Human Anti-ERBB2 Recombinant Antibody (clone FWP51) (CAT#: FAMAB-1130CQ)

Figure 1 Binding of specific mAbs to the erbB-2 protein from tunicamycin-treated SKBR3 cells.

In lane 1 lysates from control SKBR3 cells were immunoprecipitated with 21N serum; in lanes 3,5, 7, and 9 lysates were immunoprecipitated with, respectively, mAbsFRP5, FSP16, FWP51, and FSP77. In lane 2 lysates from tunicamycin-treated SKBR3 cells were immunoprecipitated with 21N serum; in lanes 4,6,8, and 10, lysates from tunicamycin-treated cells were immunoprecipitated with, respectively, mAbs FRP5, FSP16,FWP51, and FSP77. The precipitated proteins were electrophoresed,electroblotted, and the erbB-2 protein detected with 21N serum followed by 125I-protein A treatment of the filter. The positions of the glycosylated p185 erbB-2 protein and the unglycosylated p170 erbB2 protein are indicated.

Harwerth, I. M., Wels, W., Marte, B. M., & Hynes, N. E. (1992). Monoclonal antibodies against the extracellular domain of the erbB-2 receptor function as partial ligand agonists. Journal of Biological Chemistry, 267(21), 15160-15167.

Figure 2 Antibody-induced tyrosine phosphorylation of the erbB-2 protein in in vivo cultured cells.

SKRR3 cells (panels A and B) or HC11 clone R11 cells (panel C) were incubated for 15min at 37°C with 10 ug/ml of mAb FRP5, FSP16, FWP51, and FSP77 (A and R, lanes 2-5; C, lanes 3-6). In panels A and B, lane I, the cells were left untreated; in panel C, lanes 1 and 2, cells were incubated, respectively, 10 min at 37°C with 100 ng/ml EGF or left untreated. Equal amounts of cell lysates were analyzed on SDSPAGE. The phosphotyrosine was detected with a specific mAb (panels A and C), the erbB-2 was detected with 21N antiserum (panel B), and the filters were treated with 125I-protein A. The amount of radioactivity in each band was quantitated with a phosphoimager.The positions of the p185 erbB-2 receptor and the p170 EGF receptor are indicated.

Harwerth, I. M., Wels, W., Marte, B. M., & Hynes, N. E. (1992). Monoclonal antibodies against the extracellular domain of the erbB-2 receptor function as partial ligand agonists. Journal of Biological Chemistry, 267(21), 15160-15167.