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high binding microplates  (R&D Systems)


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    R&D Systems high binding microplates
    High Binding Microplates, supplied by R&D Systems, used in various techniques. Bioz Stars score: 95/100, based on 93 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/high+binding+microplate/Clear+Polystyrene+Microplates/pmc13058453-104-0-3
    Average 95 stars, based on 93 article reviews
    high binding microplates - by Bioz Stars, 2026-10
    95/100 stars

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    other:

    Article Title: Label-Free Single-Molecule Immunoassay.
    Article Snippet: Reagent diluent (catalog no. DY995), streptavidin conjugated horseradish peroxidase (streptavidin-HRP, catalog no. DY998), stop solution (catalog no. DY994) and high-binding microplate (catalog no. DY990) were purchased from R&D Systems.

    Article Title: Label‐Free Single‐Molecule Immunoassay
    Article Snippet: Reagent diluent (catalog no. DY995), streptavidin conjugated horseradish peroxidase (streptavidin‐HRP, catalog no. DY998), stop solution (catalog no. DY994) and high‐binding microplate (catalog no. DY990) were purchased from R&D Systems.

    Article Title: Microfluidic Digital Immunoassay for Point-of-Care Detection of NT-proBNP from Whole Blood.
    Article Snippet: The high prevalence and economic burden of heart failure remain a challenge to global health.. This lifelong disease leads to a buildup of permanent heart damage, making early detection and frequent monitoring crucial for effective treatment.. N-terminal proBNP (NT-proBNP) is an important biomarker for monitoring the disease state, but current commercial and research NT-proBNP assays require phlebotomy and bulky equipment or do not satisfy clinical requirements such as sensitivity and detection thresholds.



