of corticorubral projections ipsilateral and contralateral to the stroke in mice receiving cascade blue (CB) and biotinylated dextran amine (BDA) injections into the lesion-sided and contralesional motor cortex [for experimental procedures see (A) ]. Percent of midline-crossing fibers to (B) the contralesional red nucleus (RN) traced by CB and (C) ipsilesional red nucleus traced by BDA. Note that the percentage of midline-crossing fibers after ipsilesional CB injection increases in response to stroke (though not significantly) (B) . Importantly, rosuvastatin, delivered at a dose of 2 mg/kg/day, does not further elevate the percentage of midline-crossing fibers originating from the ipsilesional pyramidal tract (B) , but increases the percentage of contralesional pyramidal tract fibers growing out across the midline in direction to the ipsilesional red nucleus (C) . (D) Microphotographs of representative vehicle-treated and rosuvastatin-treated ischemic mice illustrating BDA traced corticorubral fibers crossing the midline in between both red nuclei. Note that the ipsilesional (left) red nucleus receives more BDA traced fibers after rosuvastatin than vehicle delivery. Data are mean values ± SD ( n = 10 animals/group). § p

    Techniques Used: Mouse Assay, Injection

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    Article Snippet: The right halves of brains and entire spinal cords from animals sacrificed at days 3, 5, and 7 p.i. were fixed in formalin, embedded in paraffin, sectioned, and stained for viral antigen or inflammation. .. Antigen staining was performed by the avidin-biotin-immunoperoxidase technique (Vector Laboratories, Burlingame, Calif.) by using diaminobenzidine tetrahydrochloride as the substrate and a 1:20 dilution of rabbit antinucleocapsid monoclonal antibody (kindly provided by Julian Leibowitz). .. Hematoxylin-and-eosin (H-and-E) staining for inflammation was carried out, and analysis was performed in a blinded manner by a neuropathologist.

    Article Title: Inflammatory Responses Are Not Sufficient to Cause Delayed Neuronal Death in ATP-Induced Acute Brain Injury
    Article Snippet: Sections were incubated overnight at room temperature with primary antibodies against tyrosine hydroxylase (TH; 1∶2000 dilution; Pelfreeze Biologicals, Rogers, AR), ionized calcium binding adaptor molecule 1 (Iba-1; 1∶1000; Wako Pure Chemical Industries, Osaka, Japan), myeloperoxidase (MPO; 1∶1000; Dako, Glostrup, Denmark), CD45 (1∶200; AbD Serotec, Oxford, UK), CD11b (OX-42; 1∶200; Serotec, Oxford, UK), Ki-67 (1∶100; Abcam, Cambridge, UK), interleukin-1β (IL-1β; 1∶200; R & D systems, MN), inducible nitric oxide synthase (iNOS; 1∶200; Abcam, Cambridge, UK), CD68 (1∶200; AbD Serotec, oxford, UK) or Neuronal Nuclei (NeuN; 1: 300; Chemicon, CA, USA). .. Following rinsing in PBST, sections were incubated with biotinylated secondary antibodies (Vector Laboratories, Burlingame, CA) for 1 h and the avidin/biotin system (Vector Laboratories, Burlingame, CA) for 1 h and visualized using DAB solution (0.05% DAB and 0.003% hydrogen peroxide in 0.1 M PB). .. For double-labeling with TH and Iba-1, sections were stained with TH antibody following the above procedure, and visualized with DAB (brown product).

    Incubation:

    Article Title: A regulated PNUTS mRNA to lncRNA splice switch mediates EMT and tumor progression
    Article Snippet: Immunohistochemistry Formalin-fixed, paraffin-embedded sections were deparaffinized in xylene, rehydrated in alcohol, and processed as follows: Sections were incubated with target retrieval solution (Dako) in a steamer for 45 min followed by 3% hydrogen peroxide solution for 10 min and protein block (Dako) for 20 min at room temperature. .. Sections were incubated overnight in a humid chamber at 4°C with antibody against Ki-67 purchased from Cell signaling technology company (Clone [D2H10], Cat. #9027, 1:1600 dilution) followed by biotinylated secondary antibody (Vector laboratories) for 30 min and ABC reagent for 30 min. Immunocomplexes of horseradish peroxidase were visualized by DAB reaction (Dako), and sections were counterstained with hematoxylin before mounting. .. Micrographs of stained sections were taken using a Leica DMIL LED microscope with Amscope camera and acquisition software.

