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mouse anti transferrin receptor cd71 mab  (Danaher Inc)


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    Structured Review

    Danaher Inc mouse anti transferrin receptor cd71 mab
    Lipid microdomains localization of LRP8 and phospho-Dab2 following triggering with anti-β2-GPI antibodies. ( A ). Sucrose gradient fractions obtained from HUVECs, treated with affinity-purified anti-β2-GPI antibodies for 45 min, or left untreated, were analyzed with Western Blot using anti-LRP8 mAb, anti-phospho-Dab2 (ser24) Ab, <t>anti-CD71</t> mAb or anti-flotillin Ab. Right panel. Bar graphs of densitometric analysis. The columns indicate the percentage distribution across the gel of raft fractions 4-5-6 (Triton X-100-insoluble fractions) and 9-10-11 (Tri-ton X-100-soluble fractions), as detected with scanning densitometric analysis. Results represent the mean ± SD from 3 independent experiments. **** p < 0.0001. ( B ). Fractions (4–6) (insoluble Triton X-100 fractions) and fractions 9–11 (soluble Triton X-100 fractions) were spotted onto nitrocellulose strips and analyzed via dot blot using Cholera Toxin (CTx) B Subunit-Peroxidase.
    Mouse Anti Transferrin Receptor Cd71 Mab, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Role of Lipid Rafts on LRP8 Signaling Triggered by Anti-β2-GPI Antibodies in Endothelial Cells"

    Article Title: Role of Lipid Rafts on LRP8 Signaling Triggered by Anti-β2-GPI Antibodies in Endothelial Cells

    Journal: Biomedicines

    doi: 10.3390/biomedicines11123135

    Lipid microdomains localization of LRP8 and phospho-Dab2 following triggering with anti-β2-GPI antibodies. ( A ). Sucrose gradient fractions obtained from HUVECs, treated with affinity-purified anti-β2-GPI antibodies for 45 min, or left untreated, were analyzed with Western Blot using anti-LRP8 mAb, anti-phospho-Dab2 (ser24) Ab, anti-CD71 mAb or anti-flotillin Ab. Right panel. Bar graphs of densitometric analysis. The columns indicate the percentage distribution across the gel of raft fractions 4-5-6 (Triton X-100-insoluble fractions) and 9-10-11 (Tri-ton X-100-soluble fractions), as detected with scanning densitometric analysis. Results represent the mean ± SD from 3 independent experiments. **** p < 0.0001. ( B ). Fractions (4–6) (insoluble Triton X-100 fractions) and fractions 9–11 (soluble Triton X-100 fractions) were spotted onto nitrocellulose strips and analyzed via dot blot using Cholera Toxin (CTx) B Subunit-Peroxidase.
    Figure Legend Snippet: Lipid microdomains localization of LRP8 and phospho-Dab2 following triggering with anti-β2-GPI antibodies. ( A ). Sucrose gradient fractions obtained from HUVECs, treated with affinity-purified anti-β2-GPI antibodies for 45 min, or left untreated, were analyzed with Western Blot using anti-LRP8 mAb, anti-phospho-Dab2 (ser24) Ab, anti-CD71 mAb or anti-flotillin Ab. Right panel. Bar graphs of densitometric analysis. The columns indicate the percentage distribution across the gel of raft fractions 4-5-6 (Triton X-100-insoluble fractions) and 9-10-11 (Tri-ton X-100-soluble fractions), as detected with scanning densitometric analysis. Results represent the mean ± SD from 3 independent experiments. **** p < 0.0001. ( B ). Fractions (4–6) (insoluble Triton X-100 fractions) and fractions 9–11 (soluble Triton X-100 fractions) were spotted onto nitrocellulose strips and analyzed via dot blot using Cholera Toxin (CTx) B Subunit-Peroxidase.

