Mouse Anti-EPCAM Recombinant Antibody (clone M79) (CAT#: HPAB-S0025-YC)

Figure 1 Isolation of proteins from cell and tissue lysates by affnity chromatography using M79- and Con A-sepharose columns.

By affnity chromatography using M79-sepharose column, a 33-kDa protein (P33) was isolated from HCT cell lysates. Moreover, a 50-kDa protein (P50) was isolated from lysates of human colorectal tumor tissues. A 65-kDa protein (P65) was also found by affnity chromatography using Con A-sepharose column and then M79-sepharose column.

Chen, Y. H., Yu, T., Bai, Y., & Zhao, N. (1999). Two proteins share immunological epitopes on the tumor-associated antigen 17-1A. Cancer letters, 144(1), 101-105.

Figure 2 Identification of interaction of mAbs 17-1A and M79 with the isolated proteins by ELISA.

a: A, mAb 17-1A binding to P33; B, mAb M79 binding to P33. b: A, mAb 17-1A binding to P50; B, mAb M79 binding to P50. c: mAb 17-1A binding to P65; B, mAb M79 binding to P65. Control: gelatine instead of these antigens by coating the microtiter plate.

Chen, Y. H., Yu, T., Bai, Y., & Zhao, N. (1999). Two proteins share immunological epitopes on the tumor-associated antigen 17-1A. Cancer letters, 144(1), 101-105.

Figure 3 Inhibition of mAb 17-1A (a) and M79 (b) binding to HT-29 cells by P50, in flow cytometry analysis.

P50 showed an enhancement effect on the binding of both mAbs.

Chen, Y. H., Yu, T., Bai, Y., & Zhao, N. (1999). Two proteins share immunological epitopes on the tumor-associated antigen 17-1A. Cancer letters, 144(1), 101-105.

Figure 4 Inhibition of mAb 17-1A (a) and M79 (b) binding to HT-29 cells by P65, in flow cytometry analysis.

P65 did not inhibit the binding of mAb 17-1A to HT-29 cells, and on the contrary, could weakly up-modulate the binding of M79.

Chen, Y. H., Yu, T., Bai, Y., & Zhao, N. (1999). Two proteins share immunological epitopes on the tumor-associated antigen 17-1A. Cancer letters, 144(1), 101-105.