    Article Title: Anti-GRP78 autoantibodies induce endothelial cell activation and accelerate the development of atherosclerotic lesions
    Article Snippet: Aortic sections (4-μm thick) were deparaffinized, and the endogenous peroxidase activity was blocked with 0.5% H2 O2 in methanol for 10 minutes, as described previously ( ). .. Following antigen retrieval where necessary, sections were blocked with 5% normal serum, and incubated with the primary antibody for 1 hour, followed by biotinylated secondary antibody (Vector Laboratories, Burlingame, CA) diluted 1:500, and streptavidin HRP (Vector Laboratories) diluted 1:50. .. Sections were developed in Nova Red peroxidase substrate (Vector Laboratories) and counterstained with hematoxylin.

    Article Title: Y-cell receptive field and collicular projection of parasol ganglion cells in macaque monkey retina
    Article Snippet: In some retinas we alternatively improved photostaining by an additional immunohistochemical step using biotinylated anti-rhodamine prior to HRP processing. .. Following fixation, retinas were incubated in 0.1% Triton X-100 in PBS (0.1 M, pH 7.4) containing biotinylated anti-rhodamine (C# BA-0605, Vector Labs) at a concentration of 1:100 for 36 hr at room temperature, then washed in phosphate buffer overnight. .. Retinas were then processed for HRP histochemistry as described above using the Vector avidin-biotin-HRP complex and DAB.

    Article Title: Physiological Modulation of Intestinal Motility by Enteric Dopaminergic Neurons and the D2 Receptor: Analysis of Dopamine Receptor Expression, Location, Development, and Function in Wild-Type and Knock-Out Mice
    Article Snippet: Briefly, preparations were incubated (30 min) with 10% normal serum (of the species in which the secondary antibodies were raised) to inhibit nonspecific staining. .. The blocked tissue was then incubated overnight with primary antibodies, washed with PBS, and exposed with intervening washes in PBS to the biotinylated secondary antibodies (2 h), 0.3% H2 O2 in 0.3% blocking sera (5 min), Elite ABC reagent (1 h; Vector Laboratories), and 3′,5′-diaminobenzidine solution (2–10 min) until suitable staining developed. .. As a control for the specificity of antibodies to the D2 and D3 receptors, attempts were made to immunostain the corresponding receptors in the gut of knock-out animals lacking these receptors.

    Article Title: Inflammatory Responses Are Not Sufficient to Cause Delayed Neuronal Death in ATP-Induced Acute Brain Injury
    Article Snippet: Sections were incubated overnight at room temperature with primary antibodies against tyrosine hydroxylase (TH; 1∶2000 dilution; Pelfreeze Biologicals, Rogers, AR), ionized calcium binding adaptor molecule 1 (Iba-1; 1∶1000; Wako Pure Chemical Industries, Osaka, Japan), myeloperoxidase (MPO; 1∶1000; Dako, Glostrup, Denmark), CD45 (1∶200; AbD Serotec, Oxford, UK), CD11b (OX-42; 1∶200; Serotec, Oxford, UK), Ki-67 (1∶100; Abcam, Cambridge, UK), interleukin-1β (IL-1β; 1∶200; R & D systems, MN), inducible nitric oxide synthase (iNOS; 1∶200; Abcam, Cambridge, UK), CD68 (1∶200; AbD Serotec, oxford, UK) or Neuronal Nuclei (NeuN; 1: 300; Chemicon, CA, USA). .. Following rinsing in PBST, sections were incubated with biotinylated secondary antibodies (Vector Laboratories, Burlingame, CA) for 1 h and the avidin/biotin system (Vector Laboratories, Burlingame, CA) for 1 h and visualized using DAB solution (0.05% DAB and 0.003% hydrogen peroxide in 0.1 M PB). .. For double-labeling with TH and Iba-1, sections were stained with TH antibody following the above procedure, and visualized with DAB (brown product).

    Article Title: Region-specific astrogliosis: differential vessel formation contributes to different patterns of astrogliosis in the cortex and striatum
    Article Snippet: After incubation with 1% bovine serum albumin (BSA) in PBS, the sections were incubated overnight at 4 °C with primary antibodies (Table ). .. The sections were rinsed three times with PBS and incubated with biotinylated secondary antibodies (Vector Laboratories, Burlingame, CA, USA). .. Immunoreactive proteins were visualized using an avidin-biotin-peroxidase-DAB solution (0.05% DAB and 0.003% H2 O2 in 0.1 M PB) according to the manufacturer’s instructions.