    Techniques Used: Affinity Purification, Western Blot, Dot Blot



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    a Schematic representation of CSPs upregulated in hypoxic NPC identified through DGE analysis among a total of 1442 CSPs. b Left: Venn diagram illustrating the intersection of CSPs upregulated in tumor samples of the three cohorts: GSE12452 (log 2 (fold change) >1 and P < 0.01), GSE53819 (log 2 (fold change) >1 and P < 0.01), and GSE61218 (log 2 (fold change) >1 and P < 0.01). Right: Venn diagram illustrating the intersection of CSPs that are upregulated in tumor samples with high hypoxia scores of the GSE102349 cohort (log 2 (fold change) >10 and P < 0.01). c Distribution of <t>TfR1</t> mRNA abundance in tumor and normal samples from different cohorts: GSE12452 (normal, n = 10; tumor, n = 31), GSE53819 (normal, n = 18; tumor, n = 18), and GSE61218 (normal, n = 6; tumor, n = 10). d Distribution of TFRC mRNA abundance in tumor samples from the GSE102349 cohort ( n = 113) with high or low hypoxia scores. e Representative images of IHC staining showing TfR1 protein expression in clinical primary NPC tissues and NNE tissues collected from multiple patients. Scale bar, 50 μm. f Distribution of TfR1 IHC staining scores in NPC ( n = 174) and NNE ( n = 98) tissues. g Distribution of TfR1 IHC staining scores in NPC and matched adjacent non-cancerous tissues ( n = 117). h IF staining analysis in NPC tissues depicting the co-expression of HIF-1α and TfR1. Scale bar, 50 μm. i Spearman correlation between HIF-1α expression and TfR1 expression based on h ( n = 40 random regions from different tissues). The box plots in c , d , and f show the median ±1 quartile, with whiskers extending to the minimum or maximum values within 1.5 times the interquartile range from the box boundaries. Mann–Whitney test in c , d , and f and Wilcoxon matched-pairs signed rank test in g were used to calculate P values. Source data are provided as a Source Data file.
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    a Schematic representation of CSPs upregulated in hypoxic NPC identified through DGE analysis among a total of 1442 CSPs. b Left: Venn diagram illustrating the intersection of CSPs upregulated in tumor samples of the three cohorts: GSE12452 (log 2 (fold change) >1 and P < 0.01), GSE53819 (log 2 (fold change) >1 and P < 0.01), and GSE61218 (log 2 (fold change) >1 and P < 0.01). Right: Venn diagram illustrating the intersection of CSPs that are upregulated in tumor samples with high hypoxia scores of the GSE102349 cohort (log 2 (fold change) >10 and P < 0.01). c Distribution of <t>TfR1</t> mRNA abundance in tumor and normal samples from different cohorts: GSE12452 (normal, n = 10; tumor, n = 31), GSE53819 (normal, n = 18; tumor, n = 18), and GSE61218 (normal, n = 6; tumor, n = 10). d Distribution of TFRC mRNA abundance in tumor samples from the GSE102349 cohort ( n = 113) with high or low hypoxia scores. e Representative images of IHC staining showing TfR1 protein expression in clinical primary NPC tissues and NNE tissues collected from multiple patients. Scale bar, 50 μm. f Distribution of TfR1 IHC staining scores in NPC ( n = 174) and NNE ( n = 98) tissues. g Distribution of TfR1 IHC staining scores in NPC and matched adjacent non-cancerous tissues ( n = 117). h IF staining analysis in NPC tissues depicting the co-expression of HIF-1α and TfR1. Scale bar, 50 μm. i Spearman correlation between HIF-1α expression and TfR1 expression based on h ( n = 40 random regions from different tissues). The box plots in c , d , and f show the median ±1 quartile, with whiskers extending to the minimum or maximum values within 1.5 times the interquartile range from the box boundaries. Mann–Whitney test in c , d , and f and Wilcoxon matched-pairs signed rank test in g were used to calculate P values. Source data are provided as a Source Data file.
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    Lipid microdomains localization of LRP8 and phospho-Dab2 following triggering with anti-β2-GPI antibodies. ( A ). Sucrose gradient fractions obtained from HUVECs, treated with affinity-purified anti-β2-GPI antibodies for 45 min, or left untreated, were analyzed with Western Blot using anti-LRP8 mAb, anti-phospho-Dab2 (ser24) Ab, <t>anti-CD71</t> mAb or anti-flotillin Ab. Right panel. Bar graphs of densitometric analysis. The columns indicate the percentage distribution across the gel of raft fractions 4-5-6 (Triton X-100-insoluble fractions) and 9-10-11 (Tri-ton X-100-soluble fractions), as detected with scanning densitometric analysis. Results represent the mean ± SD from 3 independent experiments. **** p < 0.0001. ( B ). Fractions (4–6) (insoluble Triton X-100 fractions) and fractions 9–11 (soluble Triton X-100 fractions) were spotted onto nitrocellulose strips and analyzed via dot blot using Cholera Toxin (CTx) B Subunit-Peroxidase.
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    Lipid microdomains localization of LRP8 and phospho-Dab2 following triggering with anti-β2-GPI antibodies. ( A ). Sucrose gradient fractions obtained from HUVECs, treated with affinity-purified anti-β2-GPI antibodies for 45 min, or left untreated, were analyzed with Western Blot using anti-LRP8 mAb, anti-phospho-Dab2 (ser24) Ab, <t>anti-CD71</t> mAb or anti-flotillin Ab. Right panel. Bar graphs of densitometric analysis. The columns indicate the percentage distribution across the gel of raft fractions 4-5-6 (Triton X-100-insoluble fractions) and 9-10-11 (Tri-ton X-100-soluble fractions), as detected with scanning densitometric analysis. Results represent the mean ± SD from 3 independent experiments. **** p < 0.0001. ( B ). Fractions (4–6) (insoluble Triton X-100 fractions) and fractions 9–11 (soluble Triton X-100 fractions) were spotted onto nitrocellulose strips and analyzed via dot blot using Cholera Toxin (CTx) B Subunit-Peroxidase.
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    Lipid microdomains localization of LRP8 and phospho-Dab2 following triggering with anti-β2-GPI antibodies. ( A ). Sucrose gradient fractions obtained from HUVECs, treated with affinity-purified anti-β2-GPI antibodies for 45 min, or left untreated, were analyzed with Western Blot using anti-LRP8 mAb, anti-phospho-Dab2 (ser24) Ab, <t>anti-CD71</t> mAb or anti-flotillin Ab. Right panel. Bar graphs of densitometric analysis. The columns indicate the percentage distribution across the gel of raft fractions 4-5-6 (Triton X-100-insoluble fractions) and 9-10-11 (Tri-ton X-100-soluble fractions), as detected with scanning densitometric analysis. Results represent the mean ± SD from 3 independent experiments. **** p < 0.0001. ( B ). Fractions (4–6) (insoluble Triton X-100 fractions) and fractions 9–11 (soluble Triton X-100 fractions) were spotted onto nitrocellulose strips and analyzed via dot blot using Cholera Toxin (CTx) B Subunit-Peroxidase.
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    Figure 6. Morphology of BFA-sensitive compartments of R1 and R2 cells. Cells of the indicated cell lines were treated with 2.5 mg/ ml (A) or 5 mg/ml (B, C) BFA for 30 minutes, fixed and processed for the immunofluorescent detection of GM130 (A), TGN46 (B), or the <t>transferrin</t> receptor (C). The nuclei were stained with DAPI. Represen- tative confocal images are presented. Bar, 20 mm. doi:10.1371/journal.pone.0074491.g006
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    Figure 6. Morphology of BFA-sensitive compartments of R1 and R2 cells. Cells of the indicated cell lines were treated with 2.5 mg/ ml (A) or 5 mg/ml (B, C) BFA for 30 minutes, fixed and processed for the immunofluorescent detection of GM130 (A), TGN46 (B), or the <t>transferrin</t> receptor (C). The nuclei were stained with DAPI. Represen- tative confocal images are presented. Bar, 20 mm. doi:10.1371/journal.pone.0074491.g006
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    Figure 6. Morphology of BFA-sensitive compartments of R1 and R2 cells. Cells of the indicated cell lines were treated with 2.5 mg/ ml (A) or 5 mg/ml (B, C) BFA for 30 minutes, fixed and processed for the immunofluorescent detection of GM130 (A), TGN46 (B), or the <t>transferrin</t> receptor (C). The nuclei were stained with DAPI. Represen- tative confocal images are presented. Bar, 20 mm. doi:10.1371/journal.pone.0074491.g006
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    Image Search Results