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    Greiner Bio high binding elisa plates
    (A) Sera from MRL lpr mice (n=12, bled weekly from 8 to 13 weeks of age) were analyzed by <t>ELISA</t> using synthetic 10×RG peptides: native sequence (GRGRGRGRGRGRGRGRGRGR) vs. SDMA-modified (lowercase ‘r’ denotes SDMA; GrGrGrGRGRGrGrGrGRGR). All 12 mice developed anti SDMA antibody titers above the corresponding native controls, and the majority (9/12) showed a gradual increase in anti-SDMA titers over time. (B) Immunoblotting of HEp-2 lysates revealed progressive changes in band patterns from 10 weeks onward. To identify SDMA specific reactive proteins, cells were pretreated with the methyltransferase inhibitor EPZ015666 (EPZ) before lysis. A prominent ∼15 kDa band (arrowhead) was markedly reduced by EPZ pretreatment, supporting its recognition by anti SDMA antibodies. (C) Sera from three 12 week old MRL lpr littermates (Lpr 1, 2, 3) each showed distinct band patterns against the cell lysates. EPZ pretreatment of the cells reduced the intensity of several bands in all three mice. (D) Workflow for isolating hybridoma clones from individual plasma cells to obtain monoclonal antibodies (mAbs) specific for SDMA. MRL lpr mice were not immunized with any antigen; thus, the resulting mAbs represent naturally arising autoantibodies. (E) Two antibody clones were tested against the native versus SDMA peptide array shown in Figurè3. Clone P4A2F4 reacted extensively with most SDMA containing peptides, whereas clone P2C1C10 showed no reactivity. (F) The two mAbs produced different band patterns on cell lysates. P4A2F4 recognized bands that were reduced in EPZ pretreated lysates, consistent with SDMA specificity. (G) After implantation of the SDMA-reactive hybridoma clone into the peritoneal cavity of healthy BALB/c mice, the kidneys showed extensive IgG deposition, reminiscent of human lupus nephritis.
    High Binding Elisa Plates, supplied by Greiner Bio, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    high binding microplates  (R&D Systems)
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    (A) Sera from MRL lpr mice (n=12, bled weekly from 8 to 13 weeks of age) were analyzed by <t>ELISA</t> using synthetic 10×RG peptides: native sequence (GRGRGRGRGRGRGRGRGRGR) vs. SDMA-modified (lowercase ‘r’ denotes SDMA; GrGrGrGRGRGrGrGrGRGR). All 12 mice developed anti SDMA antibody titers above the corresponding native controls, and the majority (9/12) showed a gradual increase in anti-SDMA titers over time. (B) Immunoblotting of HEp-2 lysates revealed progressive changes in band patterns from 10 weeks onward. To identify SDMA specific reactive proteins, cells were pretreated with the methyltransferase inhibitor EPZ015666 (EPZ) before lysis. A prominent ∼15 kDa band (arrowhead) was markedly reduced by EPZ pretreatment, supporting its recognition by anti SDMA antibodies. (C) Sera from three 12 week old MRL lpr littermates (Lpr 1, 2, 3) each showed distinct band patterns against the cell lysates. EPZ pretreatment of the cells reduced the intensity of several bands in all three mice. (D) Workflow for isolating hybridoma clones from individual plasma cells to obtain monoclonal antibodies (mAbs) specific for SDMA. MRL lpr mice were not immunized with any antigen; thus, the resulting mAbs represent naturally arising autoantibodies. (E) Two antibody clones were tested against the native versus SDMA peptide array shown in Figurè3. Clone P4A2F4 reacted extensively with most SDMA containing peptides, whereas clone P2C1C10 showed no reactivity. (F) The two mAbs produced different band patterns on cell lysates. P4A2F4 recognized bands that were reduced in EPZ pretreated lysates, consistent with SDMA specificity. (G) After implantation of the SDMA-reactive hybridoma clone into the peritoneal cavity of healthy BALB/c mice, the kidneys showed extensive IgG deposition, reminiscent of human lupus nephritis.
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    high binding clear bottom plates  (Greiner Bio)
