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function-blocking monoclonal antibody against α ν β 3 (lm609)  (Merck & Co)

 
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    Structured Review

    Merck & Co function-blocking monoclonal antibody against α ν β 3 (lm609)
    Ligand binding to <t>α</t> <t>ν</t> β 3 integrin activates cMet and mTORC1 in endothelial cells. Serum-starved HUVEC were stimulated with PTN (100 ng/mL), <t>LM609</t> (10 ng/mL), crizotinib (1 μM) or combinations, for 10 min in A, C, and D and 2 h in B. ( A , C ) Representative Western blot images of phosphorylated and total S6K1 and 4EBP1 in HUVEC. The bands were quantified, and the results are presented as the mean ± standard deviation of the % ratio of phosphorylated to total protein compared to the corresponding control (cells incubated with 10 ng/mL IgG, considered 100%). The bullets on the graphs indicate independent assays. ( B ) Representative Western blot images of the newly synthesized peptides labeled with puromycin from total cell lysates from serum-starved HUVEC treated with the tested agents as shown. Puromycin was added for the last 10 min of incubation. Beta (β)-actin was used as a loading control. Results are expressed as the mean ± standard deviation (n = 3) of the % ratio of puromycin incorporation (puromycilation) compared to the control (cells incubated with 10 ng/mL IgG, considered 100%). ( D ) Representative confocal microscopy images and quantification from PLA assay of the tyrosine phosphorylation sites of cMet (red dots) in serum-starved HUVEC treated with IgG or LM609. Nuclei stained with Draq5 are shown in blue. Scale bars correspond to 10 μm. Box plots indicate the median, mean, and range of detected signals (8–10 image fields with 4–8 cells per image, per sample, n = 3).
    Function Blocking Monoclonal Antibody Against α ν β 3 (Lm609), supplied by Merck & Co, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/function-blocking monoclonal antibody against α ν β 3 (lm609)/product/Merck & Co
    Average 90 stars, based on 1 article reviews
    function-blocking monoclonal antibody against α ν β 3 (lm609) - by Bioz Stars, 2026-03
    90/100 stars

    Images

    1) Product Images from "Pleiotrophin Activates cMet- and mTORC1-Dependent Protein Synthesis through PTPRZ1—The Role of α ν β 3 Integrin"

    Article Title: Pleiotrophin Activates cMet- and mTORC1-Dependent Protein Synthesis through PTPRZ1—The Role of α ν β 3 Integrin

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms251910839

    Ligand binding to α ν β 3 integrin activates cMet and mTORC1 in endothelial cells. Serum-starved HUVEC were stimulated with PTN (100 ng/mL), LM609 (10 ng/mL), crizotinib (1 μM) or combinations, for 10 min in A, C, and D and 2 h in B. ( A , C ) Representative Western blot images of phosphorylated and total S6K1 and 4EBP1 in HUVEC. The bands were quantified, and the results are presented as the mean ± standard deviation of the % ratio of phosphorylated to total protein compared to the corresponding control (cells incubated with 10 ng/mL IgG, considered 100%). The bullets on the graphs indicate independent assays. ( B ) Representative Western blot images of the newly synthesized peptides labeled with puromycin from total cell lysates from serum-starved HUVEC treated with the tested agents as shown. Puromycin was added for the last 10 min of incubation. Beta (β)-actin was used as a loading control. Results are expressed as the mean ± standard deviation (n = 3) of the % ratio of puromycin incorporation (puromycilation) compared to the control (cells incubated with 10 ng/mL IgG, considered 100%). ( D ) Representative confocal microscopy images and quantification from PLA assay of the tyrosine phosphorylation sites of cMet (red dots) in serum-starved HUVEC treated with IgG or LM609. Nuclei stained with Draq5 are shown in blue. Scale bars correspond to 10 μm. Box plots indicate the median, mean, and range of detected signals (8–10 image fields with 4–8 cells per image, per sample, n = 3).
    Figure Legend Snippet: Ligand binding to α ν β 3 integrin activates cMet and mTORC1 in endothelial cells. Serum-starved HUVEC were stimulated with PTN (100 ng/mL), LM609 (10 ng/mL), crizotinib (1 μM) or combinations, for 10 min in A, C, and D and 2 h in B. ( A , C ) Representative Western blot images of phosphorylated and total S6K1 and 4EBP1 in HUVEC. The bands were quantified, and the results are presented as the mean ± standard deviation of the % ratio of phosphorylated to total protein compared to the corresponding control (cells incubated with 10 ng/mL IgG, considered 100%). The bullets on the graphs indicate independent assays. ( B ) Representative Western blot images of the newly synthesized peptides labeled with puromycin from total cell lysates from serum-starved HUVEC treated with the tested agents as shown. Puromycin was added for the last 10 min of incubation. Beta (β)-actin was used as a loading control. Results are expressed as the mean ± standard deviation (n = 3) of the % ratio of puromycin incorporation (puromycilation) compared to the control (cells incubated with 10 ng/mL IgG, considered 100%). ( D ) Representative confocal microscopy images and quantification from PLA assay of the tyrosine phosphorylation sites of cMet (red dots) in serum-starved HUVEC treated with IgG or LM609. Nuclei stained with Draq5 are shown in blue. Scale bars correspond to 10 μm. Box plots indicate the median, mean, and range of detected signals (8–10 image fields with 4–8 cells per image, per sample, n = 3).

