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Santa Cruz Biotechnology peroxidase conjugated secondary antibody
Agonist-induced DOP receptor phosphorylation and internalization. ( A,B top) Stably HA-tagged hDOP receptor-expressing HEK293 cells were preincubated with anti-HA <t>antibody,</t> followed by stimulation with 10 µM DPDPE, DADLE, SNC80, ADL5859, AR-M1000390, deltorphin I, deltorphin II, [Met]-enkephalin, [Leu]-enkephalin, fentanyl, (−)-methadone, morphine, morphine-6-glucuronide (M6G), buprenorphine (BUP), norbuprenorphine (norBUP) or vehicle for 30 min at 37 °C. Cells were fixed, permeabilized, immunofluorescently stained, and subsequently examined using confocal microscopy. Images are representative, n = 3. Scale bar, 20 µm. (A,B bottom) HEK293 cells stably expressing HA-hDOP receptor were stimulated with the compounds listed in (A) or vehicle at concentrations ranging from 10 -9 to 10 -5 M for 10 min at 37 °C. Lysates were immunoblotted with antibodies to pT361 or pS363. Blots were stripped and reprobed with the anti-HA antibody. Blots are representative, n = 3-5. (C) Cells described in ( A ) were preincubated with anti-HA antibody and stimulated with vehicle or 10 µM of compounds listed in ( A ) for 30 min at 37 °C. Cells were fixed and labeled with a <t>peroxidase-conjugated</t> <t>secondary</t> antibody. Receptor internalization was measured by ELISA and quantified as the percentage of internalized receptors in agonist-treated cells compared to untreated cells. Data are means ± SEM of five independent experiments performed in quadruplicate. Results were analyzed by one-way ANOVA followed by Bonferroni’s post-hoc test (*p
Peroxidase Conjugated Secondary Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 837 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "Agonist-induced phosphorylation bar code and differential post-activation signaling of the delta opioid receptor revealed by phosphosite-specific antibodies"

Article Title: Agonist-induced phosphorylation bar code and differential post-activation signaling of the delta opioid receptor revealed by phosphosite-specific antibodies

Journal: Scientific Reports

doi: 10.1038/s41598-020-65589-7

Agonist-induced DOP receptor phosphorylation and internalization. ( A,B top) Stably HA-tagged hDOP receptor-expressing HEK293 cells were preincubated with anti-HA antibody, followed by stimulation with 10 µM DPDPE, DADLE, SNC80, ADL5859, AR-M1000390, deltorphin I, deltorphin II, [Met]-enkephalin, [Leu]-enkephalin, fentanyl, (−)-methadone, morphine, morphine-6-glucuronide (M6G), buprenorphine (BUP), norbuprenorphine (norBUP) or vehicle for 30 min at 37 °C. Cells were fixed, permeabilized, immunofluorescently stained, and subsequently examined using confocal microscopy. Images are representative, n = 3. Scale bar, 20 µm. (A,B bottom) HEK293 cells stably expressing HA-hDOP receptor were stimulated with the compounds listed in (A) or vehicle at concentrations ranging from 10 -9 to 10 -5 M for 10 min at 37 °C. Lysates were immunoblotted with antibodies to pT361 or pS363. Blots were stripped and reprobed with the anti-HA antibody. Blots are representative, n = 3-5. (C) Cells described in ( A ) were preincubated with anti-HA antibody and stimulated with vehicle or 10 µM of compounds listed in ( A ) for 30 min at 37 °C. Cells were fixed and labeled with a peroxidase-conjugated secondary antibody. Receptor internalization was measured by ELISA and quantified as the percentage of internalized receptors in agonist-treated cells compared to untreated cells. Data are means ± SEM of five independent experiments performed in quadruplicate. Results were analyzed by one-way ANOVA followed by Bonferroni’s post-hoc test (*p
Figure Legend Snippet: Agonist-induced DOP receptor phosphorylation and internalization. ( A,B top) Stably HA-tagged hDOP receptor-expressing HEK293 cells were preincubated with anti-HA antibody, followed by stimulation with 10 µM DPDPE, DADLE, SNC80, ADL5859, AR-M1000390, deltorphin I, deltorphin II, [Met]-enkephalin, [Leu]-enkephalin, fentanyl, (−)-methadone, morphine, morphine-6-glucuronide (M6G), buprenorphine (BUP), norbuprenorphine (norBUP) or vehicle for 30 min at 37 °C. Cells were fixed, permeabilized, immunofluorescently stained, and subsequently examined using confocal microscopy. Images are representative, n = 3. Scale bar, 20 µm. (A,B bottom) HEK293 cells stably expressing HA-hDOP receptor were stimulated with the compounds listed in (A) or vehicle at concentrations ranging from 10 -9 to 10 -5 M for 10 min at 37 °C. Lysates were immunoblotted with antibodies to pT361 or pS363. Blots were stripped and reprobed with the anti-HA antibody. Blots are representative, n = 3-5. (C) Cells described in ( A ) were preincubated with anti-HA antibody and stimulated with vehicle or 10 µM of compounds listed in ( A ) for 30 min at 37 °C. Cells were fixed and labeled with a peroxidase-conjugated secondary antibody. Receptor internalization was measured by ELISA and quantified as the percentage of internalized receptors in agonist-treated cells compared to untreated cells. Data are means ± SEM of five independent experiments performed in quadruplicate. Results were analyzed by one-way ANOVA followed by Bonferroni’s post-hoc test (*p

