goat anti rabbit igg  (Millipore)


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  • 99
    Name:
    Bismarck Brown R
    Description:
    Bismark Brown R BB also called as basic brown 4 belongs to the class of diazo dyes It has the absorption maximum at 468nm
    Catalog Number:
    15000
    Price:
    None
    Applications:
    Bismarck Brown R has been used as an adsorbate and is used in dye decoloration experiment.
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    Structured Review

    Millipore goat anti rabbit igg
    Bismarck Brown R
    Bismark Brown R BB also called as basic brown 4 belongs to the class of diazo dyes It has the absorption maximum at 468nm
    https://www.bioz.com/result/goat anti rabbit igg/product/Millipore
    Average 99 stars, based on 40 article reviews
    Price from $9.99 to $1999.99
    goat anti rabbit igg - by Bioz Stars, 2020-08
    99/100 stars

    Images

    1) Product Images from "Absence of CD59 in guinea pigs: analysis of the Cavia Porcellus genome suggests the evolution of a CD59 pseudogene"

    Article Title: Absence of CD59 in guinea pigs: analysis of the Cavia Porcellus genome suggests the evolution of a CD59 pseudogene

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    doi: 10.4049/jimmunol.1701238

    Flow cytometric analysis of CD59 expression on erythrocytes. Guinea pig (I), CD59 deficient mouse (-CD59) (II), human (III) and wild-type mouse (+CD59) (IV) erythrocytes were stained with monoclonal anti-human CD59 MEM43 (E), monoclonal rat anti-mouse CD59a (F) or two different polyclonal anti-CD59a (G = anti CD59a.1, H = anti CD59a.2) followed by appropriate fluorescein FITC-labelled secondary antibodies, then analyses by flow cytometry. Controls are: A = unstained cells, B = donkey anti-Mouse IgG, C = rabbit anti-rat IgG, D = goat anti-Rabbit IgG; all are overlapping and negative on each of the histograms.). Positive staining for CD59 was observed on human erythrocytes and on wild-type mouse erythrocytes (F, G, H) with the species-specific monoclonal and the two polyclonal antibodies (E, G, H). In contrast, guinea pig erythrocytes and erythrocytes from CD59a-deficient mice were negative for all antibodies tested.
    Figure Legend Snippet: Flow cytometric analysis of CD59 expression on erythrocytes. Guinea pig (I), CD59 deficient mouse (-CD59) (II), human (III) and wild-type mouse (+CD59) (IV) erythrocytes were stained with monoclonal anti-human CD59 MEM43 (E), monoclonal rat anti-mouse CD59a (F) or two different polyclonal anti-CD59a (G = anti CD59a.1, H = anti CD59a.2) followed by appropriate fluorescein FITC-labelled secondary antibodies, then analyses by flow cytometry. Controls are: A = unstained cells, B = donkey anti-Mouse IgG, C = rabbit anti-rat IgG, D = goat anti-Rabbit IgG; all are overlapping and negative on each of the histograms.). Positive staining for CD59 was observed on human erythrocytes and on wild-type mouse erythrocytes (F, G, H) with the species-specific monoclonal and the two polyclonal antibodies (E, G, H). In contrast, guinea pig erythrocytes and erythrocytes from CD59a-deficient mice were negative for all antibodies tested.

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

    2) Product Images from "The amyloid fold of Gad m 1 epitopes governs IgE binding"

    Article Title: The amyloid fold of Gad m 1 epitopes governs IgE binding

    Journal: Scientific Reports

    doi: 10.1038/srep32801

    Location and relation of the immunoreactive and amyloid forming regions in the Gad m 1 chain ( a ) Sequence and location of the following regions in the Gad m 1 chain: ?(i) IgE-binding epitopes found in sera groups S-I (black and underlined) and S-II (navy blue and underlined), (ii) IgG4-binding epitopes found in S-I (pink) and S-II (orange), (iii) OC-binding segments (green), (iv) adhesive regions identified by the ZipperDB algorithm (light blue), and (v) sequence changes in the A, C and E regions (red). The sequence changes were based on the sequences of the following β-parvalbumins: (i) Q91482, Q90YK8 and E0WDA2 for A, (ii) Q90YL0, Q91482, Q91483, E0WDA2 and Q90YK8 for C, and (iii) C6GKU7 for E 36 . (b) Comparative ZipperDB analysis of the Gad m1 wt and ACE mutant chains. Red bars indicate the N-terminus of a hexapeptide with adhesive properties. The effects of the adhesive segments are depicted by rectangles and were conserved in the analysis of chains containing single A, C and E modifications.
    Figure Legend Snippet: Location and relation of the immunoreactive and amyloid forming regions in the Gad m 1 chain ( a ) Sequence and location of the following regions in the Gad m 1 chain: ?(i) IgE-binding epitopes found in sera groups S-I (black and underlined) and S-II (navy blue and underlined), (ii) IgG4-binding epitopes found in S-I (pink) and S-II (orange), (iii) OC-binding segments (green), (iv) adhesive regions identified by the ZipperDB algorithm (light blue), and (v) sequence changes in the A, C and E regions (red). The sequence changes were based on the sequences of the following β-parvalbumins: (i) Q91482, Q90YK8 and E0WDA2 for A, (ii) Q90YL0, Q91482, Q91483, E0WDA2 and Q90YK8 for C, and (iii) C6GKU7 for E 36 . (b) Comparative ZipperDB analysis of the Gad m1 wt and ACE mutant chains. Red bars indicate the N-terminus of a hexapeptide with adhesive properties. The effects of the adhesive segments are depicted by rectangles and were conserved in the analysis of chains containing single A, C and E modifications.

    Techniques Used: Sequencing, Binding Assay, Mutagenesis

    Reactivity of Gad m 1 chain. ( a ) Regions binding IgE in sera from fish-allergic patients. ( b ) Regions binding IgG4 in sera from fish-allergic patients. ( c ) Sequences with anti-amyloid OC antibody reactivity and ThT binding properties. ( d ) Relative signal of the binding of IgE and IgG4 from the sera of fish-allergic patients and the anti-amyloid OC antibody to the distinct overlapping peptides representing the Gad m 1 sequence. Signals corresponding to the IgE and IgG4 binding are displayed as the average and standard deviations of the signals of sera groups S-I (S2, S3, S4, S7, and S8) and S-II (S1, S5, S6, S12, and S13) are shown. Peptides are indicated by numbers on the top (row A: peptides 1–30, row B: peptides 31–50) and their sequences are displayed in Supplementary Fig. S1 . The sera are depicted as Si, where i is a number ( Supplementary Table S1 ).
    Figure Legend Snippet: Reactivity of Gad m 1 chain. ( a ) Regions binding IgE in sera from fish-allergic patients. ( b ) Regions binding IgG4 in sera from fish-allergic patients. ( c ) Sequences with anti-amyloid OC antibody reactivity and ThT binding properties. ( d ) Relative signal of the binding of IgE and IgG4 from the sera of fish-allergic patients and the anti-amyloid OC antibody to the distinct overlapping peptides representing the Gad m 1 sequence. Signals corresponding to the IgE and IgG4 binding are displayed as the average and standard deviations of the signals of sera groups S-I (S2, S3, S4, S7, and S8) and S-II (S1, S5, S6, S12, and S13) are shown. Peptides are indicated by numbers on the top (row A: peptides 1–30, row B: peptides 31–50) and their sequences are displayed in Supplementary Fig. S1 . The sera are depicted as Si, where i is a number ( Supplementary Table S1 ).

    Techniques Used: Binding Assay, Fluorescence In Situ Hybridization, Sequencing

    3) Product Images from "Engineering Peptide Linkers for scFv Immunosensors"

    Article Title: Engineering Peptide Linkers for scFv Immunosensors

    Journal: Analytical chemistry

    doi: 10.1021/ac7018624

    ELISA results for different scFvs on rabbit IgG, human IgG, rat IgG, goat IgG, bovine IgG, and BSA (A) scFv-RG3, (B) scFv-Cys, (C) scFv-His, (D) scFv-ZnS4, (E) scFv-CDS6, (F) scFv-RS, and negative controls: (G) I-20 scFv-RS specific for P450 CYP1B1, (H) D-11 scFv-Cys specific for isoketal protein adduct. Insertion depicts ELISA results for varying concentrations of rabbit IgG (1.25 to 0.019 µg/mL) binding with scFv-RG3.
    Figure Legend Snippet: ELISA results for different scFvs on rabbit IgG, human IgG, rat IgG, goat IgG, bovine IgG, and BSA (A) scFv-RG3, (B) scFv-Cys, (C) scFv-His, (D) scFv-ZnS4, (E) scFv-CDS6, (F) scFv-RS, and negative controls: (G) I-20 scFv-RS specific for P450 CYP1B1, (H) D-11 scFv-Cys specific for isoketal protein adduct. Insertion depicts ELISA results for varying concentrations of rabbit IgG (1.25 to 0.019 µg/mL) binding with scFv-RG3.

