Fig. 3.
Fig. 3. Detection of HTK protein in cell lines by Western blotting. (A) Proteins were immunoprecipitated from lysates of UT-7, BaF3/HTK, and BaF3/vector cells with anti-HTK MoAb, 38-1E. The immunoprecipitates were separated by SDS-PAGE (10% polyacrylamide) under reducing conditions, transferred, and probed with anti-HTK PoAb (upper column). The membrane was reprobed with anti-HTK PoAb that had been incubated with a 50-fold excess molar of HTKex-Fc (lower column). (B) Proteins in the cell lysates of surface-biotinylated cell lines were immunoprecipitated with 38-1E. Immune complexes were separated by SDS-PAGE (10% polyacrylamide) under reducing conditions, transferred, and probed with HRP-conjugated streptavidin. The positions of the molecular mass markers (in kilodaltons) are indicated on the left.

Detection of HTK protein in cell lines by Western blotting. (A) Proteins were immunoprecipitated from lysates of UT-7, BaF3/HTK, and BaF3/vector cells with anti-HTK MoAb, 38-1E. The immunoprecipitates were separated by SDS-PAGE (10% polyacrylamide) under reducing conditions, transferred, and probed with anti-HTK PoAb (upper column). The membrane was reprobed with anti-HTK PoAb that had been incubated with a 50-fold excess molar of HTKex-Fc (lower column). (B) Proteins in the cell lysates of surface-biotinylated cell lines were immunoprecipitated with 38-1E. Immune complexes were separated by SDS-PAGE (10% polyacrylamide) under reducing conditions, transferred, and probed with HRP-conjugated streptavidin. The positions of the molecular mass markers (in kilodaltons) are indicated on the left.

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