Techniques Used: Stable Transfection, Expressing, Staining, Confocal Microscopy, Labeling, Enzyme-linked Immunosorbent Assay

Time course of DPDPE-induced DOP receptor phosphorylation, concentration-dependent DOP receptor phosphorylation and internalization. ( A ) HEK293 cells stably expressing HA-tagged hDOP receptor were preincubated with anti-HA antibody and stimulated with the indicated DPDPE concentrations for 30 min at 37 °C. After stimulation, cells were fixed, permeabilized, immunofluorescently stained and examined using confocal microscopy. Images are representative from one of three independent experiments. Scale bar, 20 µm. (B) Cells described in (A) were preincubated with anti-HA antibody and stimulated with the indicated DPDPE concentrations for 30 min at 37 °C. After fixation, cells were labeled with a peroxidase-conjugated secondary antibody and receptor internalization was measured by enzyme-linked immunosorbent assay. Receptor internalization was measured by ELISA and quantified as the percentage of internalized receptors compared to untreated cells. Data are means ± SEM of four independent experiments performed in quadruplicate. (C,D) Cells described in ( A ) were exposed to 1 µM DPDPE for the indicated times and temperatures ( C ) at 37 °C, ( D ) at 22 °C (room temperature, RT) and lysates were immunoblotted with anti-pT361 or anti-pS363 antibodies. Blots are representative of n = 4 ( C ) or n = 5 ( D ) independent experiments. (E) Cells described in (A) were preincubated with anti-HA antibody and thereafter stimulated with 1 µM DPDPE for the indicated durations at 37 °C. Cells were fixed, permeabilized, immunofluorescently stained and examined using confocal microscopy. Images are representative from one of three independent experiments. Scale bar, 20 µm. (F) Cells described in ( A ) were preincubated with anti-HA antibody and stimulated with 10 µM DPDPE for the indicated durations at 37 °C. Cells were fixed and labeled with peroxidase-conjugated secondary antibody. Receptor internalization was measured by ELISA and quantified as the percentage of internalized receptors in agonist-treated cells compared to untreated cells. Data are mean ± SEM of five independent experiments performed in quadruplicate.
Figure Legend Snippet: Time course of DPDPE-induced DOP receptor phosphorylation, concentration-dependent DOP receptor phosphorylation and internalization. ( A ) HEK293 cells stably expressing HA-tagged hDOP receptor were preincubated with anti-HA antibody and stimulated with the indicated DPDPE concentrations for 30 min at 37 °C. After stimulation, cells were fixed, permeabilized, immunofluorescently stained and examined using confocal microscopy. Images are representative from one of three independent experiments. Scale bar, 20 µm. (B) Cells described in (A) were preincubated with anti-HA antibody and stimulated with the indicated DPDPE concentrations for 30 min at 37 °C. After fixation, cells were labeled with a peroxidase-conjugated secondary antibody and receptor internalization was measured by enzyme-linked immunosorbent assay. Receptor internalization was measured by ELISA and quantified as the percentage of internalized receptors compared to untreated cells. Data are means ± SEM of four independent experiments performed in quadruplicate. (C,D) Cells described in ( A ) were exposed to 1 µM DPDPE for the indicated times and temperatures ( C ) at 37 °C, ( D ) at 22 °C (room temperature, RT) and lysates were immunoblotted with anti-pT361 or anti-pS363 antibodies. Blots are representative of n = 4 ( C ) or n = 5 ( D ) independent experiments. (E) Cells described in (A) were preincubated with anti-HA antibody and thereafter stimulated with 1 µM DPDPE for the indicated durations at 37 °C. Cells were fixed, permeabilized, immunofluorescently stained and examined using confocal microscopy. Images are representative from one of three independent experiments. Scale bar, 20 µm. (F) Cells described in ( A ) were preincubated with anti-HA antibody and stimulated with 10 µM DPDPE for the indicated durations at 37 °C. Cells were fixed and labeled with peroxidase-conjugated secondary antibody. Receptor internalization was measured by ELISA and quantified as the percentage of internalized receptors in agonist-treated cells compared to untreated cells. Data are mean ± SEM of five independent experiments performed in quadruplicate.