    Techniques Used: Enzyme-linked Immunosorbent Assay, Binding Assay

    4) Product Images from "Epidermal growth factor receptor levels are reduced in mice with targeted disruption of the protein kinase A catalytic subunit"

    Article Title: Epidermal growth factor receptor levels are reduced in mice with targeted disruption of the protein kinase A catalytic subunit

    Journal: BMC Cell Biology

    doi: 10.1186/1471-2121-9-16

    Effect of PKA Cα or Cβ ablation on EGFR expression. (a) Comparison of liver from wild type and PKA Cα and Cβ ablated mice. PKA Cα KO mice showed a clear uniform reduction in size. (b) Confocal immunofluorescence microscopy of frozen liver sections stained by sheep anti-EGFR and Cy3-conjugated donkey anti-sheep antibodies. (c) Western immunoblotting analysis of EGFR expression in liver and brain from wt (+/+), heterozygote (-/+), and Cα and Cβ KO (-/-) mice. Immunoblots were incubated with sheep anti-EGFR, rabbit anti-pan PKA C and mouse anti-PKA C, and rabbit anti-erbB2. Secondary HRP-conjugated anti-IgG antibodies were used for detection. (d) PKA kinase activity in mouse liver. Activity was assayed by phosphorylation of the PKA-specific substrate Kemptide using γ-[ 32 P]ATP. The assay was performed in the presence of cAMP. Activity was measured by liquid scintillation in 3 ml Opti-fluor. Values are given as counts per minute (cpm).
    Figure Legend Snippet: Effect of PKA Cα or Cβ ablation on EGFR expression. (a) Comparison of liver from wild type and PKA Cα and Cβ ablated mice. PKA Cα KO mice showed a clear uniform reduction in size. (b) Confocal immunofluorescence microscopy of frozen liver sections stained by sheep anti-EGFR and Cy3-conjugated donkey anti-sheep antibodies. (c) Western immunoblotting analysis of EGFR expression in liver and brain from wt (+/+), heterozygote (-/+), and Cα and Cβ KO (-/-) mice. Immunoblots were incubated with sheep anti-EGFR, rabbit anti-pan PKA C and mouse anti-PKA C, and rabbit anti-erbB2. Secondary HRP-conjugated anti-IgG antibodies were used for detection. (d) PKA kinase activity in mouse liver. Activity was assayed by phosphorylation of the PKA-specific substrate Kemptide using γ-[ 32 P]ATP. The assay was performed in the presence of cAMP. Activity was measured by liquid scintillation in 3 ml Opti-fluor. Values are given as counts per minute (cpm).

    Techniques Used: Expressing, Mouse Assay, Immunofluorescence, Microscopy, Staining, Western Blot, Incubation, Activity Assay

    5) Product Images from "Characterization of two functional NKX3.1 binding sites upstream of the PCAN1 gene that are involved in the positive regulation of PCAN1 gene transcription"

    Article Title: Characterization of two functional NKX3.1 binding sites upstream of the PCAN1 gene that are involved in the positive regulation of PCAN1 gene transcription

    Journal: BMC Molecular Biology

    doi: 10.1186/1471-2199-9-45

    NKX3.1 binds to the NBSs of the PCAN1 promoter in living cells . LNCaP cells transfected with pcDNA3.1- NKX3.1 were cross-linked by formaldehyde treatment and lysed. Cell lysates were subjected to immunoprecipitation with either an antibody to NKX3.1 (A) or rabbit IgG (B). Four primers (names and sequences are shown in Table 1) spanning five NBSs of PCAN1 promoter region were used for PCR of recovered DNA from the immunoprecipitation (lanes 2–5). Input DNA was used as positive control (C).
    Figure Legend Snippet: NKX3.1 binds to the NBSs of the PCAN1 promoter in living cells . LNCaP cells transfected with pcDNA3.1- NKX3.1 were cross-linked by formaldehyde treatment and lysed. Cell lysates were subjected to immunoprecipitation with either an antibody to NKX3.1 (A) or rabbit IgG (B). Four primers (names and sequences are shown in Table 1) spanning five NBSs of PCAN1 promoter region were used for PCR of recovered DNA from the immunoprecipitation (lanes 2–5). Input DNA was used as positive control (C).

    Techniques Used: Transfection, Immunoprecipitation, Polymerase Chain Reaction, Positive Control

    6) Product Images from "ZNF265--a novel spliceosomal protein able to induce alternative splicing"

    Article Title: ZNF265--a novel spliceosomal protein able to induce alternative splicing

    Journal: The Journal of Cell Biology

    doi: 10.1083/jcb.200010059

    Subcellular colocalization of endogenous ZNF265 with endogenous nuclear factors. (A) Immunoblotting assay demonstrates specific recognition of ZNF265 by the polyclonal ZNF265 antibody (the arrow shows a 55-kD band), which was competed by ZNF265 oligopeptide antigen (2.5 μg/ml) in three replicate experiments. (B) Subcellular localization of various protein factors. Fixed Calu-6 cells were exposed to: (1st column) monoclonal antibodies against splicing factors U1-70K, Sm antigen, SC35, SMN, or transcriptosomal factors p300 and YY1, in respective rows, before incubation with Alexa 594 anti–mouse IgG (red); (2nd column) staining with anti-ZNF265 and detection with Alexa 488–conjugated anti–rabbit IgG (green); (3rd column) DAPI staining of nucleus (blue); (4th column) digital overlay of Z-series projections shown in columns 1 and 2 to demonstrate colocalization (yellow); (5th column) scattergrams of the overlayed projection shown in column 4. Each row represents the same field (width × height = 60 × 60 μm), acquired using three-channel confocal microscopy.
    Figure Legend Snippet: Subcellular colocalization of endogenous ZNF265 with endogenous nuclear factors. (A) Immunoblotting assay demonstrates specific recognition of ZNF265 by the polyclonal ZNF265 antibody (the arrow shows a 55-kD band), which was competed by ZNF265 oligopeptide antigen (2.5 μg/ml) in three replicate experiments. (B) Subcellular localization of various protein factors. Fixed Calu-6 cells were exposed to: (1st column) monoclonal antibodies against splicing factors U1-70K, Sm antigen, SC35, SMN, or transcriptosomal factors p300 and YY1, in respective rows, before incubation with Alexa 594 anti–mouse IgG (red); (2nd column) staining with anti-ZNF265 and detection with Alexa 488–conjugated anti–rabbit IgG (green); (3rd column) DAPI staining of nucleus (blue); (4th column) digital overlay of Z-series projections shown in columns 1 and 2 to demonstrate colocalization (yellow); (5th column) scattergrams of the overlayed projection shown in column 4. Each row represents the same field (width × height = 60 × 60 μm), acquired using three-channel confocal microscopy.