    Concentration Assay:

    Article Title: Y-cell receptive field and collicular projection of parasol ganglion cells in macaque monkey retina
    Article Snippet: In some retinas we alternatively improved photostaining by an additional immunohistochemical step using biotinylated anti-rhodamine prior to HRP processing. .. Following fixation, retinas were incubated in 0.1% Triton X-100 in PBS (0.1 M, pH 7.4) containing biotinylated anti-rhodamine (C# BA-0605, Vector Labs) at a concentration of 1:100 for 36 hr at room temperature, then washed in phosphate buffer overnight. .. Retinas were then processed for HRP histochemistry as described above using the Vector avidin-biotin-HRP complex and DAB.

    Blocking Assay:

    Article Title: Physiological Modulation of Intestinal Motility by Enteric Dopaminergic Neurons and the D2 Receptor: Analysis of Dopamine Receptor Expression, Location, Development, and Function in Wild-Type and Knock-Out Mice
    Article Snippet: Briefly, preparations were incubated (30 min) with 10% normal serum (of the species in which the secondary antibodies were raised) to inhibit nonspecific staining. .. The blocked tissue was then incubated overnight with primary antibodies, washed with PBS, and exposed with intervening washes in PBS to the biotinylated secondary antibodies (2 h), 0.3% H2 O2 in 0.3% blocking sera (5 min), Elite ABC reagent (1 h; Vector Laboratories), and 3′,5′-diaminobenzidine solution (2–10 min) until suitable staining developed. .. As a control for the specificity of antibodies to the D2 and D3 receptors, attempts were made to immunostain the corresponding receptors in the gut of knock-out animals lacking these receptors.

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    Vector Laboratories biotinylated secondary antibody reagent
    Functional activities of gC1qR MAbs 74.5.2 and 60.11 in rat serum. <t>Biotinylated,</t> clfA -positive bacteria were suspended (10% cell suspension) in selected serum samples from animals treated with gC1qR MAbs. Samples were applied to fibrinogen-coated microtiter
    Biotinylated Secondary Antibody Reagent, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Functional activities of gC1qR MAbs 74.5.2 and 60.11 in rat serum. Biotinylated, clfA -positive bacteria were suspended (10% cell suspension) in selected serum samples from animals treated with gC1qR MAbs. Samples were applied to fibrinogen-coated microtiter

    Journal:

    Article Title: gC1qR/p33 Blockade Reduces Staphylococcus aureus Colonization of Target Tissues in an Animal Model of Infective Endocarditis

    doi: 10.1128/IAI.01794-05

    Figure Lengend Snippet: Functional activities of gC1qR MAbs 74.5.2 and 60.11 in rat serum. Biotinylated, clfA -positive bacteria were suspended (10% cell suspension) in selected serum samples from animals treated with gC1qR MAbs. Samples were applied to fibrinogen-coated microtiter

    Article Snippet: Antibody was detected by using a biotinylated secondary antibody reagent at room temperature for 2 h (Vectastain Elite ABC kit; Vector Laboratories, Inc., Burlingame, CA) ( ).

    Techniques: Functional Assay

    Photomicrograph of ~1 mm 2 area of a macaque retina that was retrogradely tracer labeled from injections of biotinylated rhodamine dextran in the superior colliculus and photostained in the in vitro retina. Following fixation the retina was processed for

    Journal:

    Article Title: Y-cell receptive field and collicular projection of parasol ganglion cells in macaque monkey retina

    doi: 10.1523/JNEUROSCI.2982-08.2008

    Figure Lengend Snippet: Photomicrograph of ~1 mm 2 area of a macaque retina that was retrogradely tracer labeled from injections of biotinylated rhodamine dextran in the superior colliculus and photostained in the in vitro retina. Following fixation the retina was processed for

    Article Snippet: Following fixation, retinas were incubated in 0.1% Triton X-100 in PBS (0.1 M, pH 7.4) containing biotinylated anti-rhodamine (C# BA-0605, Vector Labs) at a concentration of 1:100 for 36 hr at room temperature, then washed in phosphate buffer overnight.

    Techniques: Labeling, In Vitro

    Parasol cells project to the superior colliculus. A–E , Photomicrographs of parasol cells from the retinal periphery (eccentricity range: 10 – 11.5 mm) retrogradely labeled by injection of biotinylated rhodamine-dextran into the superior

    Journal:

    Article Title: Y-cell receptive field and collicular projection of parasol ganglion cells in macaque monkey retina

    doi: 10.1523/JNEUROSCI.2982-08.2008

    Figure Lengend Snippet: Parasol cells project to the superior colliculus. A–E , Photomicrographs of parasol cells from the retinal periphery (eccentricity range: 10 – 11.5 mm) retrogradely labeled by injection of biotinylated rhodamine-dextran into the superior

    Article Snippet: Following fixation, retinas were incubated in 0.1% Triton X-100 in PBS (0.1 M, pH 7.4) containing biotinylated anti-rhodamine (C# BA-0605, Vector Labs) at a concentration of 1:100 for 36 hr at room temperature, then washed in phosphate buffer overnight.