Techniques Used: Concentration Assay, Stable Transfection, Expressing, Staining, Confocal Microscopy, Labeling, Enzyme-linked Immunosorbent Assay

Characterization of phosphosite-specific DOP receptor antibodies using λ-phosphatase and receptor mutants. ( A ) Schematic representation of the human DOP receptor (hDOP). Potential intracellular phosphorylation sites are depicted in gray. T361 was targeted for the generation of the phosphosite-specific anti-pT361 antibody and anti-pS363 antibody was acquired commercially. (B) Characterization of phosphosite-specific antibodies directed against T361 and S363 using λ-phosphatase. Stably HA-tagged hDOP-receptor expressing HEK293 cells were either not treated (−) or treated (+) with 10 µM DADLE for 10 min. Lysates were then either not incubated (−) or incubated (+) with λ-phosphatase and immunoblotted with the phosphosite-specific antibodies anti-pT361 {5038} or anti-pS363. Blots were stripped and reprobed with the anti-HA antibody {2238} as a loading control. Blots are representative, n = 3. Molecular mass markers (kDA) are indicated, left. (C) Sequence of the carboxyl-terminal tail of hDOP receptor showing all potential phosphorylation sites. Serine (S) and threonine (T) residues indicated were exchanged to alanine. (D) HEK293 cells stably expressing HA-hDOP receptor, T361A/S363A or 7 S/TA were not treated (−) or treated (+) with 1 µM DPDPE for 10 min and lysates were immunoblotted with the antibodies to pT361 or pS363. Blots were stripped and reprobed with the anti-HA antibody. Blots are representative, n = 5. (E) Cells described in (D) were preincubated with antibody to HA-tag and subsequently exposed to 10 µM DPDPE or vehicle for 30 min at 37 °C. Cells were fixed, permeabilized, immunofluorescently stained and examined using confocal microscopy. Images are representative from one of three independent experiments. Scale bar, 20 µm. (F) Receptor internalization was quantified by ELISA. Cells described in (D) were preincubated with antibody to HA-tag and stimulated with 10 µM DPDPE or vehicle at 37 °C for 30 min. Cells were fixed and labeled with a peroxidase-conjugated secondary antibody. Receptor internalization was measured by enzyme-linked immunosorbent assay and quantified as the percentage of internalized receptors in DPDPE-treated cells. Data are mean ± SEM of five independent experiments performed in quadruplicate. Results were analyzed by one-way ANOVA followed by Bonferroni’s post-hoc test (*p
Figure Legend Snippet: Characterization of phosphosite-specific DOP receptor antibodies using λ-phosphatase and receptor mutants. ( A ) Schematic representation of the human DOP receptor (hDOP). Potential intracellular phosphorylation sites are depicted in gray. T361 was targeted for the generation of the phosphosite-specific anti-pT361 antibody and anti-pS363 antibody was acquired commercially. (B) Characterization of phosphosite-specific antibodies directed against T361 and S363 using λ-phosphatase. Stably HA-tagged hDOP-receptor expressing HEK293 cells were either not treated (−) or treated (+) with 10 µM DADLE for 10 min. Lysates were then either not incubated (−) or incubated (+) with λ-phosphatase and immunoblotted with the phosphosite-specific antibodies anti-pT361 {5038} or anti-pS363. Blots were stripped and reprobed with the anti-HA antibody {2238} as a loading control. Blots are representative, n = 3. Molecular mass markers (kDA) are indicated, left. (C) Sequence of the carboxyl-terminal tail of hDOP receptor showing all potential phosphorylation sites. Serine (S) and threonine (T) residues indicated were exchanged to alanine. (D) HEK293 cells stably expressing HA-hDOP receptor, T361A/S363A or 7 S/TA were not treated (−) or treated (+) with 1 µM DPDPE for 10 min and lysates were immunoblotted with the antibodies to pT361 or pS363. Blots were stripped and reprobed with the anti-HA antibody. Blots are