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    (A) Sera from MRL lpr mice (n=12, bled weekly from 8 to 13 weeks of age) were analyzed by <t>ELISA</t> using synthetic 10×RG peptides: native sequence (GRGRGRGRGRGRGRGRGRGR) vs. SDMA-modified (lowercase ‘r’ denotes SDMA; GrGrGrGRGRGrGrGrGRGR). All 12 mice developed anti SDMA antibody titers above the corresponding native controls, and the majority (9/12) showed a gradual increase in anti-SDMA titers over time. (B) Immunoblotting of HEp-2 lysates revealed progressive changes in band patterns from 10 weeks onward. To identify SDMA specific reactive proteins, cells were pretreated with the methyltransferase inhibitor EPZ015666 (EPZ) before lysis. A prominent ∼15 kDa band (arrowhead) was markedly reduced by EPZ pretreatment, supporting its recognition by anti SDMA antibodies. (C) Sera from three 12 week old MRL lpr littermates (Lpr 1, 2, 3) each showed distinct band patterns against the cell lysates. EPZ pretreatment of the cells reduced the intensity of several bands in all three mice. (D) Workflow for isolating hybridoma clones from individual plasma cells to obtain monoclonal antibodies (mAbs) specific for SDMA. MRL lpr mice were not immunized with any antigen; thus, the resulting mAbs represent naturally arising autoantibodies. (E) Two antibody clones were tested against the native versus SDMA peptide array shown in Figurè3. Clone P4A2F4 reacted extensively with most SDMA containing peptides, whereas clone P2C1C10 showed no reactivity. (F) The two mAbs produced different band patterns on cell lysates. P4A2F4 recognized bands that were reduced in EPZ pretreated lysates, consistent with SDMA specificity. (G) After implantation of the SDMA-reactive hybridoma clone into the peritoneal cavity of healthy BALB/c mice, the kidneys showed extensive IgG deposition, reminiscent of human lupus nephritis.
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    (A) Sera from MRL lpr mice (n=12, bled weekly from 8 to 13 weeks of age) were analyzed by <t>ELISA</t> using synthetic 10×RG peptides: native sequence (GRGRGRGRGRGRGRGRGRGR) vs. SDMA-modified (lowercase ‘r’ denotes SDMA; GrGrGrGRGRGrGrGrGRGR). All 12 mice developed anti SDMA antibody titers above the corresponding native controls, and the majority (9/12) showed a gradual increase in anti-SDMA titers over time. (B) Immunoblotting of HEp-2 lysates revealed progressive changes in band patterns from 10 weeks onward. To identify SDMA specific reactive proteins, cells were pretreated with the methyltransferase inhibitor EPZ015666 (EPZ) before lysis. A prominent ∼15 kDa band (arrowhead) was markedly reduced by EPZ pretreatment, supporting its recognition by anti SDMA antibodies. (C) Sera from three 12 week old MRL lpr littermates (Lpr 1, 2, 3) each showed distinct band patterns against the cell lysates. EPZ pretreatment of the cells reduced the intensity of several bands in all three mice. (D) Workflow for isolating hybridoma clones from individual plasma cells to obtain monoclonal antibodies (mAbs) specific for SDMA. MRL lpr mice were not immunized with any antigen; thus, the resulting mAbs represent naturally arising autoantibodies. (E) Two antibody clones were tested against the native versus SDMA peptide array shown in Figurè3. Clone P4A2F4 reacted extensively with most SDMA containing peptides, whereas clone P2C1C10 showed no reactivity. (F) The two mAbs produced different band patterns on cell lysates. P4A2F4 recognized bands that were reduced in EPZ pretreated lysates, consistent with SDMA specificity. (G) After implantation of the SDMA-reactive hybridoma clone into the peritoneal cavity of healthy BALB/c mice, the kidneys showed extensive IgG deposition, reminiscent of human lupus nephritis.
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    high binding 96 well plates  (Greiner Bio)
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    (A) Sera from MRL lpr mice (n=12, bled weekly from 8 to 13 weeks of age) were analyzed by <t>ELISA</t> using synthetic 10×RG peptides: native sequence (GRGRGRGRGRGRGRGRGRGR) vs. SDMA-modified (lowercase ‘r’ denotes SDMA; GrGrGrGRGRGrGrGrGRGR). All 12 mice developed anti SDMA antibody titers above the corresponding native controls, and the majority (9/12) showed a gradual increase in anti-SDMA titers over time. (B) Immunoblotting of HEp-2 lysates revealed progressive changes in band patterns from 10 weeks onward. To identify SDMA specific reactive proteins, cells were pretreated with the methyltransferase inhibitor EPZ015666 (EPZ) before lysis. A prominent ∼15 kDa band (arrowhead) was markedly reduced by EPZ pretreatment, supporting its recognition by anti SDMA antibodies. (C) Sera from three 12 week old MRL lpr littermates (Lpr 1, 2, 3) each showed distinct band patterns against the cell lysates. EPZ pretreatment of the cells reduced the intensity of several bands in all three mice. (D) Workflow for isolating hybridoma clones from individual plasma cells to obtain monoclonal antibodies (mAbs) specific for SDMA. MRL lpr mice were not immunized with any antigen; thus, the resulting mAbs represent naturally arising autoantibodies. (E) Two antibody clones were tested against the native versus SDMA peptide array shown in Figurè3. Clone P4A2F4 reacted extensively with most SDMA containing peptides, whereas clone P2C1C10 showed no reactivity. (F) The two mAbs produced different band patterns on cell lysates. P4A2F4 recognized bands that were reduced in EPZ pretreated lysates, consistent with SDMA specificity. (G) After implantation of the SDMA-reactive hybridoma clone into the peritoneal cavity of healthy BALB/c mice, the kidneys showed extensive IgG deposition, reminiscent of human lupus nephritis.
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    (A) Sera from MRL lpr mice (n=12, bled weekly from 8 to 13 weeks of age) were analyzed by <t>ELISA</t> using synthetic 10×RG peptides: native sequence (GRGRGRGRGRGRGRGRGRGR) vs. SDMA-modified (lowercase ‘r’ denotes SDMA; GrGrGrGRGRGrGrGrGRGR). All 12 mice developed anti SDMA antibody titers above the corresponding native controls, and the majority (9/12) showed a gradual increase in anti-SDMA titers over time. (B) Immunoblotting of HEp-2 lysates revealed progressive changes in band patterns from 10 weeks onward. To identify SDMA specific reactive proteins, cells were pretreated with the methyltransferase inhibitor EPZ015666 (EPZ) before lysis. A prominent ∼15 kDa band (arrowhead) was markedly reduced by EPZ pretreatment, supporting its recognition by anti SDMA antibodies. (C) Sera from three 12 week old MRL lpr littermates (Lpr 1, 2, 3) each showed distinct band patterns against the cell lysates. EPZ pretreatment of the cells reduced the intensity of several bands in all three mice. (D) Workflow for isolating hybridoma clones from individual plasma cells to obtain monoclonal antibodies (mAbs) specific for SDMA. MRL lpr mice were not immunized with any antigen; thus, the resulting mAbs represent naturally arising autoantibodies. (E) Two antibody clones were tested against the native versus SDMA peptide array shown in Figurè3. Clone P4A2F4 reacted extensively with most SDMA containing peptides, whereas clone P2C1C10 showed no reactivity. (F) The two mAbs produced different band patterns on cell lysates. P4A2F4 recognized bands that were reduced in EPZ pretreated lysates, consistent with SDMA specificity. (G) After implantation of the SDMA-reactive hybridoma clone into the peritoneal cavity of healthy BALB/c mice, the kidneys showed extensive IgG deposition, reminiscent of human lupus nephritis.
    High Binding Plates, supplied by Greiner Bio, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    high binding 96 well plates  (R&D Systems)
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    (A) Sera from MRL lpr mice (n=12, bled weekly from 8 to 13 weeks of age) were analyzed by <t>ELISA</t> using synthetic 10×RG peptides: native sequence (GRGRGRGRGRGRGRGRGRGR) vs. SDMA-modified (lowercase ‘r’ denotes SDMA; GrGrGrGRGRGrGrGrGRGR). All 12 mice developed anti SDMA antibody titers above the corresponding native controls, and the majority (9/12) showed a gradual increase in anti-SDMA titers over time. (B) Immunoblotting of HEp-2 lysates revealed progressive changes in band patterns from 10 weeks onward. To identify SDMA specific reactive proteins, cells were pretreated with the methyltransferase inhibitor EPZ015666 (EPZ) before lysis. A prominent ∼15 kDa band (arrowhead) was markedly reduced by EPZ pretreatment, supporting its recognition by anti SDMA antibodies. (C) Sera from three 12 week old MRL lpr littermates (Lpr 1, 2, 3) each showed distinct band patterns against the cell lysates. EPZ pretreatment of the cells reduced the intensity of several bands in all three mice. (D) Workflow for isolating hybridoma clones from individual plasma cells to obtain monoclonal antibodies (mAbs) specific for SDMA. MRL lpr mice were not immunized with any antigen; thus, the resulting mAbs represent naturally arising autoantibodies. (E) Two antibody clones were tested against the native versus SDMA peptide array shown in Figurè3. Clone P4A2F4 reacted extensively with most SDMA containing peptides, whereas clone P2C1C10 showed no reactivity. (F) The two mAbs produced different band patterns on cell lysates. P4A2F4 recognized bands that were reduced in EPZ pretreated lysates, consistent with SDMA specificity. (G) After implantation of the SDMA-reactive hybridoma clone into the peritoneal cavity of healthy BALB/c mice, the kidneys showed extensive IgG deposition, reminiscent of human lupus nephritis.
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    high binding polystyrene microplate  (Greiner Bio)
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    Greiner Bio high binding polystyrene microplate
    Detection of cathelicidin (LL-37) and myeloperoxidase (MPO) in human urine samples. Protein concentrations in human urine samples were detected by ELISA. The samples were analyzed in a <t>microplate</t> reader. Bar represents mean ± SD of each group. Protein levels were compared across groups (A, C) and subgroups (B, D). (A, C) LL-37 and MPO concentrations are higher in infected (Group A and B) than in healthy urines (Control). (B, D) No difference in protein concentrations was found when comparing the subgroups of Group A. ****p < 0.0001.
    High Binding Polystyrene Microplate, supplied by Greiner Bio, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    high binding half area microplates  (Greiner Bio)
    95
    Greiner Bio high binding half area microplates
    Detection of cathelicidin (LL-37) and myeloperoxidase (MPO) in human urine samples. Protein concentrations in human urine samples were detected by ELISA. The samples were analyzed in a <t>microplate</t> reader. Bar represents mean ± SD of each group. Protein levels were compared across groups (A, C) and subgroups (B, D). (A, C) LL-37 and MPO concentrations are higher in infected (Group A and B) than in healthy urines (Control). (B, D) No difference in protein concentrations was found when comparing the subgroups of Group A. ****p < 0.0001.
    High Binding Half Area Microplates, supplied by Greiner Bio, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/high+binding+microplate/Microplate+96+Well+Ps+Half+Area+White/pm41742422-306-13-16
    Average 95 stars, based on 1 article reviews
    high binding half area microplates - by Bioz Stars, 2026-10
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    high binding microplate  (Greiner Bio)
    95
    Greiner Bio high binding microplate
    Detection of cathelicidin (LL-37) and myeloperoxidase (MPO) in human urine samples. Protein concentrations in human urine samples were detected by ELISA. The samples were analyzed in a <t>microplate</t> reader. Bar represents mean ± SD of each group. Protein levels were compared across groups (A, C) and subgroups (B, D). (A, C) LL-37 and MPO concentrations are higher in infected (Group A and B) than in healthy urines (Control). (B, D) No difference in protein concentrations was found when comparing the subgroups of Group A. ****p < 0.0001.
    High Binding Microplate, supplied by Greiner Bio, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/high+binding+microplate/Elisa+Microplate+96+Well+Ps+C-Bottom/bio_rxiv__64898__2026__03__04__709591-269-3-5
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    (A) Sera from MRL lpr mice (n=12, bled weekly from 8 to 13 weeks of age) were analyzed by ELISA using synthetic 10×RG peptides: native sequence (GRGRGRGRGRGRGRGRGRGR) vs. SDMA-modified (lowercase ‘r’ denotes SDMA; GrGrGrGRGRGrGrGrGRGR). All 12 mice developed anti SDMA antibody titers above the corresponding native controls, and the majority (9/12) showed a gradual increase in anti-SDMA titers over time. (B) Immunoblotting of HEp-2 lysates revealed progressive changes in band patterns from 10 weeks onward. To identify SDMA specific reactive proteins, cells were pretreated with the methyltransferase inhibitor EPZ015666 (EPZ) before lysis. A prominent ∼15 kDa band (arrowhead) was markedly reduced by EPZ pretreatment, supporting its recognition by anti SDMA antibodies. (C) Sera from three 12 week old MRL lpr littermates (Lpr 1, 2, 3) each showed distinct band patterns against the cell lysates. EPZ pretreatment of the cells reduced the intensity of several bands in all three mice. (D) Workflow for isolating hybridoma clones from individual plasma cells to obtain monoclonal antibodies (mAbs) specific for SDMA. MRL lpr mice were not immunized with any antigen; thus, the resulting mAbs represent naturally arising autoantibodies. (E) Two antibody clones were tested against the native versus SDMA peptide array shown in Figurè3. Clone P4A2F4 reacted extensively with most SDMA containing peptides, whereas clone P2C1C10 showed no reactivity. (F) The two mAbs produced different band patterns on cell lysates. P4A2F4 recognized bands that were reduced in EPZ pretreated lysates, consistent with SDMA specificity. (G) After implantation of the SDMA-reactive hybridoma clone into the peritoneal cavity of healthy BALB/c mice, the kidneys showed extensive IgG deposition, reminiscent of human lupus nephritis.

