Fig. 10.
Fig. 10. Integrin-mediated adhesion to LN-10/11. / Cell adhesion assays of the myeloblastic cell line, KG1a, to LN-10/11 coated at a concentration of 5 μg/mL. In the control experiment, without any inhibitory factor, strong adhesion of the KG1a cells to LN-10/11 could be observed. Addition of an antiserum against LN-10/11 (diluted 1:100) completely abolished cell adhesion (anti–LN-10/11). Preincubation of KG1a cells with the β1 integrin antibody, 4B4 (diluted 1:50), for half an hour also inhibited cell binding to LN-10/11 (anti–β1 integrin). (Original magnification × 37.)

Integrin-mediated adhesion to LN-10/11.

Cell adhesion assays of the myeloblastic cell line, KG1a, to LN-10/11 coated at a concentration of 5 μg/mL. In the control experiment, without any inhibitory factor, strong adhesion of the KG1a cells to LN-10/11 could be observed. Addition of an antiserum against LN-10/11 (diluted 1:100) completely abolished cell adhesion (anti–LN-10/11). Preincubation of KG1a cells with the β1 integrin antibody, 4B4 (diluted 1:50), for half an hour also inhibited cell binding to LN-10/11 (anti–β1 integrin). (Original magnification × 37.)

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