Journal: BMC Biotechnology

Article Title: Efficient and reproducible generation of high-expressing, stable human cell lines without need for antibiotic selection

doi: 10.1186/1472-6750-8-13

Figure Lengend Snippet: Expression of hAAT protein . Western Blot analyses for hAAT protein expressed in 10 E1-transformed amniocyte cell pools. (A) For detection of secreted hAAT, proteins in the cell culture medium were fractionated on a SDS-containing polycrylamide gel. (B) For detection of intracellular hAAT, cells were lysed and proteins were separated on a SDS-containing polyacrylamide gel. Intracellular and secreted hAAT was visualized using a monoclonal anti-hAAT antibody. For control proteins from untransformed amniocytes and hAAT purified from human plasma were used.

Article Snippet: As positive control, hAAT purified from human plasma (ICN Biomedicals) was used.

Techniques: Expressing, Western Blot, Transformation Assay, Cell Culture, Control, Purification, Clinical Proteomics

Journal: BMC Biotechnology

Article Title: Efficient and reproducible generation of high-expressing, stable human cell lines without need for antibiotic selection

doi: 10.1186/1472-6750-8-13

Figure Lengend Snippet: Glycoanalyses of hAAT . Proteins from cell culture medium of amniocyte cell pool Z171-5A were treated with increasing amounts of (A) PNGaseF or with (B) Neuraminidase and fractionated on SDS-containing polyacrylamide gels. Upon transfer on nitrocellulose Western Blot analyses were performed using a monoclonal anti-hAAT antibody. For controls hAAT purified from human plasma was used. (C) A- and B-type oligosaccharide chains of hAAT and cut positions of PNGaseF and Neuraminidase.

Article Snippet: As positive control, hAAT purified from human plasma (ICN Biomedicals) was used.

Techniques: Cell Culture, Western Blot, Purification, Clinical Proteomics