human igg4 antibody Search Results


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Biosynth Carbosynth rabbit antiserum against human plap
FIG. 5. Association of HIV-1 Env proteins on immature HIV-1 cores inde- pendently of the presence of lipid rafts. Immature HIV-1 cores were isolated from a <t>PLAP-encoding</t> virus by incubation for 1 h in detergent at either 4 or 37°C, followed by sedimentation centrifugation. Fractions were examined for the presence of PLAP and HIV-1 Env proteins. (A and B) Levels of PLAP were determined by incubation <t>of</t> <t>gradient</t> fractions with an AP substrate and quan- titated on a luminometer as relative units (RU) of luminescence. A CA-specific ELISA was used to determine the amount of virus in each gradient fraction. (C) Immunoblot analysis of the peak Pr55Gag-containing gradient fractions from immature cores treated with detergent at either 4 or 37°C (lanes 1 and 4, respectively) was performed as described in the legend to Fig. 2. Threefold serial dilutions of the peak Pr55Gag-containing fractions were also analyzed (lanes 2 and 3 and lanes 5 and 6).
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FIG. 5. Association of HIV-1 Env proteins on immature HIV-1 cores inde- pendently of the presence of lipid rafts. Immature HIV-1 cores were isolated from a <t>PLAP-encoding</t> virus by incubation for 1 h in detergent at either 4 or 37°C, followed by sedimentation centrifugation. Fractions were examined for the presence of PLAP and HIV-1 Env proteins. (A and B) Levels of PLAP were determined by incubation <t>of</t> <t>gradient</t> fractions with an AP substrate and quan- titated on a luminometer as relative units (RU) of luminescence. A CA-specific ELISA was used to determine the amount of virus in each gradient fraction. (C) Immunoblot analysis of the peak Pr55Gag-containing gradient fractions from immature cores treated with detergent at either 4 or 37°C (lanes 1 and 4, respectively) was performed as described in the legend to Fig. 2. Threefold serial dilutions of the peak Pr55Gag-containing fractions were also analyzed (lanes 2 and 3 and lanes 5 and 6).
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FIG. 5. Association of HIV-1 Env proteins on immature HIV-1 cores inde- pendently of the presence of lipid rafts. Immature HIV-1 cores were isolated from a <t>PLAP-encoding</t> virus by incubation for 1 h in detergent at either 4 or 37°C, followed by sedimentation centrifugation. Fractions were examined for the presence of PLAP and HIV-1 Env proteins. (A and B) Levels of PLAP were determined by incubation <t>of</t> <t>gradient</t> fractions with an AP substrate and quan- titated on a luminometer as relative units (RU) of luminescence. A CA-specific ELISA was used to determine the amount of virus in each gradient fraction. (C) Immunoblot analysis of the peak Pr55Gag-containing gradient fractions from immature cores treated with detergent at either 4 or 37°C (lanes 1 and 4, respectively) was performed as described in the legend to Fig. 2. Threefold serial dilutions of the peak Pr55Gag-containing fractions were also analyzed (lanes 2 and 3 and lanes 5 and 6).
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FIG. 5. Association of HIV-1 Env proteins on immature HIV-1 cores inde- pendently of the presence of lipid rafts. Immature HIV-1 cores were isolated from a <t>PLAP-encoding</t> virus by incubation for 1 h in detergent at either 4 or 37°C, followed by sedimentation centrifugation. Fractions were examined for the presence of PLAP and HIV-1 Env proteins. (A and B) Levels of PLAP were determined by incubation <t>of</t> <t>gradient</t> fractions with an AP substrate and quan- titated on a luminometer as relative units (RU) of luminescence. A CA-specific ELISA was used to determine the amount of virus in each gradient fraction. (C) Immunoblot analysis of the peak Pr55Gag-containing gradient fractions from immature cores treated with detergent at either 4 or 37°C (lanes 1 and 4, respectively) was performed as described in the legend to Fig. 2. Threefold serial dilutions of the peak Pr55Gag-containing fractions were also analyzed (lanes 2 and 3 and lanes 5 and 6).
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FIG. 5. Association of HIV-1 Env proteins on immature HIV-1 cores inde- pendently of the presence of lipid rafts. Immature HIV-1 cores were isolated from a <t>PLAP-encoding</t> virus by incubation for 1 h in detergent at either 4 or 37°C, followed by sedimentation centrifugation. Fractions were examined for the presence of PLAP and HIV-1 Env proteins. (A and B) Levels of PLAP were determined by incubation <t>of</t> <t>gradient</t> fractions with an AP substrate and quan- titated on a luminometer as relative units (RU) of luminescence. A CA-specific ELISA was used to determine the amount of virus in each gradient fraction. (C) Immunoblot analysis of the peak Pr55Gag-containing gradient fractions from immature cores treated with detergent at either 4 or 37°C (lanes 1 and 4, respectively) was performed as described in the legend to Fig. 2. Threefold serial dilutions of the peak Pr55Gag-containing fractions were also analyzed (lanes 2 and 3 and lanes 5 and 6).