    a Schematic representation of CSPs upregulated in hypoxic NPC identified through DGE analysis among a total of 1442 CSPs. b Left: Venn diagram illustrating the intersection of CSPs upregulated in tumor samples of the three cohorts: GSE12452 (log 2 (fold change) >1 and P < 0.01), GSE53819 (log 2 (fold change) >1 and P < 0.01), and GSE61218 (log 2 (fold change) >1 and P < 0.01). Right: Venn diagram illustrating the intersection of CSPs that are upregulated in tumor samples with high hypoxia scores of the GSE102349 cohort (log 2 (fold change) >10 and P < 0.01). c Distribution of TfR1 mRNA abundance in tumor and normal samples from different cohorts: GSE12452 (normal, n = 10; tumor, n = 31), GSE53819 (normal, n = 18; tumor, n = 18), and GSE61218 (normal, n = 6; tumor, n = 10). d Distribution of TFRC mRNA abundance in tumor samples from the GSE102349 cohort ( n = 113) with high or low hypoxia scores. e Representative images of IHC staining showing TfR1 protein expression in clinical primary NPC tissues and NNE tissues collected from multiple patients. Scale bar, 50 μm. f Distribution of TfR1 IHC staining scores in NPC ( n = 174) and NNE ( n = 98) tissues. g Distribution of TfR1 IHC staining scores in NPC and matched adjacent non-cancerous tissues ( n = 117). h IF staining analysis in NPC tissues depicting the co-expression of HIF-1α and TfR1. Scale bar, 50 μm. i Spearman correlation between HIF-1α expression and TfR1 expression based on h ( n = 40 random regions from different tissues). The box plots in c , d , and f show the median ±1 quartile, with whiskers extending to the minimum or maximum values within 1.5 times the interquartile range from the box boundaries. Mann–Whitney test in c , d , and f and Wilcoxon matched-pairs signed rank test in g were used to calculate P values. Source data are provided as a Source Data file.