    Techniques Used: Incubation, Staining, Confocal Microscopy

    7) Product Images from "Molecular Cloning and Characterization of a Surface-Localized Adhesion Protein in Mycoplasma bovis Hubei-1 Strain"

    Article Title: Molecular Cloning and Characterization of a Surface-Localized Adhesion Protein in Mycoplasma bovis Hubei-1 Strain

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0069644

    Assay of rVpmaX adhesion and adhesion inhibition to EBL cells visualized by confocal laser scanning microscopy. Active rVpmaX interacted with fixed EBL cells, and the surplus protein was rinsed away by washing with PBST. The attached protein was immunostained with rabbit anti-rVpmaX antibody and mouse anti-rabbit IgG-FITC. The EBL cell membranes were labeled with 1,19-dioctadecyl-3,3,3′,3′-tetramethylindocarbocyanine perchlorate (DiI), and the cell nuclei were counter-labeled with 49,6-diamidino-2-phenylindole (DAPI). (A1–A2) 10 µg rVpmaX adhering to EBL cells. (B) Adhesion inhibition of 10 µg rVpmaX to EBL cells by 10 µl rabbit anti-rVpmaX serum. (C) Adhesion of 20 µg rVpmaX to EBL cells. (D) The adhesion of 20 µg rVpmaX to EBL cells was inhibited by 20 µl rabbit anti-rVpmaX serum. (E) EBL cells without protein added.
    Figure Legend Snippet: Assay of rVpmaX adhesion and adhesion inhibition to EBL cells visualized by confocal laser scanning microscopy. Active rVpmaX interacted with fixed EBL cells, and the surplus protein was rinsed away by washing with PBST. The attached protein was immunostained with rabbit anti-rVpmaX antibody and mouse anti-rabbit IgG-FITC. The EBL cell membranes were labeled with 1,19-dioctadecyl-3,3,3′,3′-tetramethylindocarbocyanine perchlorate (DiI), and the cell nuclei were counter-labeled with 49,6-diamidino-2-phenylindole (DAPI). (A1–A2) 10 µg rVpmaX adhering to EBL cells. (B) Adhesion inhibition of 10 µg rVpmaX to EBL cells by 10 µl rabbit anti-rVpmaX serum. (C) Adhesion of 20 µg rVpmaX to EBL cells. (D) The adhesion of 20 µg rVpmaX to EBL cells was inhibited by 20 µl rabbit anti-rVpmaX serum. (E) EBL cells without protein added.

    Techniques Used: Inhibition, Confocal Laser Scanning Microscopy, Labeling

    8) Product Images from "Development and Application of Pathovar-Specific Monoclonal Antibodies That Recognize the Lipopolysaccharide O Antigen and the Type IV Fimbriae of Xanthomonas hyacinthi"

    Article Title: Development and Application of Pathovar-Specific Monoclonal Antibodies That Recognize the Lipopolysaccharide O Antigen and the Type IV Fimbriae of Xanthomonas hyacinthi

    Journal: Applied and Environmental Microbiology

    doi:

    Electron microscopy of immunogold-labeled cells of X. hyacinthi S148. The bacterial surface structures were labeled with 10-nm-diameter gold-conjugated anti-mouse IgG and IgM after incubation with MAbs 2E5 (A), 6C9 (B), 9A2 (C), and 5G8 (D). Panels B to D show fimbrial structures that are gold tagged; arrows indicate unlabeled fimbriae (C). In panel A, the cell surface LPS is labeled. Bars, 1 μm.
    Figure Legend Snippet: Electron microscopy of immunogold-labeled cells of X. hyacinthi S148. The bacterial surface structures were labeled with 10-nm-diameter gold-conjugated anti-mouse IgG and IgM after incubation with MAbs 2E5 (A), 6C9 (B), 9A2 (C), and 5G8 (D). Panels B to D show fimbrial structures that are gold tagged; arrows indicate unlabeled fimbriae (C). In panel A, the cell surface LPS is labeled. Bars, 1 μm.

    Techniques Used: Electron Microscopy, Labeling, Incubation

    9) Product Images from "The amyloid fold of Gad m 1 epitopes governs IgE binding"

    Article Title: The amyloid fold of Gad m 1 epitopes governs IgE binding

    Journal: Scientific Reports

    doi: 10.1038/srep32801

    Location and relation of the immunoreactive and amyloid forming regions in the Gad m 1 chain ( a ) Sequence and location of the following regions in the Gad m 1 chain: ?(i) IgE-binding epitopes found in sera groups S-I (black and underlined) and S-II (navy blue and underlined), (ii) IgG4-binding epitopes found in S-I (pink) and S-II (orange), (iii) OC-binding segments (green), (iv) adhesive regions identified by the ZipperDB algorithm (light blue), and (v) sequence changes in the A, C and E regions (red). The sequence changes were based on the sequences of the following β-parvalbumins: (i) Q91482, Q90YK8 and E0WDA2 for A, (ii) Q90YL0, Q91482, Q91483, E0WDA2 and Q90YK8 for C, and (iii) C6GKU7 for E 36 . (b) Comparative ZipperDB analysis of the Gad m1 wt and ACE mutant chains. Red bars indicate the N-terminus of a hexapeptide with adhesive properties. The effects of the adhesive segments are depicted by rectangles and were conserved in the analysis of chains containing single A, C and E modifications.
    Figure Legend Snippet: Location and relation of the immunoreactive and amyloid forming regions in the Gad m 1 chain ( a ) Sequence and location of the following regions in the Gad m 1 chain: ?(i) IgE-binding epitopes found in sera groups S-I (black and underlined) and S-II (navy blue and underlined), (ii) IgG4-binding epitopes found in S-I (pink) and S-II (orange), (iii) OC-binding segments (green), (iv) adhesive regions identified by the ZipperDB algorithm (light blue), and (v) sequence changes in the A, C and E regions (red). The sequence changes were based on the sequences of the following β-parvalbumins: (i) Q91482, Q90YK8 and E0WDA2 for A, (ii) Q90YL0, Q91482, Q91483, E0WDA2 and Q90YK8 for C, and (iii) C6GKU7 for E 36 . (b) Comparative ZipperDB analysis of the Gad m1 wt and ACE mutant chains. Red bars indicate the N-terminus of a hexapeptide with adhesive properties. The effects of the adhesive segments are depicted by rectangles and were conserved in the analysis of chains containing single A, C and E modifications.

    Techniques Used: Sequencing, Binding Assay, Mutagenesis

    Reactivity of Gad m 1 chain. ( a ) Regions binding IgE in sera from fish-allergic patients. ( b ) Regions binding IgG4 in sera from fish-allergic patients. ( c ) Sequences with anti-amyloid OC antibody reactivity and ThT binding properties. ( d ) Relative signal of the binding of IgE and IgG4 from the sera of fish-allergic patients and the anti-amyloid OC antibody to the distinct overlapping peptides representing the Gad m 1 sequence. Signals corresponding to the IgE and IgG4 binding are displayed as the average and standard deviations of the signals of sera groups S-I (S2, S3, S4, S7, and S8) and S-II (S1, S5, S6, S12, and S13) are shown. Peptides are indicated by numbers on the top (row A: peptides 1–30, row B: peptides 31–50) and their sequences are displayed in Supplementary Fig. S1 . The sera are depicted as Si, where i is a number ( Supplementary Table S1 ).
    Figure Legend Snippet: Reactivity of Gad m 1 chain. ( a ) Regions binding IgE in sera from fish-allergic patients. ( b ) Regions binding IgG4 in sera from fish-allergic patients. ( c ) Sequences with anti-amyloid OC antibody reactivity and ThT binding properties. ( d ) Relative signal of the binding of IgE and IgG4 from the sera of fish-allergic patients and the anti-amyloid OC antibody to the distinct overlapping peptides representing the Gad m 1 sequence. Signals corresponding to the IgE and IgG4 binding are displayed as the average and standard deviations of the signals of sera groups S-I (S2, S3, S4, S7, and S8) and S-II (S1, S5, S6, S12, and S13) are shown. Peptides are indicated by numbers on the top (row A: peptides 1–30, row B: peptides 31–50) and their sequences are displayed in Supplementary Fig. S1 . The sera are depicted as Si, where i is a number ( Supplementary Table S1 ).

    Techniques Used: Binding Assay, Fluorescence In Situ Hybridization, Sequencing

    10) Product Images from "Utilization of Complement-Dependent Cytotoxicity To Measure Low Levels of Antibodies: Application to Nonstructural Protein 1 in a Model of Japanese Encephalitis Virus ▿"

    Article Title: Utilization of Complement-Dependent Cytotoxicity To Measure Low Levels of Antibodies: Application to Nonstructural Protein 1 in a Model of Japanese Encephalitis Virus ▿

    Journal:

    doi: 10.1128/CVI.00347-07

    Time course of NS1 antibody levels/titers in mice infected with JEV. Sera were examined by the one-dilution (A) or endpoint (B) method of the CDC assay and ELISA for measuring IgG (C) or IgM (D) antibodies. The sera used in this experiment were collected
    Figure Legend Snippet: Time course of NS1 antibody levels/titers in mice infected with JEV. Sera were examined by the one-dilution (A) or endpoint (B) method of the CDC assay and ELISA for measuring IgG (C) or IgM (D) antibodies. The sera used in this experiment were collected

    Techniques Used: Mouse Assay, Infection, CDC Assay, Enzyme-linked Immunosorbent Assay

