anti mouse cd96  (Bio X Cell)

Journal: Immunity

Article Title: T cell-derived interleukin-22 drives the expression of CD155 by cancer cells to suppress NK cell function and promote metastasis

doi: 10.1016/j.immuni.2022.12.010

Figure Lengend Snippet: CD226 signaling is indispensable for IFNγ production from NK cells (A) Intravenous mouse model of 4T1 control or Pvr + metastasis in Il22 −/− mice. Animals received injections of anti-CD226 blocking antibody (420.1, 200 μg per mouse) or control i.p. on days 0, 3, and 14. (B) Numbers of macroscopic lung metastases and colonies in metastasis assay. (C) IFNγ-producing NK cells in the lungs evaluated by flow cytometry. Data presented as means ± SEM; p values <0.05 were considered significant by the Mann-Whitney U test. (D) Representative dot plots depict CD226 low, medium, and high NK cells. Frequency of IFNγ+ cells among NK cell populations (n = 5–6). Numbers represent the frequency of the parent gate. Data presented as means ± SEM; p values <0.05 were considered significant by the two-way ANOVA. (E) Intravenous mouse model of 4T1 control or Pvr + lung metastasis in Il22 −/− mice. Animals received injections of anti-TIGIT agonist antibody (1G9, 250 μg per mouse), anti-CD96 blocking antibody (3.3, 250 μg per mouse), or control i.p. on days 0, 3, and 14. (F) Numbers of macroscopic lung metastases. (G) IFNγ-producing NK and CD8 + T cells in the lungs were evaluated by flow cytometry. Numbers represent the frequency of the parent gate. Data presented as means ± SEM; p values <0.05 were considered significant by unpaired t- test (n = 5–6).

Article Snippet: InVivoMAb anti-mouse CD96 (3.3) , BioXCell , Cat# BE0337; RRID: AB_2894757.

Techniques: Control, Blocking Assay, Flow Cytometry, MANN-WHITNEY

Journal: Immunity

Article Title: T cell-derived interleukin-22 drives the expression of CD155 by cancer cells to suppress NK cell function and promote metastasis

doi: 10.1016/j.immuni.2022.12.010

Figure Lengend Snippet:

Article Snippet: InVivoMAb anti-mouse CD96 (3.3) , BioXCell , Cat# BE0337; RRID: AB_2894757.

Techniques: Purification, Control, Virus, Recombinant, Red Blood Cell Lysis, Transfection, Flow Cytometry, DNA Extraction, Gel Extraction, Plasmid Preparation, cDNA Synthesis, Cell Differentiation, Staining, Cell Isolation, Conjugation Assay, Sequencing, CRISPR, Retroviral, Software

Journal: mAbs

Article Title: Antibody blockade of CD96 by distinct molecular mechanisms

doi: 10.1080/19420862.2021.1979800

Figure Lengend Snippet: SEC-MALS of CD96 and CD155 proteins and complexes

Article Snippet: Following selection, the cells were checked by fluorescence-activated single-cell sorting for expression using an anti-mouse CD96-PE antibody (Ebioscience #12-0960-80).

Techniques:

Journal: mAbs

Article Title: Antibody blockade of CD96 by distinct molecular mechanisms

doi: 10.1080/19420862.2021.1979800

Figure Lengend Snippet: SPR-binding kinetics and ligand blocking activity of anti-mouse CD96 antibodies

Article Snippet: Following selection, the cells were checked by fluorescence-activated single-cell sorting for expression using an anti-mouse CD96-PE antibody (Ebioscience #12-0960-80).

Techniques: Blocking Assay, Activity Assay

Journal: mAbs

Article Title: Antibody blockade of CD96 by distinct molecular mechanisms

doi: 10.1080/19420862.2021.1979800

Figure Lengend Snippet: Binding and ligand blocking of anti-mouse CD96 bivalent (filled symbols) and monovalent (open symbols) IgGs on cells. (a) Binding of antibodies to mouse CD96-expressing CHO cells (mean ± SD, n = 3; independent experiments performed three times). (b) Antibody blocking of mouse CD155 tetramers (mean ± SD, n = 2, independent experiments performed three times). All antibodies were expressed in the mIgG1-D265A isotype

Article Snippet: Following selection, the cells were checked by fluorescence-activated single-cell sorting for expression using an anti-mouse CD96-PE antibody (Ebioscience #12-0960-80).