    Journal: Nature Communications

    Article Title: Hypoxia-tropic delivery of nanozymes targeting transferrin receptor 1 for nasopharyngeal carcinoma radiotherapy sensitization

    doi: 10.1038/s41467-025-56134-z

    Figure Lengend Snippet: a Schematic representation of CSPs upregulated in hypoxic NPC identified through DGE analysis among a total of 1442 CSPs. b Left: Venn diagram illustrating the intersection of CSPs upregulated in tumor samples of the three cohorts: GSE12452 (log 2 (fold change) >1 and P < 0.01), GSE53819 (log 2 (fold change) >1 and P < 0.01), and GSE61218 (log 2 (fold change) >1 and P < 0.01). Right: Venn diagram illustrating the intersection of CSPs that are upregulated in tumor samples with high hypoxia scores of the GSE102349 cohort (log 2 (fold change) >10 and P < 0.01). c Distribution of TfR1 mRNA abundance in tumor and normal samples from different cohorts: GSE12452 (normal, n = 10; tumor, n = 31), GSE53819 (normal, n = 18; tumor, n = 18), and GSE61218 (normal, n = 6; tumor, n = 10). d Distribution of TFRC mRNA abundance in tumor samples from the GSE102349 cohort ( n = 113) with high or low hypoxia scores. e Representative images of IHC staining showing TfR1 protein expression in clinical primary NPC tissues and NNE tissues collected from multiple patients. Scale bar, 50 μm. f Distribution of TfR1 IHC staining scores in NPC ( n = 174) and NNE ( n = 98) tissues. g Distribution of TfR1 IHC staining scores in NPC and matched adjacent non-cancerous tissues ( n = 117). h IF staining analysis in NPC tissues depicting the co-expression of HIF-1α and TfR1. Scale bar, 50 μm. i Spearman correlation between HIF-1α expression and TfR1 expression based on h ( n = 40 random regions from different tissues). The box plots in c , d , and f show the median ±1 quartile, with whiskers extending to the minimum or maximum values within 1.5 times the interquartile range from the box boundaries. Mann–Whitney test in c , d , and f and Wilcoxon matched-pairs signed rank test in g were used to calculate P values. Source data are provided as a Source Data file.

    Article Snippet: Subsequently, 300 µL of 5% skimmed milk was added to each well and incubated at 37 °C for 2 h. After further washing, each well was incubated with 100 µL of TfR1 solution (SinoBiological, catalog no. 11020-H07H, 2 µg/mL) at 37 °C for 2 h. After another round of washing, each well was incubated with 100 µL of anti-TfR1 antibody (SinoBiological, catalog no. 11020-MM02, 1 µg/mL) at 37 °C for 2 h. Following additional washes, 100 µL of HRP-conjugated anti-mouse IgG (GE Healthcare, catalog no. NA931, 1:5000) was added and incubated at 37 °C for 1 h. Finally, 100 µL of one-component TMB chromogenic substrate (InnoReagents, catalog no. TMB-S-004) was added to each well.