    Percentages of specific cell lysis obtained with the day-4 serum or HMS depleted of IgG or IgM as determined by the one-dilution method of the CDC assay. Serum was incubated with anti-mouse IgG or IgM and examined for depletion by a sandwich ELISA for
    Figure Legend Snippet: Percentages of specific cell lysis obtained with the day-4 serum or HMS depleted of IgG or IgM as determined by the one-dilution method of the CDC assay. Serum was incubated with anti-mouse IgG or IgM and examined for depletion by a sandwich ELISA for

    Techniques Used: Lysis, CDC Assay, Incubation, Sandwich ELISA

    11) Product Images from "Upregulated SLC22A3 has a potential for improving survival of patients with head and neck squamous cell carcinoma receiving cisplatin treatment"

    Article Title: Upregulated SLC22A3 has a potential for improving survival of patients with head and neck squamous cell carcinoma receiving cisplatin treatment

    Journal: Oncotarget

    doi: 10.18632/oncotarget.20637

    Uptake of cisplatin by SCC-4 and SCC-25 cells ( A ) SCC-4 and SLC22A3 (OCT) -overexpressing SCC-4 cells and ( B ) SCC-25 and SLC22A3 (OCT) -knocked down SCC-25 cells were treated with 50 μM cisplatin for 6 hours. Confocal microscopy was performed using anti-cisplatin-modified DNA antibody (primary antibody) plus TRITC-labelled goat anti-rabbit IgG (secondary antibody) and anti-SLC22A3 (OCT) antibody (primary antibody) plus Alexa Fluor 488-labelled goat anti-rat IgG (secondary antibody). DNA was counterstained with DAPI. The red signal represents SLC22A3 protein and the blue signal represents nucleus. The green signal represents influx of cisplatin-binding DNA.
    Figure Legend Snippet: Uptake of cisplatin by SCC-4 and SCC-25 cells ( A ) SCC-4 and SLC22A3 (OCT) -overexpressing SCC-4 cells and ( B ) SCC-25 and SLC22A3 (OCT) -knocked down SCC-25 cells were treated with 50 μM cisplatin for 6 hours. Confocal microscopy was performed using anti-cisplatin-modified DNA antibody (primary antibody) plus TRITC-labelled goat anti-rabbit IgG (secondary antibody) and anti-SLC22A3 (OCT) antibody (primary antibody) plus Alexa Fluor 488-labelled goat anti-rat IgG (secondary antibody). DNA was counterstained with DAPI. The red signal represents SLC22A3 protein and the blue signal represents nucleus. The green signal represents influx of cisplatin-binding DNA.

    Techniques Used: Confocal Microscopy, Modification, Binding Assay

    12) Product Images from "A multivalent Kaposi sarcoma-associated herpesvirus-like particle vaccine capable of eliciting high titers of neutralizing antibodies in immunized rabbits"

    Article Title: A multivalent Kaposi sarcoma-associated herpesvirus-like particle vaccine capable of eliciting high titers of neutralizing antibodies in immunized rabbits

    Journal: Vaccine

    doi: 10.1016/j.vaccine.2019.04.071

    KSHV-glycoprotein-specific IgG titers in immunized New Zealand white rabbits. (a) Coomassie stain (left) and immunoblot (right) of KSHV gpK8.1, gB, and gH/gL recombinant Fc-His tagged proteins. Fc-6xHis-tagged recombinant KSHV gpK8.1, gB, and gH/gL proteins were expressed by transiently transfecting HEK-293–6E cells. Culture media was harvested six days post-transfection by centrifugation and filtration through a 0.22 µM. Fc-6xHis-tagged KSHV proteins in the media were purified using protein A spin-columns, concentrated in PBS using Amicon Ultra 15 centrifugal filter units, and quantified using a nanodrop spectrophotometer. To confirm the specificity of the proteins, the concentrated proteins were separated on a 4–12% SDS-PAGE and detected by Coomassie blue stain (for molecular weight) or transferred to a polyvinylidene fluoride membrane for immunoblot analysis using monoclonal anti-gpK8.1 or anti-gH/gL or polyclonal goat anti-human Fc (gB) antibodies as indicated. (b) Immunization and bleeding schedules of wild-type New Zealand white rabbits. Eight- to 10-week-old rabbits (n = 6/treatment) were immunized subcutaneously at Days 0, 28 and 42 with 50 µg purified KSHV-LPs−/+HR2, UV-inactivated KSHV, or TNE buffer, all adsorbed to alum and MPL as adjuvants. Immunized rabbits were bled seven days pre-immunization (−7) and on Days 14, 35, 49, 70, and 90 (terminal bleed). (c) Serum KSHV glycoprotein-specific antibody responses. KSHV-glycoprotein IgG-specific antibody titers in diluted (1:300 and 1:900) sera from immunized rabbits were determined using ELISA with recombinant tagged gpK8.1, gB, and gH/gL proteins; results of quadruplicate replicates for each of the six animals per group are expressed as mean ± standard deviation (SD). Differences in antibody titers between all groups were analyzed using a Kruskal-Wallis test; differences between the −HR2 and+HR2 vaccine were assessed using a Mann-Whitney test. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)
    Figure Legend Snippet: KSHV-glycoprotein-specific IgG titers in immunized New Zealand white rabbits. (a) Coomassie stain (left) and immunoblot (right) of KSHV gpK8.1, gB, and gH/gL recombinant Fc-His tagged proteins. Fc-6xHis-tagged recombinant KSHV gpK8.1, gB, and gH/gL proteins were expressed by transiently transfecting HEK-293–6E cells. Culture media was harvested six days post-transfection by centrifugation and filtration through a 0.22 µM. Fc-6xHis-tagged KSHV proteins in the media were purified using protein A spin-columns, concentrated in PBS using Amicon Ultra 15 centrifugal filter units, and quantified using a nanodrop spectrophotometer. To confirm the specificity of the proteins, the concentrated proteins were separated on a 4–12% SDS-PAGE and detected by Coomassie blue stain (for molecular weight) or transferred to a polyvinylidene fluoride membrane for immunoblot analysis using monoclonal anti-gpK8.1 or anti-gH/gL or polyclonal goat anti-human Fc (gB) antibodies as indicated. (b) Immunization and bleeding schedules of wild-type New Zealand white rabbits. Eight- to 10-week-old rabbits (n = 6/treatment) were immunized subcutaneously at Days 0, 28 and 42 with 50 µg purified KSHV-LPs−/+HR2, UV-inactivated KSHV, or TNE buffer, all adsorbed to alum and MPL as adjuvants. Immunized rabbits were bled seven days pre-immunization (−7) and on Days 14, 35, 49, 70, and 90 (terminal bleed). (c) Serum KSHV glycoprotein-specific antibody responses. KSHV-glycoprotein IgG-specific antibody titers in diluted (1:300 and 1:900) sera from immunized rabbits were determined using ELISA with recombinant tagged gpK8.1, gB, and gH/gL proteins; results of quadruplicate replicates for each of the six animals per group are expressed as mean ± standard deviation (SD). Differences in antibody titers between all groups were analyzed using a Kruskal-Wallis test; differences between the −HR2 and+HR2 vaccine were assessed using a Mann-Whitney test. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Techniques Used: Staining, Recombinant, Transfection, Centrifugation, Filtration, Purification, Spectrophotometry, SDS Page, Molecular Weight, Enzyme-linked Immunosorbent Assay, Standard Deviation, MANN-WHITNEY

    13) Product Images from "Role of Cyclin D3 in the Biology of Herpes Simplex Virus 1 ICP0"

    Article Title: Role of Cyclin D3 in the Biology of Herpes Simplex Virus 1 ICP0

    Journal: Journal of Virology

    doi: 10.1128/JVI.75.4.1888-1898.2001

    Digital images of HEL fibroblasts infected with HSV-1(F) or R7914 (D199A mutant) and reacted with antibodies to ICP0 and PML. The infected cells were fixed at 3 and 6 h after infection and reacted with a mouse monoclonal antibody to PML and a rabbit polyclonal antibody to ICP0. The secondary antibodies were anti-mouse IgG conjugated to Texas red and rabbit IgG conjugated to fluorescein isothiocyanate. Left and middle columns, single-color images captured separately; right column, merged images. The yellow color visualized in the overlaid image represents colocalization of ICP0 and PML. The images were captured with a Zeiss confocal microscope and software provided by Ziess. The digitized images were not modified subsequent to capture.
    Figure Legend Snippet: Digital images of HEL fibroblasts infected with HSV-1(F) or R7914 (D199A mutant) and reacted with antibodies to ICP0 and PML. The infected cells were fixed at 3 and 6 h after infection and reacted with a mouse monoclonal antibody to PML and a rabbit polyclonal antibody to ICP0. The secondary antibodies were anti-mouse IgG conjugated to Texas red and rabbit IgG conjugated to fluorescein isothiocyanate. Left and middle columns, single-color images captured separately; right column, merged images. The yellow color visualized in the overlaid image represents colocalization of ICP0 and PML. The images were captured with a Zeiss confocal microscope and software provided by Ziess. The digitized images were not modified subsequent to capture.

