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abx-ma1  (PDL BioPharma)

 
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    PDL BioPharma abx-ma1
    Abx Ma1, supplied by PDL BioPharma, 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/product/abx-ma1/abx+ma1/us09441034-1526-80-75
    Average 90 stars, based on 1 article reviews
    abx-ma1 - by Bioz Stars, 2026-10
    90/100 stars

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    other:

    Article Title: Compositions and methods for inhibiting PDGFRβ and VEGF-A
    Article Snippet: TABLE 8 Monoclonal Antibody Therapies for Use in Combination with PDGFRβ and/or VEGF- A Antagonists Target Drug Name Clinical Indication Company TRAIL-R1 HGS-ETR1 cancers HGS TRAIL-R2 HGS-ETR2 solid tumors HGS CD40 SGN40 MM Seattle Genetics HER2 Herceptin Breast cancer Genentech EGF-R ABX-EGF CRC, NSCLC, RCC Abgenix EGF-R EMD72000 solid tumors Merck EGF-R MDX-214 EGF-R-positive tumors Medarex EGF-R Erbitux CRC Imclone α5β3 integrin Vitaxin psoriasis, prostate cancer AME/Lilly CD152 CTLA-4 cancers Medarex CD49e Integrin α5 cancers Protein Design Labs MUC18 (TIM-like) ABX-MA1 melanoma TAG-72 Mucin Anatumomab cancers CD3 Ecromeximab melanoma Kyowa Hakko CD64 (Fc GR1) AntiCD64 cancers Medarex CEA CEA-Cide cancers Immunomedics EpCAM Panorex colorectal cancer Centocor Lewis-Y-Ag SGN15 cancers Seattle Genetics b. Tyrosine Kinase Inhibitors in Combination with PDGFRβ and/or VEGF-A Antagonist In some embodiments, a PDGFRβ and/or VEGF-A antagonist as described herein is used in combination with a tyrosine kinase inhibitor.

    Article Title: Monoclonal antibodies that bind B7H6 and uses thereof
    Article Snippet: TABLE 6 Monoclonal Antibody Therapies for Use in Combination with Anti-B7H6 Antibodies or Antibody-drug Conjugates Clinical Target Drug Name Indication Company TRAIL-R1 HGS-ETR1 Cancers HGS TRAIL-R2 HGS-ETR2 solid tumors HGS CD40 SGN40 MM Seattle Genetics HER2 Herceptin Breast cancer Genentech EGF-R ABX-EGF CRC, NSCLC, Abgenix RCC EGF-R EMD72000 solid tumors Merck EGF-R MDX-214 EGF-R-positive Medarex tumors EGF-R Erbitux CRC Imclone α5β3 integrin Vitaxin psoriasis, AME/Lilly prostate cancer CD152 CTLA-4 Cancers Medarex CD49e Integrin α5 Cancers Protein Design Labs MUC18 (TIM-like) ABX-MA1 Melanoma TAG-72 Mucin Anatumomab Cancers CD3 Ecromeximab Melanoma Kyowa Hakko CD64 (Fc GR1) AntiCD64 Cancers Medarex CEA CEA-Cide Cancers Immunomedics EpCAM Panorex colorectal Centocor cancer Lewis-Y-Ag SGN15 Cancers Seattle Genetics b. Tyrosine Kinase Inhibitors In some embodiments, an anti-human-B7H6 monoclonal antibody or antibody-drug conjugate as described herein is used in combination with a tyrosine kinase inhibitor.