    Techniques: Immunohistochemistry, Expressing, Staining, MANN-WHITNEY

    Lipid microdomains localization of LRP8 and phospho-Dab2 following triggering with anti-β2-GPI antibodies. ( A ). Sucrose gradient fractions obtained from HUVECs, treated with affinity-purified anti-β2-GPI antibodies for 45 min, or left untreated, were analyzed with Western Blot using anti-LRP8 mAb, anti-phospho-Dab2 (ser24) Ab, anti-CD71 mAb or anti-flotillin Ab. Right panel. Bar graphs of densitometric analysis. The columns indicate the percentage distribution across the gel of raft fractions 4-5-6 (Triton X-100-insoluble fractions) and 9-10-11 (Tri-ton X-100-soluble fractions), as detected with scanning densitometric analysis. Results represent the mean ± SD from 3 independent experiments. **** p < 0.0001. ( B ). Fractions (4–6) (insoluble Triton X-100 fractions) and fractions 9–11 (soluble Triton X-100 fractions) were spotted onto nitrocellulose strips and analyzed via dot blot using Cholera Toxin (CTx) B Subunit-Peroxidase.

    Journal: Biomedicines

    Article Title: Role of Lipid Rafts on LRP8 Signaling Triggered by Anti-β2-GPI Antibodies in Endothelial Cells

    doi: 10.3390/biomedicines11123135

    Figure Lengend Snippet: Lipid microdomains localization of LRP8 and phospho-Dab2 following triggering with anti-β2-GPI antibodies. ( A ). Sucrose gradient fractions obtained from HUVECs, treated with affinity-purified anti-β2-GPI antibodies for 45 min, or left untreated, were analyzed with Western Blot using anti-LRP8 mAb, anti-phospho-Dab2 (ser24) Ab, anti-CD71 mAb or anti-flotillin Ab. Right panel. Bar graphs of densitometric analysis. The columns indicate the percentage distribution across the gel of raft fractions 4-5-6 (Triton X-100-insoluble fractions) and 9-10-11 (Tri-ton X-100-soluble fractions), as detected with scanning densitometric analysis. Results represent the mean ± SD from 3 independent experiments. **** p < 0.0001. ( B ). Fractions (4–6) (insoluble Triton X-100 fractions) and fractions 9–11 (soluble Triton X-100 fractions) were spotted onto nitrocellulose strips and analyzed via dot blot using Cholera Toxin (CTx) B Subunit-Peroxidase.

    Article Snippet: The proteins were electrophoretically transferred onto PVDF membranes (Bio-Rad), blocked with 1% BSA in TBS-T (Bio-Rad) and probed with mouse anti-LRP8 mAb (Invitrogen), rabbit anti-phospho-Dab2 (ser24) Ab (Bioss Antibodies), mouse anti-Transferrin receptor (CD71) mAb (Abcam), and goat anti-flotillin Ab (Abcam).

    Techniques: Affinity Purification, Western Blot, Dot Blot

    Figure 6. Morphology of BFA-sensitive compartments of R1 and R2 cells. Cells of the indicated cell lines were treated with 2.5 mg/ ml (A) or 5 mg/ml (B, C) BFA for 30 minutes, fixed and processed for the immunofluorescent detection of GM130 (A), TGN46 (B), or the transferrin receptor (C). The nuclei were stained with DAPI. Represen- tative confocal images are presented. Bar, 20 mm. doi:10.1371/journal.pone.0074491.g006

    Journal: PloS one

    Article Title: Hepatitis C virus replication and Golgi function in brefeldin a-resistant hepatoma-derived cells.

    doi: 10.1371/journal.pone.0074491

    Figure Lengend Snippet: Figure 6. Morphology of BFA-sensitive compartments of R1 and R2 cells. Cells of the indicated cell lines were treated with 2.5 mg/ ml (A) or 5 mg/ml (B, C) BFA for 30 minutes, fixed and processed for the immunofluorescent detection of GM130 (A), TGN46 (B), or the transferrin receptor (C). The nuclei were stained with DAPI. Represen- tative confocal images are presented. Bar, 20 mm. doi:10.1371/journal.pone.0074491.g006

    Article Snippet: Mouse anti-CD71 (transferrin receptor) MAb was purchased from Santa Cruz Biotechnology.

    Techniques: Staining