    Techniques Used: Infection, Mutagenesis, Microscopy, Software, Modification

    Digital images of HSV-1(F) and recombinant R7914-infected HEL cells reacted with antibody to ICP0 at early and late times of infection. The infected cells were fixed 3 or 12 h after infection and reacted with polyclonal rabbit antibody to ICP0 and then reacted with anti-rabbit IgG conjugated to fluorescein isothiocyanate. The single-color images were captured with a Zeiss confocal microscope and software provided by Ziess. The digitized images were not modified subsequent to capture.
    Figure Legend Snippet: Digital images of HSV-1(F) and recombinant R7914-infected HEL cells reacted with antibody to ICP0 at early and late times of infection. The infected cells were fixed 3 or 12 h after infection and reacted with polyclonal rabbit antibody to ICP0 and then reacted with anti-rabbit IgG conjugated to fluorescein isothiocyanate. The single-color images were captured with a Zeiss confocal microscope and software provided by Ziess. The digitized images were not modified subsequent to capture.

    Techniques Used: Recombinant, Infection, Microscopy, Software, Modification

    14) Product Images from "The Localization of Myosin VI at the Golgi Complex and Leading Edge of Fibroblasts and Its Phosphorylation and Recruitment into Membrane Ruffles of A431 Cells after Growth Factor Stimulation "

    Article Title: The Localization of Myosin VI at the Golgi Complex and Leading Edge of Fibroblasts and Its Phosphorylation and Recruitment into Membrane Ruffles of A431 Cells after Growth Factor Stimulation

    Journal: The Journal of Cell Biology

    doi:

    Localization of myosin VI, V, and ezrin in A431 cells after stimulation with EGF. Cells were fixed at 0, 2, 5, and 15 min after addition of EGF and stained with rabbit polyclonal antibodies to myosin VI (affinity-purified PGT ab), myosin V (affinity-purified tail domain ab), and ezrin (affinity-purified ab) followed by fluorescently labeled anti–rabbit IgG. Extended focus projections of a z-series of images obtained by confocal microscopy are shown. Bar, 20 μm.
    Figure Legend Snippet: Localization of myosin VI, V, and ezrin in A431 cells after stimulation with EGF. Cells were fixed at 0, 2, 5, and 15 min after addition of EGF and stained with rabbit polyclonal antibodies to myosin VI (affinity-purified PGT ab), myosin V (affinity-purified tail domain ab), and ezrin (affinity-purified ab) followed by fluorescently labeled anti–rabbit IgG. Extended focus projections of a z-series of images obtained by confocal microscopy are shown. Bar, 20 μm.

    Techniques Used: Staining, Affinity Purification, Labeling, Confocal Microscopy

    15) Product Images from "Activation-induced nuclear translocation of RING3"

    Article Title: Activation-induced nuclear translocation of RING3

    Journal: Journal of cell science

    doi:

    Nuclear translocation of endogenous RING3 protein after serum stimulation. RING3 protein was visualised with rabbit anti-RING3 primary antibody and goat anti-rabbit IgG-FITC secondary. (A) Starved BALB cells; (B) differential interference contrast (dic); (C) serum-stimulated; (D) dic. Bars, 10 µm.
    Figure Legend Snippet: Nuclear translocation of endogenous RING3 protein after serum stimulation. RING3 protein was visualised with rabbit anti-RING3 primary antibody and goat anti-rabbit IgG-FITC secondary. (A) Starved BALB cells; (B) differential interference contrast (dic); (C) serum-stimulated; (D) dic. Bars, 10 µm.

    Techniques Used: Translocation Assay

    16) Product Images from "Intracellular Localization of Poliovirus Plus- and Minus-Strand RNA Visualized by Strand-Specific Fluorescent In Situ Hybridization"

    Article Title: Intracellular Localization of Poliovirus Plus- and Minus-Strand RNA Visualized by Strand-Specific Fluorescent In Situ Hybridization

    Journal: Journal of Virology

    doi:

    Viral RNA and protein detected in PV-infected HEp-2 cells by fluorescent confocal microscopy. Bar, 5 μm. (A) Simultaneous visualization of viral plus- and minus-strand RNA in the same cell by double-labelling FISH. Plus-strand RNA (panels a and d), detected with a Texas red-labelled riboprobe of minus polarity, is found in several small granules, at first dispersed and later in infection concentrated in a juxtanuclear area. Minus-strand RNA (panels b and e), detected with an FITC-labelled riboprobe of plus polarity, is present in larger, distinct granules. Superimposed plus- and minus-strand detection shows colocalization of both signals in yellow (panels c and f). Panels a to c, 2.5 h p.i.; panels d to f, 3.5 h p.i. (B) Minus-strand RNA, detected with an FITC-labelled riboprobe as for panel A, remains in distinct granules throughout the replication cycle. Panel a, 2.25 h p.i.; panel b, 2.5 h p.i.; panel c, 3.0 h p.i.; panel d, 3.5 h p.i. (C) Simultaneous visualization of viral plus-strand RNA and viral protein 2C by combined FISH and IF. Plus-strand RNA (panels a and d) is detected with an FITC-labelled riboprobe. Protein 2C and 2C-containing precursors (panels b and e) are detected with an anti-2C MAb and Texas red-labelled anti-mouse IgG. Superimposed FISH and IF show that early in infection, plus-strand RNA and 2C are colocalized (yellow in panel c); at later times some dissociation of 2C from RNA is visible (panel f). Panels a to c, 2.0 h p.i.; panels d to f, 3.5 h p.i. (D) IF with a MAb against Golgi protein p58 detected with Texas red-labelled anti-mouse IgG, combined with IF with a polyclonal rabbit anti-2C Ab detected with an FITC-labelled anti-rabbit IgG. Panel a, intact Golgi complexes at 2 h p.i. Panel b, the same cells as in panel a, showing IF with anti-2C Ab superimposed. Little colocalization (yellow) of the two targets is found. Panel c, superimposed pictures of a cell double labelled by IF with anti-p58 and anti-2C Ab at 2.5 h p.i. The Golgi marker and viral protein 2C colocalize partially. Panel d, superimposed pictures as in panels b and c at 3 h p.i. The Golgi marker is distributed in the cytoplasm and is colocalized with protein 2C mainly at the border of the juxtanuclear area of vesicles.
    Figure Legend Snippet: Viral RNA and protein detected in PV-infected HEp-2 cells by fluorescent confocal microscopy. Bar, 5 μm. (A) Simultaneous visualization of viral plus- and minus-strand RNA in the same cell by double-labelling FISH. Plus-strand RNA (panels a and d), detected with a Texas red-labelled riboprobe of minus polarity, is found in several small granules, at first dispersed and later in infection concentrated in a juxtanuclear area. Minus-strand RNA (panels b and e), detected with an FITC-labelled riboprobe of plus polarity, is present in larger, distinct granules. Superimposed plus- and minus-strand detection shows colocalization of both signals in yellow (panels c and f). Panels a to c, 2.5 h p.i.; panels d to f, 3.5 h p.i. (B) Minus-strand RNA, detected with an FITC-labelled riboprobe as for panel A, remains in distinct granules throughout the replication cycle. Panel a, 2.25 h p.i.; panel b, 2.5 h p.i.; panel c, 3.0 h p.i.; panel d, 3.5 h p.i. (C) Simultaneous visualization of viral plus-strand RNA and viral protein 2C by combined FISH and IF. Plus-strand RNA (panels a and d) is detected with an FITC-labelled riboprobe. Protein 2C and 2C-containing precursors (panels b and e) are detected with an anti-2C MAb and Texas red-labelled anti-mouse IgG. Superimposed FISH and IF show that early in infection, plus-strand RNA and 2C are colocalized (yellow in panel c); at later times some dissociation of 2C from RNA is visible (panel f). Panels a to c, 2.0 h p.i.; panels d to f, 3.5 h p.i. (D) IF with a MAb against Golgi protein p58 detected with Texas red-labelled anti-mouse IgG, combined with IF with a polyclonal rabbit anti-2C Ab detected with an FITC-labelled anti-rabbit IgG. Panel a, intact Golgi complexes at 2 h p.i. Panel b, the same cells as in panel a, showing IF with anti-2C Ab superimposed. Little colocalization (yellow) of the two targets is found. Panel c, superimposed pictures of a cell double labelled by IF with anti-p58 and anti-2C Ab at 2.5 h p.i. The Golgi marker and viral protein 2C colocalize partially. Panel d, superimposed pictures as in panels b and c at 3 h p.i. The Golgi marker is distributed in the cytoplasm and is colocalized with protein 2C mainly at the border of the juxtanuclear area of vesicles.