representative, n = 5. (E) Cells described in (D) were preincubated with antibody to HA-tag and subsequently exposed to 10 µM DPDPE or vehicle for 30 min at 37 °C. Cells were fixed, permeabilized, immunofluorescently stained and examined using confocal microscopy. Images are representative from one of three independent experiments. Scale bar, 20 µm. (F) Receptor internalization was quantified by ELISA. Cells described in (D) were preincubated with antibody to HA-tag and stimulated with 10 µM DPDPE or vehicle at 37 °C for 30 min. Cells were fixed and labeled with a peroxidase-conjugated secondary antibody. Receptor internalization was measured by enzyme-linked immunosorbent assay and quantified as the percentage of internalized receptors in DPDPE-treated cells. Data are mean ± SEM of five independent experiments performed in quadruplicate. Results were analyzed by one-way ANOVA followed by Bonferroni’s post-hoc test (*p

Techniques Used: Stable Transfection, Expressing, Incubation, Sequencing, Staining, Confocal Microscopy, Enzyme-linked Immunosorbent Assay, Labeling

Antagonist-selective inhibition of DPDPE-induced DOP receptor phosphorylation, internalization and G protein signaling. ( A ) Stably HA-hDOP receptor-expressing HEK293 cells were either not preincubated (−) or preincubated (+) with 5 µM naloxone, naltrindole, naltriben or naltrexone for 30 min at 37 °C, then stimulated with vehicle (water, -) or with 1 µM DPDPE (+) for 10 min at 37 °C. Cell lysates were then immunoblotted with antibodies to pT361 or pS363. Blots were stripped and reprobed with the anti-HA antibody. Blots are representative, n = 4. (B) Cells described in ( A ) were preincubated with anti-HA antibody and then treated with vehicle (DMSO), 5 µM naloxone, naltrindole or naltriben and with or without 1 µM DPDPE for 10 min at 37 °C. After fixation, cells were permeabilized, immunofluorescently stained and examined using confocal microscopy. Images are representative, n = 3. Scale bar, 20 µm. (C) Cells described in ( A ) were preincubated with anti-HA antibody and stimulated with vehicle (DMSO), 5 µM naloxone, naltrindole or naltriben and with or without 1 µM DPDPE for 10 min at 37 °C. Cells were then fixed and labeled with a peroxidase-conjugated secondary antibody. Receptor internalization was measured by ELISA and quantified as percentage of internalized receptors in agonist-treated cells. Data are means ± SEM from five independent experiments performed in quadruplicate. *p
Figure Legend Snippet: Antagonist-selective inhibition of DPDPE-induced DOP receptor phosphorylation, internalization and G protein signaling. ( A ) Stably HA-hDOP receptor-expressing HEK293 cells were either not preincubated (−) or preincubated (+) with 5 µM naloxone, naltrindole, naltriben or naltrexone for 30 min at 37 °C, then stimulated with vehicle (water, -) or with 1 µM DPDPE (+) for 10 min at 37 °C. Cell lysates were then immunoblotted with antibodies to pT361 or pS363. Blots were stripped and reprobed with the anti-HA antibody. Blots are representative, n = 4. (B) Cells described in ( A ) were preincubated with anti-HA antibody and then treated with vehicle (DMSO), 5 µM naloxone, naltrindole or naltriben and with or without 1 µM DPDPE for 10 min at 37 °C. After fixation, cells were permeabilized, immunofluorescently stained and examined using confocal microscopy. Images are representative, n = 3. Scale bar, 20 µm. (C) Cells described in ( A ) were preincubated with anti-HA antibody and stimulated with vehicle (DMSO), 5 µM naloxone, naltrindole or naltriben and with or without 1 µM DPDPE for 10 min at 37 °C. Cells were then fixed and labeled with a peroxidase-conjugated secondary antibody. Receptor internalization was measured by ELISA and quantified as percentage of internalized receptors in agonist-treated cells. Data are means ± SEM from five independent experiments performed in quadruplicate. *p