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FIG. 5. Association of HIV-1 Env proteins on immature HIV-1 cores inde- pendently of the presence of lipid rafts. Immature HIV-1 cores were isolated from a <t>PLAP-encoding</t> virus by incubation for 1 h in detergent at either 4 or 37°C, followed by sedimentation centrifugation. Fractions were examined for the presence of PLAP and HIV-1 Env proteins. (A and B) Levels of PLAP were determined by incubation <t>of</t> <t>gradient</t> fractions with an AP substrate and quan- titated on a luminometer as relative units (RU) of luminescence. A CA-specific ELISA was used to determine the amount of virus in each gradient fraction. (C) Immunoblot analysis of the peak Pr55Gag-containing gradient fractions from immature cores treated with detergent at either 4 or 37°C (lanes 1 and 4, respectively) was performed as described in the legend to Fig. 2. Threefold serial dilutions of the peak Pr55Gag-containing fractions were also analyzed (lanes 2 and 3 and lanes 5 and 6).
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FIG. 5. Association of HIV-1 Env proteins on immature HIV-1 cores inde- pendently of the presence of lipid rafts. Immature HIV-1 cores were isolated from a <t>PLAP-encoding</t> virus by incubation for 1 h in detergent at either 4 or 37°C, followed by sedimentation centrifugation. Fractions were examined for the presence of PLAP and HIV-1 Env proteins. (A and B) Levels of PLAP were determined by incubation <t>of</t> <t>gradient</t> fractions with an AP substrate and quan- titated on a luminometer as relative units (RU) of luminescence. A CA-specific ELISA was used to determine the amount of virus in each gradient fraction. (C) Immunoblot analysis of the peak Pr55Gag-containing gradient fractions from immature cores treated with detergent at either 4 or 37°C (lanes 1 and 4, respectively) was performed as described in the legend to Fig. 2. Threefold serial dilutions of the peak Pr55Gag-containing fractions were also analyzed (lanes 2 and 3 and lanes 5 and 6).
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Toripalimab enhances IFN-γ secretion in CD3/CD28-activated naïve human CD8 + T cells. Naïve CD8 + T cells from seven healthy donors were activated with human anti-CD3 (0.5 µg/mL) and human anti-CD28 (0.5 µg/mL) immobilized on the plate surface. 10 µg/mL of isotype <t>control</t> <t>Ab</t> (Ctrl), pembrolizumab (pembro) or toripalimab (tori) in duplicate wells. IFN-γ levels in cell culture supernatant was quantified on day 3 of activation using ELISA. A IFN-γ levels from seven donors. B Fold change in concentration of IFN-γ relative to the Ctrl. p values in A were calculated using one-way ANOVA followed by Tukey’s multiple comparison test and those in B were calculated via paired t test. P < 0.05 is considered significant
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Toripalimab enhances IFN-γ secretion in CD3/CD28-activated naïve human CD8 + T cells. Naïve CD8 + T cells from seven healthy donors were activated with human anti-CD3 (0.5 µg/mL) and human anti-CD28 (0.5 µg/mL) immobilized on the plate surface. 10 µg/mL of isotype <t>control</t> <t>Ab</t> (Ctrl), pembrolizumab (pembro) or toripalimab (tori) in duplicate wells. IFN-γ levels in cell culture supernatant was quantified on day 3 of activation using ELISA. A IFN-γ levels from seven donors. B Fold change in concentration of IFN-γ relative to the Ctrl. p values in A were calculated using one-way ANOVA followed by Tukey’s multiple comparison test and those in B were calculated via paired t test. P < 0.05 is considered significant
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OriGene immunoglobulin g1 mouse monoclonal anti human pten
Toripalimab enhances IFN-γ secretion in CD3/CD28-activated naïve human CD8 + T cells. Naïve CD8 + T cells from seven healthy donors were activated with human anti-CD3 (0.5 µg/mL) and human anti-CD28 (0.5 µg/mL) immobilized on the plate surface. 10 µg/mL of isotype <t>control</t> <t>Ab</t> (Ctrl), pembrolizumab (pembro) or toripalimab (tori) in duplicate wells. IFN-γ levels in cell culture supernatant was quantified on day 3 of activation using ELISA. A IFN-γ levels from seven donors. B Fold change in concentration of IFN-γ relative to the Ctrl. p values in A were calculated using one-way ANOVA followed by Tukey’s multiple comparison test and those in B were calculated via paired t test. P < 0.05 is considered significant
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Image Search Results


