Figure 2
Figure 2. Identification of the CMV protein reactive with the CLL rAb CLL69D. (A) Time course experiment for presence of the 150-kDa CMV protein detected by CLL69D at early and late times during CMV infection of permissive cells. CMV-infected cells were harvested at 36 and 96 hours p.i. for Western blot analysis with the CLL rAbs CLL69D. A monoclonal Ab specific for pUL32 (α-pUL32) and CMV-negative serum (Se CMV−) served as positive and negative controls, respectively. (B) The CMV large structural phosphoprotein pUL32 (pp150) was generated recombinantly for Western blot analysis with the CLL rAb CLL69D. A monoclonal Ab specific for pUL32 (α-pUL32) and a humanized mouse monoclonal Ab of irrelevant specificity (4A5) served as positive and negative controls, respectively. Actin served as a loading control.

Identification of the CMV protein reactive with the CLL rAb CLL69D. (A) Time course experiment for presence of the 150-kDa CMV protein detected by CLL69D at early and late times during CMV infection of permissive cells. CMV-infected cells were harvested at 36 and 96 hours p.i. for Western blot analysis with the CLL rAbs CLL69D. A monoclonal Ab specific for pUL32 (α-pUL32) and CMV-negative serum (Se CMV−) served as positive and negative controls, respectively. (B) The CMV large structural phosphoprotein pUL32 (pp150) was generated recombinantly for Western blot analysis with the CLL rAb CLL69D. A monoclonal Ab specific for pUL32 (α-pUL32) and a humanized mouse monoclonal Ab of irrelevant specificity (4A5) served as positive and negative controls, respectively. Actin served as a loading control.

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