    Techniques: Labeling, Injection

    Mosaic of neighboring parasol cells retrogradely stained from injections of biotinylated rhodamine dextran injections into the superior colliculus. A , Photomicrograph of two pairs of inner parasol cells with overlapping dendritic fields, at an eccentricity

    Journal:

    Article Title: Y-cell receptive field and collicular projection of parasol ganglion cells in macaque monkey retina

    doi: 10.1523/JNEUROSCI.2982-08.2008

    Figure Lengend Snippet: Mosaic of neighboring parasol cells retrogradely stained from injections of biotinylated rhodamine dextran injections into the superior colliculus. A , Photomicrograph of two pairs of inner parasol cells with overlapping dendritic fields, at an eccentricity

    Article Snippet: Following fixation, retinas were incubated in 0.1% Triton X-100 in PBS (0.1 M, pH 7.4) containing biotinylated anti-rhodamine (C# BA-0605, Vector Labs) at a concentration of 1:100 for 36 hr at room temperature, then washed in phosphate buffer overnight.

    Techniques: Staining

    Photomicrographs of macaque brain sections showing injection of biotinylated rhodamine dextran confined to the superior colliculus. Sections are shown stacked consecutively from lower right to upper left covering ~1.2 mm distance. Orientation of stacked

    Journal:

    Article Title: Y-cell receptive field and collicular projection of parasol ganglion cells in macaque monkey retina

    doi: 10.1523/JNEUROSCI.2982-08.2008

    Figure Lengend Snippet: Photomicrographs of macaque brain sections showing injection of biotinylated rhodamine dextran confined to the superior colliculus. Sections are shown stacked consecutively from lower right to upper left covering ~1.2 mm distance. Orientation of stacked

    Article Snippet: Following fixation, retinas were incubated in 0.1% Triton X-100 in PBS (0.1 M, pH 7.4) containing biotinylated anti-rhodamine (C# BA-0605, Vector Labs) at a concentration of 1:100 for 36 hr at room temperature, then washed in phosphate buffer overnight.

    Techniques: Injection

    Death of dopaminergic neurons and microglia in the SNpc induced by ATP. ( A ) ATP (100 nmol in 2 µl PBS) or PBS (2 µl) was unilaterally injected into SNpc (*, injection sites), and brains were obtained after 3 h. Brain sections (30 µm thickness) of the midbrain including the entire SN were prepared, every sixth serial section selected and stained with TH (upper panel) and Iba-1 (lower panel) antibodies, and visualized with biotin-conjugated secondary antibodies and enzymatic detection with the avidin/biotin system unless indicated. At 100 nmol, mild neuronal and microglial damage occurred, thus, 100 nmol ATP was employed for in vivo experiments in this study. Photographs of the most damaged sections were obtained. The contralateral side (contra) and PBS-injected rat brain sections were used as control. ( B ) Serial sections obtained at 3 h were labeled with TH (left panel), Iba-1 (middle panel), and TH/Iba-1 (right panel) antibodies. For visualization of the double-labeling, color reactions using DAB (for TH) and DAB/nickel sulfate (for Iba-1) were applied. Dotted lines indicated damage areas. ( C ) Brain tissue obtained 3 h post ATP treatment was subjected to electron microscopy, as described in “ Materials and Methods ”. Nuclei of neuron (N, white arrow), astrocytes (A, white arrowhead), and microglia (M, black arrow) were shown in intact rat brain whereas cellular structures were severely disrupted in ATP-injected brain. Data in this study are representative of at least 5 animals. Scale bars, 200 µm (A); 100 µm (B); 5 µm (C).

