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anti human cd81 af488 antibody  (R&D Systems)


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    Structured Review

    R&D Systems anti human cd81 af488 antibody
    Characterization of EV. Particle numbers (A) and relative protein concentrations (B) in the fractions eluted following qEV size-exclusion chromatography. Data are mean ± SEM. (C) Tetraspanin (CD9, CD63, and <t>CD81)</t> content of purified EVs was analyzed in the indicated elution fractions by immunoblotting. (D) Size distribution of pooled fractions 7 to 10 from HDFs (left panel) and L3.6 cells (right panel). (E) Electron microscopy image of EV from HDFs (left panel) and L3.6 cells (right panel).
    Anti Human Cd81 Af488 Antibody, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/anti+human+cd81+af488+antibody/Human+CD81+Alexa+Fluor%C2%AE+488-conjugated+Antibody/pmc08759128-69-0-6
    Average 93 stars, based on 3 article reviews
    anti human cd81 af488 antibody - by Bioz Stars, 2026-10
    93/100 stars

    Images

    1) Product Images from "Polyphosphate expression by cancer cell extracellular vesicles mediates binding of factor XII and contact activation"

    Article Title: Polyphosphate expression by cancer cell extracellular vesicles mediates binding of factor XII and contact activation

    Journal: Blood Advances

    doi: 10.1182/bloodadvances.2021005116

    Characterization of EV. Particle numbers (A) and relative protein concentrations (B) in the fractions eluted following qEV size-exclusion chromatography. Data are mean ± SEM. (C) Tetraspanin (CD9, CD63, and CD81) content of purified EVs was analyzed in the indicated elution fractions by immunoblotting. (D) Size distribution of pooled fractions 7 to 10 from HDFs (left panel) and L3.6 cells (right panel). (E) Electron microscopy image of EV from HDFs (left panel) and L3.6 cells (right panel).
    Figure Legend Snippet: Characterization of EV. Particle numbers (A) and relative protein concentrations (B) in the fractions eluted following qEV size-exclusion chromatography. Data are mean ± SEM. (C) Tetraspanin (CD9, CD63, and CD81) content of purified EVs was analyzed in the indicated elution fractions by immunoblotting. (D) Size distribution of pooled fractions 7 to 10 from HDFs (left panel) and L3.6 cells (right panel). (E) Electron microscopy image of EV from HDFs (left panel) and L3.6 cells (right panel).

    Techniques Used: Size-exclusion Chromatography, Purification, Western Blot, Electron Microscopy

    polyP on EV derived from cancer cells mediates ligand binding. (A) The amount of polyP associated with cancer cell–derived EV was estimated by comparison with a standard curve (supplemental Figure 2A). (B) Detection of polyP on L3.6-derived EVs following incubation with buffer (HBS), DNase I and RNase A (D/R), or CIP. polyP of different chain lengths was used to estimate the size of EV-associated polyP. L3.6-derived EVs were preincubated with buffer or E coli PPX, and the binding of PPX-Δ12–AF488 (C), anti-CD81–AF488 (D), and or FXII-AF488 (E) was measured. The number of total EV was determined in scatter mode, and the number of ligand-binding EV was determined in fluorescence mode using a 488-nm excitation laser. The differences in fluorescent particle numbers were compared by estimating the area under each curve (AUC) using GraphPad Prism 8. Bars represent means ± SEM. *** P < .001, 1-way ANOVA with multiple comparisons. L, long; M, medium; S, short.
    Figure Legend Snippet: polyP on EV derived from cancer cells mediates ligand binding. (A) The amount of polyP associated with cancer cell–derived EV was estimated by comparison with a standard curve (supplemental Figure 2A). (B) Detection of polyP on L3.6-derived EVs following incubation with buffer (HBS), DNase I and RNase A (D/R), or CIP. polyP of different chain lengths was used to estimate the size of EV-associated polyP. L3.6-derived EVs were preincubated with buffer or E coli PPX, and the binding of PPX-Δ12–AF488 (C), anti-CD81–AF488 (D), and or FXII-AF488 (E) was measured. The number of total EV was determined in scatter mode, and the number of ligand-binding EV was determined in fluorescence mode using a 488-nm excitation laser. The differences in fluorescent particle numbers were compared by estimating the area under each curve (AUC) using GraphPad Prism 8. Bars represent means ± SEM. *** P < .001, 1-way ANOVA with multiple comparisons. L, long; M, medium; S, short.

    Techniques Used: Derivative Assay, Ligand Binding Assay, Comparison, Incubation, Binding Assay, Fluorescence

    Related Articles

    Control:

    Article Title: Polyphosphate expression by cancer cell extracellular vesicles mediates binding of factor XII and contact activation
    Article Snippet: .. Anti-human CD81-AF488 antibody (20 μg/mL, FAB4615G; R&D Systems) was used as a control ligand. ..