FIG. 5. Association of HIV-1 Env proteins on immature HIV-1 cores inde- pendently of the presence of lipid rafts. Immature HIV-1 cores were isolated from a PLAP-encoding virus by incubation for 1 h in detergent at either 4 or 37°C, followed by sedimentation centrifugation. Fractions were examined for the presence of PLAP and HIV-1 Env proteins. (A and B) Levels of PLAP were determined by incubation of gradient fractions with an AP substrate and quan- titated on a luminometer as relative units (RU) of luminescence. A CA-specific ELISA was used to determine the amount of virus in each gradient fraction. (C) Immunoblot analysis of the peak Pr55Gag-containing gradient fractions from immature cores treated with detergent at either 4 or 37°C (lanes 1 and 4, respectively) was performed as described in the legend to Fig. 2. Threefold serial dilutions of the peak Pr55Gag-containing fractions were also analyzed (lanes 2 and 3 and lanes 5 and 6).

Journal: Journal of virology

Article Title: Evidence for a stable interaction of gp41 with Pr55(Gag) in immature human immunodeficiency virus type 1 particles.

doi: 10.1128/jvi.74.20.9381-9387.2000

Figure Lengend Snippet: FIG. 5. Association of HIV-1 Env proteins on immature HIV-1 cores inde- pendently of the presence of lipid rafts. Immature HIV-1 cores were isolated from a PLAP-encoding virus by incubation for 1 h in detergent at either 4 or 37°C, followed by sedimentation centrifugation. Fractions were examined for the presence of PLAP and HIV-1 Env proteins. (A and B) Levels of PLAP were determined by incubation of gradient fractions with an AP substrate and quan- titated on a luminometer as relative units (RU) of luminescence. A CA-specific ELISA was used to determine the amount of virus in each gradient fraction. (C) Immunoblot analysis of the peak Pr55Gag-containing gradient fractions from immature cores treated with detergent at either 4 or 37°C (lanes 1 and 4, respectively) was performed as described in the legend to Fig. 2. Threefold serial dilutions of the peak Pr55Gag-containing fractions were also analyzed (lanes 2 and 3 and lanes 5 and 6).

Article Snippet: Immunoblot analysis was performed on the pelleted gradient fractions as mentioned above using rabbit antiserum against human PLAP (obtained from Fitzgerald International Industries, Inc.).

Techniques: Isolation, Virus, Incubation, Sedimentation, Centrifugation, Enzyme-linked Immunosorbent Assay, Western Blot

Toripalimab enhances IFN-γ secretion in CD3/CD28-activated naïve human CD8 + T cells. Naïve CD8 + T cells from seven healthy donors were activated with human anti-CD3 (0.5 µg/mL) and human anti-CD28 (0.5 µg/mL) immobilized on the plate surface. 10 µg/mL of isotype control Ab (Ctrl), pembrolizumab (pembro) or toripalimab (tori) in duplicate wells. IFN-γ levels in cell culture supernatant was quantified on day 3 of activation using ELISA. A IFN-γ levels from seven donors. B Fold change in concentration of IFN-γ relative to the Ctrl. p values in A were calculated using one-way ANOVA followed by Tukey’s multiple comparison test and those in B were calculated via paired t test. P < 0.05 is considered significant

Journal: Cancer Immunology, Immunotherapy

Article Title: Toripalimab, a therapeutic monoclonal anti-PD-1 antibody with high binding affinity to PD-1 and enhanced potency to activate human T cells

doi: 10.1007/s00262-024-03635-3

Figure Lengend Snippet: Toripalimab enhances IFN-γ secretion in CD3/CD28-activated naïve human CD8 + T cells. Naïve CD8 + T cells from seven healthy donors were activated with human anti-CD3 (0.5 µg/mL) and human anti-CD28 (0.5 µg/mL) immobilized on the plate surface. 10 µg/mL of isotype control Ab (Ctrl), pembrolizumab (pembro) or toripalimab (tori) in duplicate wells. IFN-γ levels in cell culture supernatant was quantified on day 3 of activation using ELISA. A IFN-γ levels from seven donors. B Fold change in concentration of IFN-γ relative to the Ctrl. p values in A were calculated using one-way ANOVA followed by Tukey’s multiple comparison test and those in B were calculated via paired t test. P < 0.05 is considered significant

Article Snippet: Pembrolizumab (Merck & Co., lot T034261), toripalimab (Junshi Biosciences, lot 202007024) and control antibody (Ab) human IgG4 (SinoBiological, Cat No. 13505-HNAH) were stored in − 80 °C in smaller aliquots to avoid repeated freeze thaw cycles.

Techniques: Cell Culture, Activation Assay, Enzyme-linked Immunosorbent Assay, Concentration Assay, Comparison