mouse anti human cd3ζ Search Results


anti cd3ζ mab  (Becton Dickinson)
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Becton Dickinson anti cd3ζ mab
Construction of the anti‐epidermal growth factor receptor variant III (EGFRvIII) chimeric antigen receptor. The construct was composed of the VH and VL regions of the anti‐EGFRvIII mAb joined by a flexible linker, a membrane‐proximal hinge region of human CD8α, and the transmembrane and cytoplasmic regions of the human <t>CD3ζ</t> chain.
Anti Cd3ζ Mab, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Construction of the anti‐epidermal growth factor receptor variant III (EGFRvIII) chimeric antigen receptor. The construct was composed of the VH and VL regions of the anti‐EGFRvIII mAb joined by a flexible linker, a membrane‐proximal hinge region of human CD8α, and the transmembrane and cytoplasmic regions of the human CD3ζ chain.

Journal: Cancer Science

Article Title: Retrovirally engineered T‐cell‐based immunotherapy targeting type III variant epidermal growth factor receptor, a glioma‐associated antigen

doi: 10.1111/j.1349-7006.2010.01734.x

Figure Lengend Snippet: Construction of the anti‐epidermal growth factor receptor variant III (EGFRvIII) chimeric antigen receptor. The construct was composed of the VH and VL regions of the anti‐EGFRvIII mAb joined by a flexible linker, a membrane‐proximal hinge region of human CD8α, and the transmembrane and cytoplasmic regions of the human CD3ζ chain.

Article Snippet: The membrane was probed with anti‐CD3ζ mAb (1:2000; BD Bioscience, Franklin Lakes, NJ, USA) and a horseradish peroxidase‐conjugated goat anti‐mouse Ab (1:3000), followed by visualization with enhanced chemiluminescence (GE Healthcare Japan, Osaka, Japan).

Techniques: Variant Assay, Construct, Membrane

Primers used in the present study

Journal: Cancer Science

Article Title: Retrovirally engineered T‐cell‐based immunotherapy targeting type III variant epidermal growth factor receptor, a glioma‐associated antigen

doi: 10.1111/j.1349-7006.2010.01734.x

Figure Lengend Snippet: Primers used in the present study

Article Snippet: The membrane was probed with anti‐CD3ζ mAb (1:2000; BD Bioscience, Franklin Lakes, NJ, USA) and a horseradish peroxidase‐conjugated goat anti‐mouse Ab (1:3000), followed by visualization with enhanced chemiluminescence (GE Healthcare Japan, Osaka, Japan).

Techniques:

The anti‐epidermal growth factor receptor variant III (EGFRvIII)‐CD3ζ chimeric antigen receptor (CAR) expression, cell surface trafficking and 3C10 binding on the surface of Jurkat cells. (A) Detection of anti‐EGFRvIII‐CD3ζ CAR expression in whole‐cell lysate derived from Jurkat cell transfectants by reducing and nonreducing western blotting analysis with a mAb specific for the human CD3ζ chain. The lower band (16 kDa) is the endogenous CD3ζ chain (white arrow), and the upper band (32 kDa) is its homodimer (black arrow). The anti‐EGFRvIII‐CD3ζ CAR was detected at the expected molecular weight of 50 kDa (white arrowhead). The anti‐EGFRvIII‐CD3ζ CAR homodimer was detected at 100 kDa (black arrowhead). C, control cell; T, transduced cells. (B) Jurkat cells were stained with biotin‐conjugated Pep3 and streptavidin‐FITC. Expression was not detected in the non‐transduced cells (black line). Data are representative of three independent experiments.

Journal: Cancer Science

Article Title: Retrovirally engineered T‐cell‐based immunotherapy targeting type III variant epidermal growth factor receptor, a glioma‐associated antigen

doi: 10.1111/j.1349-7006.2010.01734.x

Figure Lengend Snippet: The anti‐epidermal growth factor receptor variant III (EGFRvIII)‐CD3ζ chimeric antigen receptor (CAR) expression, cell surface trafficking and 3C10 binding on the surface of Jurkat cells. (A) Detection of anti‐EGFRvIII‐CD3ζ CAR expression in whole‐cell lysate derived from Jurkat cell transfectants by reducing and nonreducing western blotting analysis with a mAb specific for the human CD3ζ chain. The lower band (16 kDa) is the endogenous CD3ζ chain (white arrow), and the upper band (32 kDa) is its homodimer (black arrow). The anti‐EGFRvIII‐CD3ζ CAR was detected at the expected molecular weight of 50 kDa (white arrowhead). The anti‐EGFRvIII‐CD3ζ CAR homodimer was detected at 100 kDa (black arrowhead). C, control cell; T, transduced cells. (B) Jurkat cells were stained with biotin‐conjugated Pep3 and streptavidin‐FITC. Expression was not detected in the non‐transduced cells (black line). Data are representative of three independent experiments.

Article Snippet: The membrane was probed with anti‐CD3ζ mAb (1:2000; BD Bioscience, Franklin Lakes, NJ, USA) and a horseradish peroxidase‐conjugated goat anti‐mouse Ab (1:3000), followed by visualization with enhanced chemiluminescence (GE Healthcare Japan, Osaka, Japan).

Techniques: Variant Assay, Expressing, Binding Assay, Derivative Assay, Western Blot, Molecular Weight, Staining