Techniques Used: Inhibition, Stable Transfection, Expressing, Staining, Confocal Microscopy, Labeling, Enzyme-linked Immunosorbent Assay

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Article Snippet: .. Proteins were visualized with horseradish peroxidase-conjugated secondary antibodies (anti-mouse IgG and IgM; Santa Cruz Biotechnology) followed by incubation with Clarity™ Western ECL Blotting Substrate and chemiluminescent detection. .. Immunohistochemistry Eyecups were collected as previously described, with the lens and anterior chamber removed, fixed overnight with 4% paraformaldehyde (PFA), washed in PBS, embedded in Neg-50 cutting medium (Richard-Allen Scientific; Thermo Fisher Scientific) and sectioned using a cryostat (14-μm sections).

Incubation:

Article Title: Agonist-induced phosphorylation bar code and differential post-activation signaling of the delta opioid receptor revealed by phosphosite-specific antibodies
Article Snippet: .. Cells were washed several times with PBS and incubated with a peroxidase-conjugated secondary antibody (Santa Cruz; Heidelberg, Germany). .. After additional washing steps, the HRP-substrate ABTS was added and optical density was measured at 405 nm using an iMark™ Microplate Absorbance Reader (BioRad, Munich, Germany).

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    SOCS3 expression in peripheral blood eosinophils from Th2 patients analyzed by immunohistochemical, immunofluorescence, and Western blot techniques. Eosinophils from asthmatic and NAEB patients within healthy controls were adhered to slides and incubated with peroxidase-conjugated goat <t>antirabbit</t> <t>IgG</t> against SOCS3 antibody ((b), (c), and (d)) or rabbit IgG as a control (a), and Texas Red conjugated goat antirabbit IgG against SOCS3 antibody ((f), (g), and (h)) or rabbit IgG as a control (e). The slides were observed by optical ((a), (b), (c), (d)) or confocal ((e), (f), (g) and (h)) microscopy. Western blot analysis of the cytosolic extract of purified eosinophils was achieved using antibody against SOCS3 (i). Lane 1: recombinant SOCS3 was loaded as a positive control; lane 2: eosinophil lysate from NAEB patients; lane 3: eosinophil lysate from healthy control patients; lane 4: isotype negative control. The picture is a representative example of 5 individuals, all displaying similar results. (j): SOCS3 bands were quantified by densitometry and corrected by actin expression; data are expressed as the mean ± SD, n = 5, * P
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    Santa Cruz Biotechnology horseradish peroxidase conjugated secondary antibody
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    Santa Cruz Biotechnology hrp conjugated anti mouse igg antibody