    Techniques Used: Infection, Confocal Microscopy, Fluorescence In Situ Hybridization, Marker

    17) Product Images from "The Maize Phytoene Synthase Gene Family: Overlapping Roles for Carotenogenesis in Endosperm, Photomorphogenesis, and Thermal Stress Tolerance"

    Article Title: The Maize Phytoene Synthase Gene Family: Overlapping Roles for Carotenogenesis in Endosperm, Photomorphogenesis, and Thermal Stress Tolerance

    Journal: Plant Physiology

    doi: 10.1104/pp.108.122119

    Localization of maize PSY1 in maize B73 endosperm. Endosperm dissected at 17 DAP was probed with: A, anti-maize PSY1 antiserum and anti-rabbit IgG FITC conjugate; or B, anti-rabbit IgG FITC conjugate only. Bar = 50 μ m (A) and 100 μ m (B). Arrow points to amyloplast within an endosperm cell.
    Figure Legend Snippet: Localization of maize PSY1 in maize B73 endosperm. Endosperm dissected at 17 DAP was probed with: A, anti-maize PSY1 antiserum and anti-rabbit IgG FITC conjugate; or B, anti-rabbit IgG FITC conjugate only. Bar = 50 μ m (A) and 100 μ m (B). Arrow points to amyloplast within an endosperm cell.

    Techniques Used:

    18) Product Images from "Elevated expression of syntenin in breast cancer is correlated with lymph node metastasis and poor patient survival"

    Article Title: Elevated expression of syntenin in breast cancer is correlated with lymph node metastasis and poor patient survival

    Journal: Breast Cancer Research : BCR

    doi: 10.1186/bcr3442

    Activation of integrin β1 and ERK1/2 is essential for syntenin-induced migration and invasion . (A) Silencing of syntenin in MDA-MB-231HM cells inhibited active integrin β1 expression and phosphorylation of ERK1/2, but had no effects on JNK and p38. (B) Overexpression of syntenin increased active integrin β1 expression and ERK1/2 phosphorylation in 231-SYN cells. The activation of ERK1/2 was analyzed with Western blot by using phosphor-specific antibodies. (C) Integrin β1 functional blocking antibody blocked both active integrin β1 expression and ERK1/2 phosphorylation. Cells were treated with integrin β1 or nonspecific IgG for 1 hour before protein extraction. (D) ERK1/2 inhibitor U0126 blocked activation of ERK1/2. Cells were pretreated with dimethylsulfoxide (DMSO) or 20 µ M U0126 (U0126) for 2 hours before protein extraction. (E, F) U0126 effectively reduced the migration and invasion of breast cancer cells. GAPDH was used as loading control. Data are expressed as means of triplicate samples from three independent experiments; bars, SD. ** P
    Figure Legend Snippet: Activation of integrin β1 and ERK1/2 is essential for syntenin-induced migration and invasion . (A) Silencing of syntenin in MDA-MB-231HM cells inhibited active integrin β1 expression and phosphorylation of ERK1/2, but had no effects on JNK and p38. (B) Overexpression of syntenin increased active integrin β1 expression and ERK1/2 phosphorylation in 231-SYN cells. The activation of ERK1/2 was analyzed with Western blot by using phosphor-specific antibodies. (C) Integrin β1 functional blocking antibody blocked both active integrin β1 expression and ERK1/2 phosphorylation. Cells were treated with integrin β1 or nonspecific IgG for 1 hour before protein extraction. (D) ERK1/2 inhibitor U0126 blocked activation of ERK1/2. Cells were pretreated with dimethylsulfoxide (DMSO) or 20 µ M U0126 (U0126) for 2 hours before protein extraction. (E, F) U0126 effectively reduced the migration and invasion of breast cancer cells. GAPDH was used as loading control. Data are expressed as means of triplicate samples from three independent experiments; bars, SD. ** P

    Techniques Used: Activation Assay, Migration, Multiple Displacement Amplification, Expressing, Over Expression, Western Blot, Functional Assay, Blocking Assay, Protein Extraction

    19) Product Images from "Leureptin: a soluble, extracellular leucine-rich repeat protein from Manduca sexta that binds lipopolysaccharide"

    Article Title: Leureptin: a soluble, extracellular leucine-rich repeat protein from Manduca sexta that binds lipopolysaccharide

    Journal: Insect biochemistry and molecular biology

    doi: 10.1016/j.ibmb.2010.07.002

    Association of leureptin with hemocyte membranes Hemocytes collected 24 h after injection of saline or M. luteus were fixed on glass slides. Anti-leureptin IgG and FITC-labeled goat-anti-rabbit antibody were used to detect leureptin as described in materials and methods. The upper panels show hemocytes viewed by phase contrast, and the lower panels show hemocytes viewed by fluorescence microscopy. Both plasmatocytes (indicated by arrows ) and granulocytes stained more intensely in bacteria-challenged insects. Oenocytoids had similar labeling intensity in control and treated samples.
    Figure Legend Snippet: Association of leureptin with hemocyte membranes Hemocytes collected 24 h after injection of saline or M. luteus were fixed on glass slides. Anti-leureptin IgG and FITC-labeled goat-anti-rabbit antibody were used to detect leureptin as described in materials and methods. The upper panels show hemocytes viewed by phase contrast, and the lower panels show hemocytes viewed by fluorescence microscopy. Both plasmatocytes (indicated by arrows ) and granulocytes stained more intensely in bacteria-challenged insects. Oenocytoids had similar labeling intensity in control and treated samples.

    Techniques Used: Injection, Labeling, Fluorescence, Microscopy, Staining

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    Blocking Assay:

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    Article Snippet: .. Membranes were incubated overnight in blocking buffer at 4°C with one of the following antibodies: guinea pig-anti GLT1 antibody (1:5000; Millipore), rabbit anti-GLAST (dilution: 1:5000), rabbit anti-phospho-Akt (1:5000, Cell Signaling Technology), mouse anti-Akt (1:5000, Cell Signaling Technology), mouse anti β-tubulin antibody (1:5000; Covance), or mouse anti-GAPDH antibody (1:5000; Millipore). .. Membranes were then washed and incubated with horseradish peroxidase (HRP) donkey-anti-Guinea pig IgG (H + L) secondary antibody (1:5000), anti-mouse IgG, HRP-linked secondary antibody (1:5000), or anti-rabbit IgG, HRP-linked secondary antibody (1:5000).

    Article Title: Identification of a Highly Conserved Epitope on Avian Influenza Virus Non-Structural Protein 1 Using a Peptide Microarray
    Article Snippet: .. After blocking with 5% nonfat milk in PBS overnight at 4°C, the membrane was incubated with MAb D7 (diluted 1:2,000 in PBS) at 37°C for 1 h, washed three times with PBS containing 0.05% (w/v) Tween 20 (PBST, pH 7.4), and probed with a 1:5,000 dilution of HRP-conjugated goat anti-mouse IgG (Sigma, St. Louis, MO, USA) at 37°C for 1 h. Reactivity was visualized with the substrate 3, 3'-diaminobenzidine (DAB, Sigma). .. Indirect immunofluorescence assay The NS1 gene was amplified using primer pairs NS1-pU (5′- ACACGAGCTCATGGATTCCAACACTGTG-3′) and NS1-pL (5′- CCGCTCGAGTCAAACTTCTGACTCAATTG-′3) from the pET-30a-NS1 and cloned into vector pCAGGS with chicken β-actin/rabbit β-globin hybrid promoter (AG) and the human CMV-IE enhancer in various mammalian cells.