Techniques: Binding Assay, Blocking Assay, Expressing

Journal: mAbs

Article Title: Antibody blockade of CD96 by distinct molecular mechanisms

doi: 10.1080/19420862.2021.1979800

Figure Lengend Snippet: SEC-MALS of antibody-CD96 complexes. The individual Fab and IgG molecular weights are approximately 48 kDa and 143 kDa, respectively

Article Snippet: Following selection, the cells were checked by fluorescence-activated single-cell sorting for expression using an anti-mouse CD96-PE antibody (Ebioscience #12-0960-80).

Techniques:

Journal: mAbs

Article Title: Antibody blockade of CD96 by distinct molecular mechanisms

doi: 10.1080/19420862.2021.1979800

Figure Lengend Snippet: Cartoon schematic of binding assemblies of CD155 ligand, Fabs, and IgGs to mouse CD96 reveals two distinct antibody blocking mechanisms

Article Snippet: Following selection, the cells were checked by fluorescence-activated single-cell sorting for expression using an anti-mouse CD96-PE antibody (Ebioscience #12-0960-80).

Techniques: Binding Assay, Blocking Assay

Journal: mAbs

Article Title: Antibody blockade of CD96 by distinct molecular mechanisms

doi: 10.1080/19420862.2021.1979800

Figure Lengend Snippet: Antibodies mCD96-A and mCD96-B bind distinct epitopes on monomeric or dimeric mouse CD96 to block CD155. The crystal structures of CD96 in complex with (a) CD155 ligand, (b) mCD96-A Fab, and (c) mCD96-B Fab. The complexes are aligned onto CD96, represented as a light gray surface. In the mCD96-B structure, the other protomer of CD96 that forms the dimer is shown as a dark gray surface. CD155, mCD96-A, and mCD96-B are colored as blue, red, or green cartoons, respectively. The CD96-CD155 complex is of the human orthologs from PDB ID 6ARQ. (d) Epitopes of CD155, mCD96-A, and the CD96 dimer interface are colored blue, red, or dark gray on the surface representation of CD96. Each CD96 protomer is aligned in the same orientation. Regions contacted by the mCD96-A heavy chain or light chain are colored red or light red, respectively. (e) Epitope of mCD96-B on the surface of the CD96 homodimer, with each protomer colored light or dark gray. Regions contacted by the mCD96-B heavy chain or light chain are colored green or light green, respectively

Article Snippet: Following selection, the cells were checked by fluorescence-activated single-cell sorting for expression using an anti-mouse CD96-PE antibody (Ebioscience #12-0960-80).

Techniques: Blocking Assay

Journal: mAbs

Article Title: Antibody blockade of CD96 by distinct molecular mechanisms

doi: 10.1080/19420862.2021.1979800

Figure Lengend Snippet: Comparisons of the human and mouse CD96 D1 domains. (a) Structural alignment of the D1 domains of the human CD96-CD155 heterodimeric complex (PDB ID 6ARQ) and the mouse CD96 homodimer from the mCD96-B complex. (b) Sequence alignment of the human and mouse CD96 D1 domains. Interacting residues to human CD96 by CD155 or of the mouse CD96 homodimer conserved across both protomers were calculated by Areaimol and are highlighted blue or gray, respectively

Article Snippet: Following selection, the cells were checked by fluorescence-activated single-cell sorting for expression using an anti-mouse CD96-PE antibody (Ebioscience #12-0960-80).

Techniques: Sequencing

Journal: mAbs

Article Title: Antibody blockade of CD96 by distinct molecular mechanisms

doi: 10.1080/19420862.2021.1979800

Figure Lengend Snippet: CD96 molecular recognition similarities at the lock-and-key interface. The (a) CD155, (b) mCD96-A, (c) and mouse CD96 dimer complexes are represented as cartoons and the residues of the ligand, mCD96-A, and opposing CD96 protomer that form the key are shown as sticks and are colored blue, red, or dark gray, respectively. The CD96 lock and Y78 residues in each of the complexes are shown as sticks and are colored light gray

Article Snippet: Following selection, the cells were checked by fluorescence-activated single-cell sorting for expression using an anti-mouse CD96-PE antibody (Ebioscience #12-0960-80).

Techniques: