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spectraplate 384 with high protein binding  (Revvity)


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    Revvity spectraplate 384 with high protein binding

    Spectraplate 384 With High Protein Binding, supplied by Revvity, used in various techniques. Bioz Stars score: 91/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/high+binding+microplate/SpectraPlate-384+HB%2C+Clear+384-well+Microplate+with+High+Protein+Binding+Affinity/pmc07843029-87-0-6
    Average 91 stars, based on 7 article reviews
    spectraplate 384 with high protein binding - by Bioz Stars, 2026-10
    91/100 stars

    Images

    1) Product Images from "Circulating SARS-CoV-2 spike N439K variants maintain fitness while evading antibody-mediated immunity"

    Article Title: Circulating SARS-CoV-2 spike N439K variants maintain fitness while evading antibody-mediated immunity

    Journal: Cell

    doi: 10.1016/j.cell.2021.01.037


    Figure Legend Snippet:

    Techniques Used: Virus, Clinical Proteomics, Infection, Recombinant, Blocking Assay, Transfection, Multiplex Assay, Protein Binding, Expressing, Plasmid Preparation, Software, Sequencing, Real-time Polymerase Chain Reaction

    Related Articles

    Enzyme-linked Immunosorbent Assay:

    Article Title: PTEN acts as a metabolic checkpoint molecule in mature B cells to suppress TLR9-mediated inflammation
    Article Snippet: Data were analyzed by TargetLynx software (Waters). .. ELISA assay Serum IgM and IgG1 were captured by Goat anti-mouse IgM (1020-1, Southern Biotech) and IgG1 (1070-1, Southern Biotech) antibodies which were coated on the surface of SpectraPlate-384 HB (6007500, PerkinElmer), and then those titers were detected by HRP-conjugated goat anti-mouse IgG (115-035- 174, Jackson ImmunoResearch). .. Serum autoantibodies were determined by using anti-dsDNA ELISA Kit (AKRDD-061, Fuji lm-Wako-Shibayagi inc.) and anti-nuclear antibody ELISA kit (ABIN772680, antibodiesonline GmbH).


    Software:


    Blocking Assay:


    Clinical Proteomics:


    Concentration Assay:


    Incubation:




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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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    Image Search Results


    (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