    Expression of recombinant protein in ZYP-5052 medium. A) . Coomassie stained 12% SDS-PAGE of lysates shows proteins expressed in ZYP-5052 at 25°C at different incubation time. Equal culture densities (corresponding to 1 OD 600 cells) were analysed in each lane. Cells grown to saturation in PG, a non-inducing growth medium were loaded as control. Lane L: Protein marker; Lane C: Control; Lane 3 h-45 h: Induced samples at different incubation time, as indicated on top of each lane. B) . Western blot of expressed protein. Expressed protein was transferred to nitrocellulose membrane at 30 V overnight at 4°C. After blocking in 3% BSA, membrane was treated with mouse raised anti-His antibody (1 : 500) and <t>HRP-conjugated</t> anti-mouse <t>IgG</t> antibody and developed with DAB. Bold arrow denotes distinct band in induced sample corresponding to expressed protein of 25 kDa size. Control used is culture grown to saturation in PG medium. No expression is seen in control. Lane L: Protein marker; Lane C: Control; Lane 45 h: Sample processed 45 hr post incubation at 25°C.
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    Santa Cruz Biotechnology goat horseradish peroxidase hrp conjugated secondary anti mouse antibody
    <t>BtaE</t> localization. (A and C) Western blot analysis of whole-membrane fractions from B. suis (A) and E. coli pBBR btaE (C) was carried out. Membrane samples were submitted to a strong denaturing process. Samples were electrophoresed by SDS-PAGE and transferred to a PDVF membrane. Blots were incubated with anti-BtaE antisera and with anti-mouse <t>HRP-conjugated</t> secondary antibody and finally revealed using ECL Plus. On the right, a Coomassie blue pattern is shown as a loading control (ctrl). (B and D) Detection of BtaE (in red) on the B. suis surface (B) and on the E. coli pBBR btaE surface (D) by immunofluorescence of GFP-tagged bacteria. Cultures of GFP-labeled strains were fixed, incubated with anti-BtaE antibodies, and then probed with a CY3-conjugated donkey anti-mouse antibody preparation. Samples were observed with a Plan-Aprochromat 100×/1.4 oil DIC objective on a Zeiss LSM 5 Pascal confocal microscope.
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    SOCS3 expression in peripheral blood eosinophils from Th2 patients analyzed by immunohistochemical, immunofluorescence, and Western blot techniques. Eosinophils from asthmatic and NAEB patients within healthy controls were adhered to slides and incubated with peroxidase-conjugated goat antirabbit IgG against SOCS3 antibody ((b), (c), and (d)) or rabbit IgG as a control (a), and Texas Red conjugated goat antirabbit IgG against SOCS3 antibody ((f), (g), and (h)) or rabbit IgG as a control (e). The slides were observed by optical ((a), (b), (c), (d)) or confocal ((e), (f), (g) and (h)) microscopy. Western blot analysis of the cytosolic extract of purified eosinophils was achieved using antibody against SOCS3 (i). Lane 1: recombinant SOCS3 was loaded as a positive control; lane 2: eosinophil lysate from NAEB patients; lane 3: eosinophil lysate from healthy control patients; lane 4: isotype negative control. The picture is a representative example of 5 individuals, all displaying similar results. (j): SOCS3 bands were quantified by densitometry and corrected by actin expression; data are expressed as the mean ± SD, n = 5, * P

    Journal: Clinical and Developmental Immunology

    Article Title: Suppressors of Cytokine Signaling 3 Expression in Eosinophils: Regulation by PGE2 and Th2 Cytokines

    doi: 10.1155/2011/917015

    Figure Lengend Snippet: SOCS3 expression in peripheral blood eosinophils from Th2 patients analyzed by immunohistochemical, immunofluorescence, and Western blot techniques. Eosinophils from asthmatic and NAEB patients within healthy controls were adhered to slides and incubated with peroxidase-conjugated goat antirabbit IgG against SOCS3 antibody ((b), (c), and (d)) or rabbit IgG as a control (a), and Texas Red conjugated goat antirabbit IgG against SOCS3 antibody ((f), (g), and (h)) or rabbit IgG as a control (e). The slides were observed by optical ((a), (b), (c), (d)) or confocal ((e), (f), (g) and (h)) microscopy. Western blot analysis of the cytosolic extract of purified eosinophils was achieved using antibody against SOCS3 (i). Lane 1: recombinant SOCS3 was loaded as a positive control; lane 2: eosinophil lysate from NAEB patients; lane 3: eosinophil lysate from healthy control patients; lane 4: isotype negative control. The picture is a representative example of 5 individuals, all displaying similar results. (j): SOCS3 bands were quantified by densitometry and corrected by actin expression; data are expressed as the mean ± SD, n = 5, * P

    Article Snippet: The secondary antibody, HRP-conjugated goat antirabbit IgG (Santa Cruz Biotechnology, Inc.), was diluted 1 : 1000.

    Techniques: Expressing, Immunohistochemistry, Immunofluorescence, Western Blot, Incubation, Microscopy, Purification, Recombinant, Positive Control, Negative Control

    Confirmation of the differentially expressed proteins of annexin A2 and beta-actin by Western blot . The equal cell lysates of control and DHBV infected PDHs at 12, 24, 72 and 120 h post-infection were separated by SDS-PAGE, and detected by Western blotting with mouse anti-beta-actin and anti-duck annexin A2 as primary antibodies and then followed by horseradish peroxidase-conjugated goat anti-mouse IgG as secondary antibody (A). The same amount protein of each sample were applied to a parallel SDS-PAGE gel and stained with Coomassie brilliant blue (B).

    Journal: Proteome Science

    Article Title: Proteomic analysis of primary duck hepatocytes infected with duck hepatitis B virus

    doi: 10.1186/1477-5956-8-28

    Figure Lengend Snippet: Confirmation of the differentially expressed proteins of annexin A2 and beta-actin by Western blot . The equal cell lysates of control and DHBV infected PDHs at 12, 24, 72 and 120 h post-infection were separated by SDS-PAGE, and detected by Western blotting with mouse anti-beta-actin and anti-duck annexin A2 as primary antibodies and then followed by horseradish peroxidase-conjugated goat anti-mouse IgG as secondary antibody (A). The same amount protein of each sample were applied to a parallel SDS-PAGE gel and stained with Coomassie brilliant blue (B).

    Article Snippet: The blots were then washed four times with PBS containing 0.1% Tween-20, and incubated with the appropriate horseradish peroxidase-conjugated secondary antibody (Santa Cruz Biotechnology) 1 hour at room temperature.

    Techniques: Western Blot, Infection, SDS Page, Staining

    Expression of recombinant protein in ZYP-5052 medium. A) . Coomassie stained 12% SDS-PAGE of lysates shows proteins expressed in ZYP-5052 at 25°C at different incubation time. Equal culture densities (corresponding to 1 OD 600 cells) were analysed in each lane. Cells grown to saturation in PG, a non-inducing growth medium were loaded as control. Lane L: Protein marker; Lane C: Control; Lane 3 h-45 h: Induced samples at different incubation time, as indicated on top of each lane. B) . Western blot of expressed protein. Expressed protein was transferred to nitrocellulose membrane at 30 V overnight at 4°C. After blocking in 3% BSA, membrane was treated with mouse raised anti-His antibody (1 : 500) and HRP-conjugated anti-mouse IgG antibody and developed with DAB. Bold arrow denotes distinct band in induced sample corresponding to expressed protein of 25 kDa size. Control used is culture grown to saturation in PG medium. No expression is seen in control. Lane L: Protein marker; Lane C: Control; Lane 45 h: Sample processed 45 hr post incubation at 25°C.