    Techniques Used: Ligand Binding Assay, Western Blot, Standard Deviation, Control, Incubation, Synthesized, Labeling, Confocal Microscopy, Staining

    A schematic representation of the PTN/PTPRZ1 signaling pathway that includes α ν β integrin and leads to cMet and mTORC1 activation and enhanced protein synthesis. ( A ) PTN binds to PTPRZ1 and leads to cMet activation, as previously shown . PTPRZ1 deletion is also known to lead to cMet activation . cMet activates mTORC1, which results in enhanced protein synthesis and cell migration. ( B ) LM609 and PTN 112–136 bind to α ν β integrin and activate cMet, mTORC1, and protein synthesis. The arrows signify up-regulation.
    Figure Legend Snippet: A schematic representation of the PTN/PTPRZ1 signaling pathway that includes α ν β integrin and leads to cMet and mTORC1 activation and enhanced protein synthesis. ( A ) PTN binds to PTPRZ1 and leads to cMet activation, as previously shown . PTPRZ1 deletion is also known to lead to cMet activation . cMet activates mTORC1, which results in enhanced protein synthesis and cell migration. ( B ) LM609 and PTN 112–136 bind to α ν β integrin and activate cMet, mTORC1, and protein synthesis. The arrows signify up-regulation.

    Techniques Used: Activation Assay, Migration



    Similar Products

    function-blocking monoclonal antibody against α ν β 3 (lm609)  (Merck & Co)
    90
    Merck & Co function-blocking monoclonal antibody against α ν β 3 (lm609)
    Ligand binding to <t>α</t> <t>ν</t> β 3 integrin activates cMet and mTORC1 in endothelial cells. Serum-starved HUVEC were stimulated with PTN (100 ng/mL), <t>LM609</t> (10 ng/mL), crizotinib (1 μM) or combinations, for 10 min in A, C, and D and 2 h in B. ( A , C ) Representative Western blot images of phosphorylated and total S6K1 and 4EBP1 in HUVEC. The bands were quantified, and the results are presented as the mean ± standard deviation of the % ratio of phosphorylated to total protein compared to the corresponding control (cells incubated with 10 ng/mL IgG, considered 100%). The bullets on the graphs indicate independent assays. ( B ) Representative Western blot images of the newly synthesized peptides labeled with puromycin from total cell lysates from serum-starved HUVEC treated with the tested agents as shown. Puromycin was added for the last 10 min of incubation. Beta (β)-actin was used as a loading control. Results are expressed as the mean ± standard deviation (n = 3) of the % ratio of puromycin incorporation (puromycilation) compared to the control (cells incubated with 10 ng/mL IgG, considered 100%). ( D ) Representative confocal microscopy images and quantification from PLA assay of the tyrosine phosphorylation sites of cMet (red dots) in serum-starved HUVEC treated with IgG or LM609. Nuclei stained with Draq5 are shown in blue. Scale bars correspond to 10 μm. Box plots indicate the median, mean, and range of detected signals (8–10 image fields with 4–8 cells per image, per sample, n = 3).
    Function Blocking Monoclonal Antibody Against α ν β 3 (Lm609), supplied by Merck & Co, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/function-blocking monoclonal antibody against α ν β 3 (lm609)/product/Merck & Co
    Average 90 stars, based on 1 article reviews
    function-blocking monoclonal antibody against α ν β 3 (lm609) - by Bioz Stars, 2026-03
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    Ligand binding to α ν β 3 integrin activates cMet and mTORC1 in endothelial cells. Serum-starved HUVEC were stimulated with PTN (100 ng/mL), LM609 (10 ng/mL), crizotinib (1 μM) or combinations, for 10 min in A, C, and D and 2 h in B. ( A , C ) Representative Western blot images of phosphorylated and total S6K1 and 4EBP1 in HUVEC. The bands were quantified, and the results are presented as the mean ± standard deviation of the % ratio of phosphorylated to total protein compared to the corresponding control (cells incubated with 10 ng/mL IgG, considered 100%). The bullets on the graphs indicate independent assays. ( B ) Representative Western blot images of the newly synthesized peptides labeled with puromycin from total cell lysates from serum-starved HUVEC treated with the tested agents as shown. Puromycin was added for the last 10 min of incubation. Beta (β)-actin was used as a loading control. Results are expressed as the mean ± standard deviation (n = 3) of the % ratio of puromycin incorporation (puromycilation) compared to the control (cells incubated with 10 ng/mL IgG, considered 100%). ( D ) Representative confocal microscopy images and quantification from PLA assay of the tyrosine phosphorylation sites of cMet (red dots) in serum-starved HUVEC treated with IgG or LM609. Nuclei stained with Draq5 are shown in blue. Scale bars correspond to 10 μm. Box plots indicate the median, mean, and range of detected signals (8–10 image fields with 4–8 cells per image, per sample, n = 3).