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    mOI-3, chOI-3 and <t>ABX-MA1</t> bind to CD146 expressed on human mesothelioma cancer cell lines. ( A ) and ( C ) Representative flow cytometry histograms comparing the binding of increasing concentrations, 0.001–10 µg of mOI-3 Alexa 488 and chOI-3 Alexa 488 to ( A ) MSTO-211H, and ( C ) NCI-H226 cells for 30 min at 4 °C. Unstained cells, mouse, and human isotype controls were used as negative controls. ( B ) and ( D ) relative median fluorescence intensity (rMFI) for all samples was calculated based on rMFI of isotype control cells for MSTO-211H and NCI-H226, respectively. A one-site binding model (Y = B max × X / (KD + X)) was used to analyze the data plotted as a hyperbolic curve (GraphPad Prism, La Jolla, USA). This analysis aimed to determine the apparent equilibrium dissociation constant (K D APP ) specific to cancer cell lines. For MSTO-211H, K D APP was 3.3 ± 0.3 nM and 9.2 ± 1.4 nM for chOI-3 and mOI-3 respectively. For NCI-H226, K D APP was 5.9 ± 1.3 nM and 11.4 ± 4.0 nM for chOI-3 and mOI-3 respectively. ( E ) MSTO-211H, and ( F ) NCI-H226 cells were stained with human unlabeled antibody ABX-MA1 and chOI-3 for 30 min at 4 °C. Following the incubation, goat anti-human Alexa 488 antibody was used for 30 min 4 °C. In all experiments, only MitoTracker Red CMXRos and DRAQ5 double positive cells were included in the analysis. Samples were collected using CytoFlex. Data are representative of at least two or three independent experiments.
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    mOI-3, chOI-3 and <t>ABX-MA1</t> bind to CD146 expressed on human mesothelioma cancer cell lines. ( A ) and ( C ) Representative flow cytometry histograms comparing the binding of increasing concentrations, 0.001–10 µg of mOI-3 Alexa 488 and chOI-3 Alexa 488 to ( A ) MSTO-211H, and ( C ) NCI-H226 cells for 30 min at 4 °C. Unstained cells, mouse, and human isotype controls were used as negative controls. ( B ) and ( D ) relative median fluorescence intensity (rMFI) for all samples was calculated based on rMFI of isotype control cells for MSTO-211H and NCI-H226, respectively. A one-site binding model (Y = B max × X / (KD + X)) was used to analyze the data plotted as a hyperbolic curve (GraphPad Prism, La Jolla, USA). This analysis aimed to determine the apparent equilibrium dissociation constant (K D APP ) specific to cancer cell lines. For MSTO-211H, K D APP was 3.3 ± 0.3 nM and 9.2 ± 1.4 nM for chOI-3 and mOI-3 respectively. For NCI-H226, K D APP was 5.9 ± 1.3 nM and 11.4 ± 4.0 nM for chOI-3 and mOI-3 respectively. ( E ) MSTO-211H, and ( F ) NCI-H226 cells were stained with human unlabeled antibody ABX-MA1 and chOI-3 for 30 min at 4 °C. Following the incubation, goat anti-human Alexa 488 antibody was used for 30 min 4 °C. In all experiments, only MitoTracker Red CMXRos and DRAQ5 double positive cells were included in the analysis. Samples were collected using CytoFlex. Data are representative of at least two or three independent experiments.
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    mOI-3, chOI-3 and <t>ABX-MA1</t> bind to CD146 expressed on human mesothelioma cancer cell lines. ( A ) and ( C ) Representative flow cytometry histograms comparing the binding of increasing concentrations, 0.001–10 µg of mOI-3 Alexa 488 and chOI-3 Alexa 488 to ( A ) MSTO-211H, and ( C ) NCI-H226 cells for 30 min at 4 °C. Unstained cells, mouse, and human isotype controls were used as negative controls. ( B ) and ( D ) relative median fluorescence intensity (rMFI) for all samples was calculated based on rMFI of isotype control cells for MSTO-211H and NCI-H226, respectively. A one-site binding model (Y = B max × X / (KD + X)) was used to analyze the data plotted as a hyperbolic curve (GraphPad Prism, La Jolla, USA). This analysis aimed to determine the apparent equilibrium dissociation constant (K D APP ) specific to cancer cell lines. For MSTO-211H, K D APP was 3.3 ± 0.3 nM and 9.2 ± 1.4 nM for chOI-3 and mOI-3 respectively. For NCI-H226, K D APP was 5.9 ± 1.3 nM and 11.4 ± 4.0 nM for chOI-3 and mOI-3 respectively. ( E ) MSTO-211H, and ( F ) NCI-H226 cells were stained with human unlabeled antibody ABX-MA1 and chOI-3 for 30 min at 4 °C. Following the incubation, goat anti-human Alexa 488 antibody was used for 30 min 4 °C. In all experiments, only MitoTracker Red CMXRos and DRAQ5 double positive cells were included in the analysis. Samples were collected using CytoFlex. Data are representative of at least two or three independent experiments.
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    Image Search Results


