Fig. 4.
Fig. 4. Inhibition of induction of apoptosis in K562 cells and in CCRF-CEM cells by anti-β2m MoAb. (A) β2m-induced apoptosis in K562 cells was suppressed by the addition of 100 μg anti-β2m MoAb derived from hybridoma clone NK2. Anti-β2m MoAbs (clone NK1 and NK3) were the negative controls at the same concentration. (B) β2m-induced apoptosis in CCRF-CEM cells was suppressed by preincubation with anti-β2m MoAb (clone NK2). Apoptotic cells were assayed by TUNEL. Data are expressed as the mean ± SE of 3 independent experiments. (C) The effects of anti-β2m MoAbs for the interaction of biotinilated β2m and the cell surface on CCRF-CEM cells were analyzed using FACS (dotted line, control; thin line, no additive of anti-β2m MoAb; thick line, additive of anti-β2m MoAb).

Inhibition of induction of apoptosis in K562 cells and in CCRF-CEM cells by anti-β2m MoAb. (A) β2m-induced apoptosis in K562 cells was suppressed by the addition of 100 μg anti-β2m MoAb derived from hybridoma clone NK2. Anti-β2m MoAbs (clone NK1 and NK3) were the negative controls at the same concentration. (B) β2m-induced apoptosis in CCRF-CEM cells was suppressed by preincubation with anti-β2m MoAb (clone NK2). Apoptotic cells were assayed by TUNEL. Data are expressed as the mean ± SE of 3 independent experiments. (C) The effects of anti-β2m MoAbs for the interaction of biotinilated β2m and the cell surface on CCRF-CEM cells were analyzed using FACS (dotted line, control; thin line, no additive of anti-β2m MoAb; thick line, additive of anti-β2m MoAb).

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