    Journal: International Journal of Molecular Sciences

    Article Title: Pleiotrophin Activates cMet- and mTORC1-Dependent Protein Synthesis through PTPRZ1—The Role of α ν β 3 Integrin

    doi: 10.3390/ijms251910839

    Figure Lengend Snippet: Ligand binding to α ν β 3 integrin activates cMet and mTORC1 in endothelial cells. Serum-starved HUVEC were stimulated with PTN (100 ng/mL), LM609 (10 ng/mL), crizotinib (1 μM) or combinations, for 10 min in A, C, and D and 2 h in B. ( A , C ) Representative Western blot images of phosphorylated and total S6K1 and 4EBP1 in HUVEC. The bands were quantified, and the results are presented as the mean ± standard deviation of the % ratio of phosphorylated to total protein compared to the corresponding control (cells incubated with 10 ng/mL IgG, considered 100%). The bullets on the graphs indicate independent assays. ( B ) Representative Western blot images of the newly synthesized peptides labeled with puromycin from total cell lysates from serum-starved HUVEC treated with the tested agents as shown. Puromycin was added for the last 10 min of incubation. Beta (β)-actin was used as a loading control. Results are expressed as the mean ± standard deviation (n = 3) of the % ratio of puromycin incorporation (puromycilation) compared to the control (cells incubated with 10 ng/mL IgG, considered 100%). ( D ) Representative confocal microscopy images and quantification from PLA assay of the tyrosine phosphorylation sites of cMet (red dots) in serum-starved HUVEC treated with IgG or LM609. Nuclei stained with Draq5 are shown in blue. Scale bars correspond to 10 μm. Box plots indicate the median, mean, and range of detected signals (8–10 image fields with 4–8 cells per image, per sample, n = 3).

    Article Snippet: Function-blocking monoclonal antibody against α ν β 3 (LM609) was from Merck (#MAB1976, Merck KGaA, Darmstadt, Germany).

    Techniques: Ligand Binding Assay, Western Blot, Standard Deviation, Control, Incubation, Synthesized, Labeling, Confocal Microscopy, Staining

    A schematic representation of the PTN/PTPRZ1 signaling pathway that includes α ν β integrin and leads to cMet and mTORC1 activation and enhanced protein synthesis. ( A ) PTN binds to PTPRZ1 and leads to cMet activation, as previously shown . PTPRZ1 deletion is also known to lead to cMet activation . cMet activates mTORC1, which results in enhanced protein synthesis and cell migration. ( B ) LM609 and PTN 112–136 bind to α ν β integrin and activate cMet, mTORC1, and protein synthesis. The arrows signify up-regulation.

    Journal: International Journal of Molecular Sciences

    Article Title: Pleiotrophin Activates cMet- and mTORC1-Dependent Protein Synthesis through PTPRZ1—The Role of α ν β 3 Integrin

    doi: 10.3390/ijms251910839

    Figure Lengend Snippet: A schematic representation of the PTN/PTPRZ1 signaling pathway that includes α ν β integrin and leads to cMet and mTORC1 activation and enhanced protein synthesis. ( A ) PTN binds to PTPRZ1 and leads to cMet activation, as previously shown . PTPRZ1 deletion is also known to lead to cMet activation . cMet activates mTORC1, which results in enhanced protein synthesis and cell migration. ( B ) LM609 and PTN 112–136 bind to α ν β integrin and activate cMet, mTORC1, and protein synthesis. The arrows signify up-regulation.

    Article Snippet: Function-blocking monoclonal antibody against α ν β 3 (LM609) was from Merck (#MAB1976, Merck KGaA, Darmstadt, Germany).

    Techniques: Activation Assay, Migration