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    93
    R&D Systems anti human cd81 af488 antibody
    Characterization of EV. Particle numbers (A) and relative protein concentrations (B) in the fractions eluted following qEV size-exclusion chromatography. Data are mean ± SEM. (C) Tetraspanin (CD9, CD63, and <t>CD81)</t> content of purified EVs was analyzed in the indicated elution fractions by immunoblotting. (D) Size distribution of pooled fractions 7 to 10 from HDFs (left panel) and L3.6 cells (right panel). (E) Electron microscopy image of EV from HDFs (left panel) and L3.6 cells (right panel).
    Anti Human Cd81 Af488 Antibody, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/anti+human+cd81+af488+antibody/Human+CD81+Alexa+Fluor%C2%AE+488-conjugated+Antibody/pmc08759128-69-0-6
    Average 93 stars, based on 1 article reviews
    anti human cd81 af488 antibody - by Bioz Stars, 2026-10
    93/100 stars
      Buy from Supplier

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    Characterization of EV. Particle numbers (A) and relative protein concentrations (B) in the fractions eluted following qEV size-exclusion chromatography. Data are mean ± SEM. (C) Tetraspanin (CD9, CD63, and CD81) content of purified EVs was analyzed in the indicated elution fractions by immunoblotting. (D) Size distribution of pooled fractions 7 to 10 from HDFs (left panel) and L3.6 cells (right panel). (E) Electron microscopy image of EV from HDFs (left panel) and L3.6 cells (right panel).

    Journal: Blood Advances

    Article Title: Polyphosphate expression by cancer cell extracellular vesicles mediates binding of factor XII and contact activation

    doi: 10.1182/bloodadvances.2021005116

    Figure Lengend Snippet: Characterization of EV. Particle numbers (A) and relative protein concentrations (B) in the fractions eluted following qEV size-exclusion chromatography. Data are mean ± SEM. (C) Tetraspanin (CD9, CD63, and CD81) content of purified EVs was analyzed in the indicated elution fractions by immunoblotting. (D) Size distribution of pooled fractions 7 to 10 from HDFs (left panel) and L3.6 cells (right panel). (E) Electron microscopy image of EV from HDFs (left panel) and L3.6 cells (right panel).

    Article Snippet: Anti-human CD81-AF488 antibody (20 μg/mL, FAB4615G; R&D Systems) was used as a control ligand.

    Techniques: Size-exclusion Chromatography, Purification, Western Blot, Electron Microscopy

    polyP on EV derived from cancer cells mediates ligand binding. (A) The amount of polyP associated with cancer cell–derived EV was estimated by comparison with a standard curve (supplemental Figure 2A). (B) Detection of polyP on L3.6-derived EVs following incubation with buffer (HBS), DNase I and RNase A (D/R), or CIP. polyP of different chain lengths was used to estimate the size of EV-associated polyP. L3.6-derived EVs were preincubated with buffer or E coli PPX, and the binding of PPX-Δ12–AF488 (C), anti-CD81–AF488 (D), and or FXII-AF488 (E) was measured. The number of total EV was determined in scatter mode, and the number of ligand-binding EV was determined in fluorescence mode using a 488-nm excitation laser. The differences in fluorescent particle numbers were compared by estimating the area under each curve (AUC) using GraphPad Prism 8. Bars represent means ± SEM. *** P < .001, 1-way ANOVA with multiple comparisons. L, long; M, medium; S, short.

    Journal: Blood Advances

    Article Title: Polyphosphate expression by cancer cell extracellular vesicles mediates binding of factor XII and contact activation

    doi: 10.1182/bloodadvances.2021005116

    Figure Lengend Snippet: polyP on EV derived from cancer cells mediates ligand binding. (A) The amount of polyP associated with cancer cell–derived EV was estimated by comparison with a standard curve (supplemental Figure 2A). (B) Detection of polyP on L3.6-derived EVs following incubation with buffer (HBS), DNase I and RNase A (D/R), or CIP. polyP of different chain lengths was used to estimate the size of EV-associated polyP. L3.6-derived EVs were preincubated with buffer or E coli PPX, and the binding of PPX-Δ12–AF488 (C), anti-CD81–AF488 (D), and or FXII-AF488 (E) was measured. The number of total EV was determined in scatter mode, and the number of ligand-binding EV was determined in fluorescence mode using a 488-nm excitation laser. The differences in fluorescent particle numbers were compared by estimating the area under each curve (AUC) using GraphPad Prism 8. Bars represent means ± SEM. *** P < .001, 1-way ANOVA with multiple comparisons. L, long; M, medium; S, short.

    Article Snippet: Anti-human CD81-AF488 antibody (20 μg/mL, FAB4615G; R&D Systems) was used as a control ligand.

    Techniques: Derivative Assay, Ligand Binding Assay, Comparison, Incubation, Binding Assay, Fluorescence