Human Anti-MET Recombinant Antibody (clone 5D5) (CAT#: PABL-271)

Figure 1 MKN45 cells treated with 5 μg/ml of F46 or 5D5 were incubated for 24 h. c-Met degradation was measured by Western blot (A) and ELISA (B). Phosphorylation of c-Met and Akt in Caki-1 cells was measured by Western blot (C, E) and ELISA (D, F). Caki-1 cells were incubated for 30 min with 5 μg/ml of F46 or 5D5 or 100 ng/ml of HGF. The error bars indicate the mean ± SD of three independent experiments. Phosphorylation of c-Met downstream kinases in Caki-1 (G) and NCI-H441 (I) cells were measured by Western blot. Co-immunoprecipitation experiment showed induced binding between Gab1 and c-Met by 5D5, but not by F46 (H).

Oh, Y. M., Song, Y. J., Lee, S. B., Jeong, Y., Kim, B., Kim, G. W.,... & Nam, D. H. (2012). A new anti-c-Met antibody selected by a mechanism-based dual-screening method: therapeutic potential in cancer. Molecules and cells, 34(6), 523-529.

Figure 2 MKN45 cells were incubated with increasing amounts of recombinant human HGF. They were added with 0.5 μg of 5D5 or F46 followed by flow cytometry. ΔMFI (y-axis) indicates the decrease in percentage of mean fluorescence intensity (MFI) upon treatment with F46 or 5D5 (top). For the competition ELISA, biotinylated HGF and differing concentrations of IgG, F46, or free HGF were treated on c-Met coated plate (bottom).

Oh, Y. M., Song, Y. J., Lee, S. B., Jeong, Y., Kim, B., Kim, G. W.,... & Nam, D. H. (2012). A new anti-c-Met antibody selected by a mechanism-based dual-screening method: therapeutic potential in cancer. Molecules and cells, 34(6), 523-529.

Figure 3 A549, H441, and MDA-MB-435 cells were kept serum-free and treated with 10 μg/ml rSema or anti-Met 5D5-Fab.

The samples were immunoblotted with phospho-tyrosine, Met, phospho-MAPK, or MAPK antibodies.

Kong-Beltran, M., Stamos, J., & Wickramasinghe, D. (2004). The Sema domain of Met is necessary for receptor dimerization and activation. Cancer cell, 6(1), 75-84.

Figure 4 293 cells were transfected with the indicated constructs and analyzed by 4%–12% SDS-PAGE. Lysates were immunoprecipitated with anti-Met 5D5 antibody and immunoblotted with His antibody (top) and reprobed with Met C-12 antibody (bottom).

Kong-Beltran, M., Stamos, J., & Wickramasinghe, D. (2004). The Sema domain of Met is necessary for receptor dimerization and activation. Cancer cell, 6(1), 75-84.

Figure 5 rSema and anti-Met 5D5-Fab inhibit cell motility.

A: H441 cells were scraped on Day 0 and treated with increasing concentrations of rSema plus HGF in serum-free media. The scrapes were photographed on Day 0 and Day 1. A representative data set of three independent experiments is shown. B: H441 cells were scraped and treated with mock, rSema, or anti-Met 5D5-Fab in serum-free media over the course of 2 days. Photographs were taken on Day 0 and Day 2.

Kong-Beltran, M., Stamos, J., & Wickramasinghe, D. (2004). The Sema domain of Met is necessary for receptor dimerization and activation. Cancer cell, 6(1), 75-84.

Figure 6 Cell migration is inhibited by rSema and anti-Met 5D5-Fab.

Kong-Beltran, M., Stamos, J., & Wickramasinghe, D. (2004). The Sema domain of Met is necessary for receptor dimerization and activation. Cancer cell, 6(1), 75-84.

Figure 1 Human Anti-MET Recombinant Antibody (PABL-271) in SDS-PAGE

SDS-PAGE analysis of PABL-271 in non-reduced (Lane 1, 2 μg) and reduced (Lane 2, 2 μg) conditions.

Figure 2 Human Anti-MET Recombinant Antibody (PABL-271) in HPLC

The purity of PABL-271 was greater than 95% as determined by SEC-HPLC.

Figure 3 Human Anti-MET Recombinant Antibody (PABL-271) in WB

Western blot analysis of PABL-271 was performed by loading recombinant human MET.

PABL-271 incubation concentration: 2 ng/μL.
The secondary antibody: HRP-anti-human IgG
Lane 1: Reduced Antigen (0.3 μg)
Lane 2: Reduced Antigen (0.6 μg)

Figure 4 Human Anti-MET Recombinant Antibody (PABL-271) in ELISA

ELISA analysis of PABL-271 was performed by coating with recombinant human MET.

The secondary antibody: HRP-anti-human IgG

Figure 5 Human Anti-MET Recombinant Antibody (PABL-271) in DB

Dot Blot analysis of PABL-271 was performed by coating with recombinant human MET.

The secondary antibody: HRP-anti-human IgG