    Purification:

    Article Title: Kir4.1-Dependent Astrocyte-Fast Motor Neuron Interactions Are Required for Peak Strength
    Article Snippet: .. Primary antibodies used included: goat ChAT (AB144P, Millipore, 1:200), rabbit DsRed (632496, Clonetech, 1:500), rat GFAP (13-0300, Invitrogen, 1:1000), chicken GFP (GFP-1020, Aves, 1:500), rabbit Kir4.1 (APC035, Alomone, 1:2000), rabbit laminin (L9393, Sigma, 1:1000), goat MMP-9 (M9570, Sigma, 1:500), mouse Myosin type 1 (M8421, Sigma, 1:4000), mouse Myosin type 2 (M4276, Sigma, 1:400), mouse NeuN (MAB377, Millipore, 1:1000), Purified anti-Neurofilament H (NF-H), Nonphosphorylated Antibody (SMI32, 801701, Biolegend, 1:10 000), guinea pig VGLUT1 (AB5905, Millipore, 1:5000), guinea pig VGLUT2 (AB2251, Millipore, 1:5000). .. Images were acquired on a Leica TCS SPE laser confocal microscope with either 20x or 40x objectives; all pictures are z stack confocal images, unless stated otherwise.

    Produced:

    Article Title: R9AP Stabilizes RGS11-G?5 and Accelerates the Early Light Response of ON-Bipolar Cells
    Article Snippet: .. The following antibodies (and dilutions) were used in these studies: a rabbit polyclonal antibody (R4612) raised against full-length bovine RGS7 (1:1000) and a goat polyclonal antibody against a Gβ5 peptide (MATDGLHENETLASLKC; 1:1000) both produced by Bethyl Laboratories (Montgomery, TX; ( )); a rabbit polyclonal antibody raised against residues 248–471 of mouse RGS11 (1:1000–1:5000) ( ); a goat polyclonal antiserum raised against R9AP (1:1000) ( ); an affinity purified sheep polyclonal antibody against mGluR6 (1:100; ); and a mouse monoclonal antibody (clone MC5) against PKCα (1:5000; Sigma-Aldrich, St. Louis, MO). .. HEK293 cells were grown, transfected as previously described ( ).

    Incubation:

    Article Title: Effects of MS-153 on chronic ethanol consumption and GLT1 modulation of glutamate levels in male alcohol-preferring rats
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    Article Title: The amyloid fold of Gad m 1 epitopes governs IgE binding
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    Staining:

    Article Title: Identification of Cilia Genes That Affect Cell-Cycle Progression Using Whole-Genome Transcriptome Analysis in Chlamydomonas reinhardtti
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    Affinity Purification:

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  • 97
    Millipore duolink in situ pla probe anti rabbit plus
    TrkA and APP interaction in septal primary neurons measured by proximity ligation assay. (A) Confocal microscopy analysis of double-staining of APP (rabbit APP-CT A8717, red) and Trk (mouse Trk B3, green) in primary septal neurons showing co-localization of APP and TrkA. (B) The TrkA/APP complex was visualized by <t>PLA,</t> which generates red dots when the two proteins are in close proximity. Mouse and rabbit anti TrkA-CT (mouse Trk B3 and rabbit TrkA ab7261) and anti APP-CT (rabbit APP-CT A8717 and mouse APP clone C1-6.1) were used as primary antibodies and anti-mouse MINUS and anti-rabbit <t>PLUS</t> were used as secondary antibodies. Red fluorescent dot represents single interaction between TrkA and APP. (C) In addition to PLA (red dots), rat primary septal neurons were immunostained with goat anti ChAt (green) and with DAPI for nuclei (blue). (D) PLA assay using mouse anti APP (C1-6.1) and rabbit anti TrkB (sc-119) or TrkC (sc-117).
    Duolink In Situ Pla Probe Anti Rabbit Plus, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 33 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/duolink in situ pla probe anti rabbit plus/product/Millipore
    Average 97 stars, based on 33 article reviews
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    88
    Millipore goat anti rabbit igg fitc conjugated
    Alcohol Induces HDAC2 Protein and this Effect is Inhibited by TSA After reaching confluency, SK-N-MC were pre-incubated with TSA for 2 hours, then treated with EtOH (0.1%) for 48 hours. In figure 3a, 10 µg of protein were analyzed using western blot with primary anti-HDAC2 and secondary <t>anti-IgG-HRP</t> antibodies. GAPDH was used as a loading control. Data presented show a representative blot indicating modulation of HDAC2 protein expression and a bar graph representing the mean ± SE of % densitometry values of HDAC2 protein levels (% control) of three independent experiments. # represents significance compared to control. * represents significance compared to EtOH treatment. For the flow cytometry experiments, 1 × 10 6 cells were fixed and permeabilized prior to intracellular staining with primary anti-HDAC2 and secondary <t>anti-IgG-FITC</t> antibody. Data presented in figure 3b show a representative histogram overlay of the gated cells. The bar graph represents the mean ± SE of % of gated cells expressing HDAC2. 10000 events were analyzed per sample. The gray and black histograms represent the unlabeled and secondary antibody controls respectively; the green histogram is the untreated control (~52%), blue represents EtOH (~69 %), purple represents TSA (~45%), and orange represents TSA + EtOH (~49%) treated cells. Data are representative of three independent experiments.
    Goat Anti Rabbit Igg Fitc Conjugated, supplied by Millipore, used in various techniques. Bioz Stars score: 88/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/goat anti rabbit igg fitc conjugated/product/Millipore
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    96
    Millipore anti bdnf
    Effects of the ethanol withdrawal procedure on the hyperpolarization-activated cyclic nucleotide-gated cation channel <t>(HCN1)</t> and brain-derived neurotrophic factor <t>(BDNF)</t> protein or gene level changes in the nucleus accumbens (NAc). (A) The expression of BDNF BDNF mRNA in the NAc. (B) The expression of BDNF-positive cells in the NAc. (C) Expression of BDNF positive cells in the NAc. (D) The number of BDNF-positive cells in the Hip. (E) The expression of HCN1 mRNA in the NAc. (F) The expression of HCN1-positive cells in the NAc. (G) Expression of HCN1 positive cells in the NAc. (H) The number of HCN1-positive cells in the NAc. The BDNF- and HCN1-positive cells in the NAc are represented by photomicrographs (400×). Data are mean ± standard error. * P
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    TrkA and APP interaction in septal primary neurons measured by proximity ligation assay. (A) Confocal microscopy analysis of double-staining of APP (rabbit APP-CT A8717, red) and Trk (mouse Trk B3, green) in primary septal neurons showing co-localization of APP and TrkA. (B) The TrkA/APP complex was visualized by PLA, which generates red dots when the two proteins are in close proximity. Mouse and rabbit anti TrkA-CT (mouse Trk B3 and rabbit TrkA ab7261) and anti APP-CT (rabbit APP-CT A8717 and mouse APP clone C1-6.1) were used as primary antibodies and anti-mouse MINUS and anti-rabbit PLUS were used as secondary antibodies. Red fluorescent dot represents single interaction between TrkA and APP. (C) In addition to PLA (red dots), rat primary septal neurons were immunostained with goat anti ChAt (green) and with DAPI for nuclei (blue). (D) PLA assay using mouse anti APP (C1-6.1) and rabbit anti TrkB (sc-119) or TrkC (sc-117).

    Journal: Frontiers in Molecular Neuroscience

    Article Title: Association of TrkA and APP Is Promoted by NGF and Reduced by Cell Death-Promoting Agents

    doi: 10.3389/fnmol.2017.00015

    Figure Lengend Snippet: TrkA and APP interaction in septal primary neurons measured by proximity ligation assay. (A) Confocal microscopy analysis of double-staining of APP (rabbit APP-CT A8717, red) and Trk (mouse Trk B3, green) in primary septal neurons showing co-localization of APP and TrkA. (B) The TrkA/APP complex was visualized by PLA, which generates red dots when the two proteins are in close proximity. Mouse and rabbit anti TrkA-CT (mouse Trk B3 and rabbit TrkA ab7261) and anti APP-CT (rabbit APP-CT A8717 and mouse APP clone C1-6.1) were used as primary antibodies and anti-mouse MINUS and anti-rabbit PLUS were used as secondary antibodies. Red fluorescent dot represents single interaction between TrkA and APP. (C) In addition to PLA (red dots), rat primary septal neurons were immunostained with goat anti ChAt (green) and with DAPI for nuclei (blue). (D) PLA assay using mouse anti APP (C1-6.1) and rabbit anti TrkB (sc-119) or TrkC (sc-117).