    mOI-3, chOI-3 and ABX-MA1 bind to CD146 expressed on human mesothelioma cancer cell lines. ( A ) and ( C ) Representative flow cytometry histograms comparing the binding of increasing concentrations, 0.001–10 µg of mOI-3 Alexa 488 and chOI-3 Alexa 488 to ( A ) MSTO-211H, and ( C ) NCI-H226 cells for 30 min at 4 °C. Unstained cells, mouse, and human isotype controls were used as negative controls. ( B ) and ( D ) relative median fluorescence intensity (rMFI) for all samples was calculated based on rMFI of isotype control cells for MSTO-211H and NCI-H226, respectively. A one-site binding model (Y = B max × X / (KD + X)) was used to analyze the data plotted as a hyperbolic curve (GraphPad Prism, La Jolla, USA). This analysis aimed to determine the apparent equilibrium dissociation constant (K D APP ) specific to cancer cell lines. For MSTO-211H, K D APP was 3.3 ± 0.3 nM and 9.2 ± 1.4 nM for chOI-3 and mOI-3 respectively. For NCI-H226, K D APP was 5.9 ± 1.3 nM and 11.4 ± 4.0 nM for chOI-3 and mOI-3 respectively. ( E ) MSTO-211H, and ( F ) NCI-H226 cells were stained with human unlabeled antibody ABX-MA1 and chOI-3 for 30 min at 4 °C. Following the incubation, goat anti-human Alexa 488 antibody was used for 30 min 4 °C. In all experiments, only MitoTracker Red CMXRos and DRAQ5 double positive cells were included in the analysis. Samples were collected using CytoFlex. Data are representative of at least two or three independent experiments.

    Journal: Scientific Reports

    Article Title: Antigen targeting and anti-tumor activity of a novel anti-CD146 212 Pb internalizing alpha-radioimmunoconjugate against malignant peritoneal mesothelioma

    doi: 10.1038/s41598-024-76778-z

    Figure Lengend Snippet: mOI-3, chOI-3 and ABX-MA1 bind to CD146 expressed on human mesothelioma cancer cell lines. ( A ) and ( C ) Representative flow cytometry histograms comparing the binding of increasing concentrations, 0.001–10 µg of mOI-3 Alexa 488 and chOI-3 Alexa 488 to ( A ) MSTO-211H, and ( C ) NCI-H226 cells for 30 min at 4 °C. Unstained cells, mouse, and human isotype controls were used as negative controls. ( B ) and ( D ) relative median fluorescence intensity (rMFI) for all samples was calculated based on rMFI of isotype control cells for MSTO-211H and NCI-H226, respectively. A one-site binding model (Y = B max × X / (KD + X)) was used to analyze the data plotted as a hyperbolic curve (GraphPad Prism, La Jolla, USA). This analysis aimed to determine the apparent equilibrium dissociation constant (K D APP ) specific to cancer cell lines. For MSTO-211H, K D APP was 3.3 ± 0.3 nM and 9.2 ± 1.4 nM for chOI-3 and mOI-3 respectively. For NCI-H226, K D APP was 5.9 ± 1.3 nM and 11.4 ± 4.0 nM for chOI-3 and mOI-3 respectively. ( E ) MSTO-211H, and ( F ) NCI-H226 cells were stained with human unlabeled antibody ABX-MA1 and chOI-3 for 30 min at 4 °C. Following the incubation, goat anti-human Alexa 488 antibody was used for 30 min 4 °C. In all experiments, only MitoTracker Red CMXRos and DRAQ5 double positive cells were included in the analysis. Samples were collected using CytoFlex. Data are representative of at least two or three independent experiments.

    Article Snippet: Anti-CD146 human mAb, ABX-MA1 was purchased from ProteoGenix (PX-TA1914, lot 110,620-A01, Schiltigheim, France).

    Techniques: Flow Cytometry, Binding Assay, Fluorescence, Control, Staining, Incubation