    Journal: PLoS ONE

    Article Title: Inflammatory Responses Are Not Sufficient to Cause Delayed Neuronal Death in ATP-Induced Acute Brain Injury

    doi: 10.1371/journal.pone.0013756

    Figure Lengend Snippet: Death of dopaminergic neurons and microglia in the SNpc induced by ATP. ( A ) ATP (100 nmol in 2 µl PBS) or PBS (2 µl) was unilaterally injected into SNpc (*, injection sites), and brains were obtained after 3 h. Brain sections (30 µm thickness) of the midbrain including the entire SN were prepared, every sixth serial section selected and stained with TH (upper panel) and Iba-1 (lower panel) antibodies, and visualized with biotin-conjugated secondary antibodies and enzymatic detection with the avidin/biotin system unless indicated. At 100 nmol, mild neuronal and microglial damage occurred, thus, 100 nmol ATP was employed for in vivo experiments in this study. Photographs of the most damaged sections were obtained. The contralateral side (contra) and PBS-injected rat brain sections were used as control. ( B ) Serial sections obtained at 3 h were labeled with TH (left panel), Iba-1 (middle panel), and TH/Iba-1 (right panel) antibodies. For visualization of the double-labeling, color reactions using DAB (for TH) and DAB/nickel sulfate (for Iba-1) were applied. Dotted lines indicated damage areas. ( C ) Brain tissue obtained 3 h post ATP treatment was subjected to electron microscopy, as described in “ Materials and Methods ”. Nuclei of neuron (N, white arrow), astrocytes (A, white arrowhead), and microglia (M, black arrow) were shown in intact rat brain whereas cellular structures were severely disrupted in ATP-injected brain. Data in this study are representative of at least 5 animals. Scale bars, 200 µm (A); 100 µm (B); 5 µm (C).

    Article Snippet: Following rinsing in PBST, sections were incubated with biotinylated secondary antibodies (Vector Laboratories, Burlingame, CA) for 1 h and the avidin/biotin system (Vector Laboratories, Burlingame, CA) for 1 h and visualized using DAB solution (0.05% DAB and 0.003% hydrogen peroxide in 0.1 M PB).

    Techniques: Injection, Staining, Avidin-Biotin Assay, In Vivo, Labeling, Electron Microscopy

    D 2 and D 3 immunocytochemistry were performed on the submucosal plexus of the ileum of CD-1 mice. The same tissue preparation from D 2 and D 3 KO mice was used as control. D 2 receptor immunoreactivity (IR) was revealed by a D 2 rabbit antibody and a donkey anti-rabbit Alexa 594 secondary antibody. D 3 receptor immunoreactivity was revealed by a D 3 goat antibody, a biotinylated donkey anti-goat secondary antibody, and streptavidin FITC. On the tissue of CD-1 mice, D 2 -immunoreactive products were present in the enteric neurons ( A ), and D 3 -immunoreactive products were also present in the enteric neurons ( B ). D 2 and D 3 immunoreactivities were colocalized in the same cell ( C ). However, D 2 immunoreactivity was not detected on the tissue of D 2 knock-out (KO) mice ( D ); no D 3 immunoreactivity was detected on the tissue of D 3 knock-out mouse ( E ). The arrows indicate the immunoreactive neurons. Scale bar: (in C ) 25 μm.

    Journal: The Journal of Neuroscience

    Article Title: Physiological Modulation of Intestinal Motility by Enteric Dopaminergic Neurons and the D2 Receptor: Analysis of Dopamine Receptor Expression, Location, Development, and Function in Wild-Type and Knock-Out Mice

    doi: 10.1523/JNEUROSCI.4720-05.2006

    Figure Lengend Snippet: D 2 and D 3 immunocytochemistry were performed on the submucosal plexus of the ileum of CD-1 mice. The same tissue preparation from D 2 and D 3 KO mice was used as control. D 2 receptor immunoreactivity (IR) was revealed by a D 2 rabbit antibody and a donkey anti-rabbit Alexa 594 secondary antibody. D 3 receptor immunoreactivity was revealed by a D 3 goat antibody, a biotinylated donkey anti-goat secondary antibody, and streptavidin FITC. On the tissue of CD-1 mice, D 2 -immunoreactive products were present in the enteric neurons ( A ), and D 3 -immunoreactive products were also present in the enteric neurons ( B ). D 2 and D 3 immunoreactivities were colocalized in the same cell ( C ). However, D 2 immunoreactivity was not detected on the tissue of D 2 knock-out (KO) mice ( D ); no D 3 immunoreactivity was detected on the tissue of D 3 knock-out mouse ( E ). The arrows indicate the immunoreactive neurons. Scale bar: (in C ) 25 μm.

    Article Snippet: The blocked tissue was then incubated overnight with primary antibodies, washed with PBS, and exposed with intervening washes in PBS to the biotinylated secondary antibodies (2 h), 0.3% H2 O2 in 0.3% blocking sera (5 min), Elite ABC reagent (1 h; Vector Laboratories), and 3′,5′-diaminobenzidine solution (2–10 min) until suitable staining developed.

    Techniques: Immunocytochemistry, Mouse Assay, Knock-Out