    Article Snippet: Coverslips were washed three times for 5 min PBS 1X and then incubated with PLA Probe Anti-mouse MINUS (DUO92004) and Anti-rabbit PLUS (DUO92002) for 1 h at 37°C.

    Techniques: Proximity Ligation Assay, Confocal Microscopy, Double Staining

    Alcohol Induces HDAC2 Protein and this Effect is Inhibited by TSA After reaching confluency, SK-N-MC were pre-incubated with TSA for 2 hours, then treated with EtOH (0.1%) for 48 hours. In figure 3a, 10 µg of protein were analyzed using western blot with primary anti-HDAC2 and secondary anti-IgG-HRP antibodies. GAPDH was used as a loading control. Data presented show a representative blot indicating modulation of HDAC2 protein expression and a bar graph representing the mean ± SE of % densitometry values of HDAC2 protein levels (% control) of three independent experiments. # represents significance compared to control. * represents significance compared to EtOH treatment. For the flow cytometry experiments, 1 × 10 6 cells were fixed and permeabilized prior to intracellular staining with primary anti-HDAC2 and secondary anti-IgG-FITC antibody. Data presented in figure 3b show a representative histogram overlay of the gated cells. The bar graph represents the mean ± SE of % of gated cells expressing HDAC2. 10000 events were analyzed per sample. The gray and black histograms represent the unlabeled and secondary antibody controls respectively; the green histogram is the untreated control (~52%), blue represents EtOH (~69 %), purple represents TSA (~45%), and orange represents TSA + EtOH (~49%) treated cells. Data are representative of three independent experiments.

    Journal: Alcoholism, clinical and experimental research

    Article Title: Effects of Alcohol on Histone Deacetylase 2 (HDAC2) and the Neuroprotective Role of Trichostatin A (TSA)

    doi: 10.1111/j.1530-0277.2011.01492.x

    Figure Lengend Snippet: Alcohol Induces HDAC2 Protein and this Effect is Inhibited by TSA After reaching confluency, SK-N-MC were pre-incubated with TSA for 2 hours, then treated with EtOH (0.1%) for 48 hours. In figure 3a, 10 µg of protein were analyzed using western blot with primary anti-HDAC2 and secondary anti-IgG-HRP antibodies. GAPDH was used as a loading control. Data presented show a representative blot indicating modulation of HDAC2 protein expression and a bar graph representing the mean ± SE of % densitometry values of HDAC2 protein levels (% control) of three independent experiments. # represents significance compared to control. * represents significance compared to EtOH treatment. For the flow cytometry experiments, 1 × 10 6 cells were fixed and permeabilized prior to intracellular staining with primary anti-HDAC2 and secondary anti-IgG-FITC antibody. Data presented in figure 3b show a representative histogram overlay of the gated cells. The bar graph represents the mean ± SE of % of gated cells expressing HDAC2. 10000 events were analyzed per sample. The gray and black histograms represent the unlabeled and secondary antibody controls respectively; the green histogram is the untreated control (~52%), blue represents EtOH (~69 %), purple represents TSA (~45%), and orange represents TSA + EtOH (~49%) treated cells. Data are representative of three independent experiments.

    Article Snippet: The HDAC2 protein was detected with the primary monoclonal antibody, rabbit anti-histone deacetylase 2 (Millipore) and secondary antibody, goat anti-rabbit IgG FITC-conjugated (Millipore).

    Techniques: Incubation, Western Blot, Expressing, Flow Cytometry, Cytometry, Staining

    Effects of the ethanol withdrawal procedure on the hyperpolarization-activated cyclic nucleotide-gated cation channel (HCN1) and brain-derived neurotrophic factor (BDNF) protein or gene level changes in the nucleus accumbens (NAc). (A) The expression of BDNF BDNF mRNA in the NAc. (B) The expression of BDNF-positive cells in the NAc. (C) Expression of BDNF positive cells in the NAc. (D) The number of BDNF-positive cells in the Hip. (E) The expression of HCN1 mRNA in the NAc. (F) The expression of HCN1-positive cells in the NAc. (G) Expression of HCN1 positive cells in the NAc. (H) The number of HCN1-positive cells in the NAc. The BDNF- and HCN1-positive cells in the NAc are represented by photomicrographs (400×). Data are mean ± standard error. * P

    Journal: Frontiers in Psychiatry

    Article Title: Synaptic Ultrastructure Might Be Involved in HCN1-Related BDNF mRNA in Withdrawal-Anxiety After Ethanol Dependence

    doi: 10.3389/fpsyt.2018.00215

    Figure Lengend Snippet: Effects of the ethanol withdrawal procedure on the hyperpolarization-activated cyclic nucleotide-gated cation channel (HCN1) and brain-derived neurotrophic factor (BDNF) protein or gene level changes in the nucleus accumbens (NAc). (A) The expression of BDNF BDNF mRNA in the NAc. (B) The expression of BDNF-positive cells in the NAc. (C) Expression of BDNF positive cells in the NAc. (D) The number of BDNF-positive cells in the Hip. (E) The expression of HCN1 mRNA in the NAc. (F) The expression of HCN1-positive cells in the NAc. (G) Expression of HCN1 positive cells in the NAc. (H) The number of HCN1-positive cells in the NAc. The BDNF- and HCN1-positive cells in the NAc are represented by photomicrographs (400×). Data are mean ± standard error. * P

    Article Snippet: The next day, the membrane was washed three times, 10 min each time, with PBS-T and incubated at room temperature with secondary antibodies, including anti-HCN1 [Peroxidase-Conjugated Affinipure Goat Anti-mouse IgG (H + L), 1:200] and anti-BDNF [Peroxidase-Conjugated Affinipure Goat Anti-Rabbit IgG (H + L), 1:200], and reacted with the Immobilon western chemiluminescent HRP substrate (WBKLS0500; Millipore, Bedford, MA, USA) for the color reaction.

    Techniques: Derivative Assay, Expressing

    Effects of the ethanol withdrawal procedure on the hyperpolarization-activated cyclic nucleotide-gated cation channel (HCN1) and brain-derived neurotrophic factor (BDNF) protein or gene level changes in the hippocampus (Hip). (A) The expression of BDNF BDNF mRNA in the Hip. (B) The expression of BDNF-positive cells in the Hip. (C) Expression of BDNF positive cells in the Hip. (D) The number of BDNF-positive cells in the Hip. (E) The expression of HCN1 mRNA in the Hip. (F) The expression of HCN1-positive cells in the Hip. (G) Expression of HCN1 positive cells in Hip. (H) The number of HCN1-positive cells in the Hip. The BDNF- and HCN1-positive cells in the Hip are represented by photomicrographs (400×). Data are mean ± standard error. * P

    Journal: Frontiers in Psychiatry

    Article Title: Synaptic Ultrastructure Might Be Involved in HCN1-Related BDNF mRNA in Withdrawal-Anxiety After Ethanol Dependence

    doi: 10.3389/fpsyt.2018.00215

    Figure Lengend Snippet: Effects of the ethanol withdrawal procedure on the hyperpolarization-activated cyclic nucleotide-gated cation channel (HCN1) and brain-derived neurotrophic factor (BDNF) protein or gene level changes in the hippocampus (Hip). (A) The expression of BDNF BDNF mRNA in the Hip. (B) The expression of BDNF-positive cells in the Hip. (C) Expression of BDNF positive cells in the Hip. (D) The number of BDNF-positive cells in the Hip. (E) The expression of HCN1 mRNA in the Hip. (F) The expression of HCN1-positive cells in the Hip. (G) Expression of HCN1 positive cells in Hip. (H) The number of HCN1-positive cells in the Hip. The BDNF- and HCN1-positive cells in the Hip are represented by photomicrographs (400×). Data are mean ± standard error. * P

    Article Snippet: The next day, the membrane was washed three times, 10 min each time, with PBS-T and incubated at room temperature with secondary antibodies, including anti-HCN1 [Peroxidase-Conjugated Affinipure Goat Anti-mouse IgG (H + L), 1:200] and anti-BDNF [Peroxidase-Conjugated Affinipure Goat Anti-Rabbit IgG (H + L), 1:200], and reacted with the Immobilon western chemiluminescent HRP substrate (WBKLS0500; Millipore, Bedford, MA, USA) for the color reaction.

    Techniques: Derivative Assay, Expressing