    Journal: Virology Journal

    Article Title: Cloning and expression of N22 region of Torque Teno virus (TTV) genome and use of peptide in developing immunoassay for TTV antibodies

    doi: 10.1186/1743-422X-11-96

    Figure Lengend Snippet: Expression of recombinant protein in ZYP-5052 medium. A) . Coomassie stained 12% SDS-PAGE of lysates shows proteins expressed in ZYP-5052 at 25°C at different incubation time. Equal culture densities (corresponding to 1 OD 600 cells) were analysed in each lane. Cells grown to saturation in PG, a non-inducing growth medium were loaded as control. Lane L: Protein marker; Lane C: Control; Lane 3 h-45 h: Induced samples at different incubation time, as indicated on top of each lane. B) . Western blot of expressed protein. Expressed protein was transferred to nitrocellulose membrane at 30 V overnight at 4°C. After blocking in 3% BSA, membrane was treated with mouse raised anti-His antibody (1 : 500) and HRP-conjugated anti-mouse IgG antibody and developed with DAB. Bold arrow denotes distinct band in induced sample corresponding to expressed protein of 25 kDa size. Control used is culture grown to saturation in PG medium. No expression is seen in control. Lane L: Protein marker; Lane C: Control; Lane 45 h: Sample processed 45 hr post incubation at 25°C.

    Article Snippet: For immunodetection of the His fusion proteins, the primary antibody used was His probe (H-3) mouse monoclonal IgG (1 : 500; Santa Cruz Biotechnology, USA) and the secondary antibody was HRP-conjugated anti-mouse IgG antibody (1 : 2000; Santa Cruz Biotechnology, USA).

    Techniques: Expressing, Recombinant, Staining, SDS Page, Incubation, Marker, Western Blot, Blocking Assay

    BtaE localization. (A and C) Western blot analysis of whole-membrane fractions from B. suis (A) and E. coli pBBR btaE (C) was carried out. Membrane samples were submitted to a strong denaturing process. Samples were electrophoresed by SDS-PAGE and transferred to a PDVF membrane. Blots were incubated with anti-BtaE antisera and with anti-mouse HRP-conjugated secondary antibody and finally revealed using ECL Plus. On the right, a Coomassie blue pattern is shown as a loading control (ctrl). (B and D) Detection of BtaE (in red) on the B. suis surface (B) and on the E. coli pBBR btaE surface (D) by immunofluorescence of GFP-tagged bacteria. Cultures of GFP-labeled strains were fixed, incubated with anti-BtaE antibodies, and then probed with a CY3-conjugated donkey anti-mouse antibody preparation. Samples were observed with a Plan-Aprochromat 100×/1.4 oil DIC objective on a Zeiss LSM 5 Pascal confocal microscope.

    Journal: Infection and Immunity

    Article Title: BtaE, an Adhesin That Belongs to the Trimeric Autotransporter Family, Is Required for Full Virulence and Defines a Specific Adhesive Pole of Brucella suis

    doi: 10.1128/IAI.01241-12

    Figure Lengend Snippet: BtaE localization. (A and C) Western blot analysis of whole-membrane fractions from B. suis (A) and E. coli pBBR btaE (C) was carried out. Membrane samples were submitted to a strong denaturing process. Samples were electrophoresed by SDS-PAGE and transferred to a PDVF membrane. Blots were incubated with anti-BtaE antisera and with anti-mouse HRP-conjugated secondary antibody and finally revealed using ECL Plus. On the right, a Coomassie blue pattern is shown as a loading control (ctrl). (B and D) Detection of BtaE (in red) on the B. suis surface (B) and on the E. coli pBBR btaE surface (D) by immunofluorescence of GFP-tagged bacteria. Cultures of GFP-labeled strains were fixed, incubated with anti-BtaE antibodies, and then probed with a CY3-conjugated donkey anti-mouse antibody preparation. Samples were observed with a Plan-Aprochromat 100×/1.4 oil DIC objective on a Zeiss LSM 5 Pascal confocal microscope.

    Article Snippet: Blots were probed with polyclonal mouse anti-BtaE serum (1:8,000) and a goat horseradish peroxidase (HRP)-conjugated secondary anti-mouse antibody (1:30,000; Santa Cruz) and then revealed using ECL Plus (Amersham).

    Techniques: Western Blot, SDS Page, Incubation, Immunofluorescence, Labeling, Microscopy