    Journal: bioRxiv

    Article Title: Symmetric Dimethylarginine Modification Drives Shared and Divergent Antigen Reactivity in Lupus

    doi: 10.64898/2026.09.22.753525

    Figure Lengend Snippet: (A) Sera from MRL lpr mice (n=12, bled weekly from 8 to 13 weeks of age) were analyzed by ELISA using synthetic 10×RG peptides: native sequence (GRGRGRGRGRGRGRGRGRGR) vs. SDMA-modified (lowercase ‘r’ denotes SDMA; GrGrGrGRGRGrGrGrGRGR). All 12 mice developed anti SDMA antibody titers above the corresponding native controls, and the majority (9/12) showed a gradual increase in anti-SDMA titers over time. (B) Immunoblotting of HEp-2 lysates revealed progressive changes in band patterns from 10 weeks onward. To identify SDMA specific reactive proteins, cells were pretreated with the methyltransferase inhibitor EPZ015666 (EPZ) before lysis. A prominent ∼15 kDa band (arrowhead) was markedly reduced by EPZ pretreatment, supporting its recognition by anti SDMA antibodies. (C) Sera from three 12 week old MRL lpr littermates (Lpr 1, 2, 3) each showed distinct band patterns against the cell lysates. EPZ pretreatment of the cells reduced the intensity of several bands in all three mice. (D) Workflow for isolating hybridoma clones from individual plasma cells to obtain monoclonal antibodies (mAbs) specific for SDMA. MRL lpr mice were not immunized with any antigen; thus, the resulting mAbs represent naturally arising autoantibodies. (E) Two antibody clones were tested against the native versus SDMA peptide array shown in Figurè3. Clone P4A2F4 reacted extensively with most SDMA containing peptides, whereas clone P2C1C10 showed no reactivity. (F) The two mAbs produced different band patterns on cell lysates. P4A2F4 recognized bands that were reduced in EPZ pretreated lysates, consistent with SDMA specificity. (G) After implantation of the SDMA-reactive hybridoma clone into the peritoneal cavity of healthy BALB/c mice, the kidneys showed extensive IgG deposition, reminiscent of human lupus nephritis.

    Article Snippet: High-binding ELISA plates (Greiner Bio-One, 655081) were coated with 250 ng/well of streptavidin (Leinco Technologies, S203) overnight at 4°C.

    Techniques: Enzyme-linked Immunosorbent Assay, Sequencing, Modification, Western Blot, Lysis, Clone Assay, Clinical Proteomics, Bioprocessing, Autoantibodies, Peptide Microarray, Produced

    Detection of cathelicidin (LL-37) and myeloperoxidase (MPO) in human urine samples. Protein concentrations in human urine samples were detected by ELISA. The samples were analyzed in a microplate reader. Bar represents mean ± SD of each group. Protein levels were compared across groups (A, C) and subgroups (B, D). (A, C) LL-37 and MPO concentrations are higher in infected (Group A and B) than in healthy urines (Control). (B, D) No difference in protein concentrations was found when comparing the subgroups of Group A. ****p < 0.0001.

    Journal: Frontiers in Immunology

    Article Title: Presence of neutrophil extracellular traps (NETs) in different types of human urinary tract infections (UTI). A pilot study

    doi: 10.3389/fimmu.2026.1745166

    Figure Lengend Snippet: Detection of cathelicidin (LL-37) and myeloperoxidase (MPO) in human urine samples. Protein concentrations in human urine samples were detected by ELISA. The samples were analyzed in a microplate reader. Bar represents mean ± SD of each group. Protein levels were compared across groups (A, C) and subgroups (B, D). (A, C) LL-37 and MPO concentrations are higher in infected (Group A and B) than in healthy urines (Control). (B, D) No difference in protein concentrations was found when comparing the subgroups of Group A. ****p < 0.0001.

    Article Snippet: For the MPO-specific ELISA kit, a 96-well high-binding polystyrene microplate (F-bottom, Greiner Bio-One, #655061) was used.

    Techniques: Enzyme-linked Immunosorbent Assay, Infection, Control