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New Line of Cancer Antibodies

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Western blot analysis of adult mouse brain untreated (lanes 1, 3, 5, & 7) or treated with lambda phosphatase (lanes 2, 4, 6, & 8). The blots were probed with rat monoclonal anti-EB3 (EM5091) (lanes 1 & 2), and rabbit polyclonals anti-EB3 (Ser-162) (lanes 3 & 4), anti-EB3 (Ser-176) (lanes 5 & 6), and anti-EB3 (a.a. 171-182) (lanes 7 & 8).
Western blot of EB proteins in mouse brain (lanes 1-5). The blot was probed with rat monoclonals EM5041 anti-EB1 (lane 1), EM5061 anti-EB1/2/3 (lane 2), EM5081 anti-EB2 (lane 3), EM5101 anti-EB3 (lane 4), and EM5091 anti-EB3 (lane 5). Then the antibodies were detected using goat anti-Rat IgG Light Chain specific:HRP (RS3121).
Western blot of EB proteins in mouse brain (lanes 1-5). The blot was probed with rat monoclonals EM5041 anti-EB1 (lane 1), EM5061 anti-EB1/2/3 (lane 2), EM5081 anti-EB2 (lane 3), EM5101 anti-EB3 (lane 4), and EM5091 anti-EB3 (lane 5). Then the antibodies were detected using goat anti-Rat IgG Light Chain specific:HRP (RS3121).Immunocytochemical labeling of EB3 in paraformaldehyde-fixed and NP40-permeabilized A431 cells. The cells were dual labeled with mouse monoclonal anti-α-Tubulin (TM4111) (green)  and rat monoclonal anti-EB3 (EM5091) (red). The antibodies were detected using either goat anti-mouse:DyLight® 488 (MS3011) or goat anti-Rat:DyLight® 594 (RS3111).
Western blot image of eEF2K in human A431 (lane 1), Jurkat (lane 2), and HeLa (lane 3) cells, and immunoprecipitation of eEF2K from HeLa cell lysate using anti-eEF2K (C-terminus) antibody (lanes 4 & 6). Negative control immunopreciptations with no antibody are shown in lane 5 and 7. The blots were probed with anit-eEF2K (C-terminus) (lanes 1-5) or with anti-eEF2K (N-terminal) antibody (lanes 6 & 7).Immunocytochemical labeling of eEF2K in paraformaldehyde fixed and NP-40 permeabilized A431 cells. The cells were labeled with rabbit polyclonal anti-eEF2K (EP4661). The antibody was detected using goat anti-rabbit DyLight® 594.
Western blot image of human A431 cells treated with Calyculin A (100 nM) for 30 min. Blot lanes were untreated (lanes 1, 3, & 5) or treated with lambda phosphatase (lanes 2, 4, & 6) then were probed with anti-EGFR (a.a. 961-972) (lanes 1 & 2), anti-EGFR (Ser-967) (lanes 3 & 4), and anti-EGFR (Ser-1142) (lanes 5 & 6).Immunocytochemical labeling in A431 cells untreated or treated with Calyculin A (50 nM) for 15 min. Cells were labeled with anti-EGFR (a.a. 961-972) or anti-EGFR (Ser-1142) antibodies. The specificity of labeling was demonstrated for each antibody by blocking the signals with their respective blocking peptides, EGFR (a.a. 961-972) (EX1875) and phospho-EGFR (Ser-1142) (EX1935).
Western blot analysis of human umbilical vein endothelial cells before (lanes 1, 3, 5) and after (lanes 2, 4, 6) treatment with lambda phosphatase. The blots were probed with anti-endothelial Nitric Oxide Synthase (eNOS) monoclonal antibody (lanes 1 & 2), anti-eNOS (Ser-632) phospho-specific antibody (lanes 3 & 4), and anti-eNOS polyclonal antibody (lanes 5 & 6).Immunocytochemical labeling of endothelial nitric oxide synthase (eNOS) in paraformaldehyde-fixed and NP-40-permeabilized human umbilical vein endothelial cells. The cells were labeled with mouse monoclonal eNOS (NM2211) and rabbit polyclonal eNOS (NP2281) antibodies, then the antibodies were detected using appropriate secondary antibodies conjugated to Cy3.
Western blot analysis of human umbilical vein endothelial cells treated with calyculin A (100 nM) for 30 min. (lanes 1, 3, 5 & 7) then the blots were treated with lambda phosphatase (lanes 2, 4, 6 & 8). The blots were probed with anti-endothelial nitric oxide synthase (eNOS) (C-terminal region) (lanes 1 & 2), anti-eNOS (Ser-632) (lanes 3 & 4), anti-eNOS (Ser-1177) (lanes 5 & 6) and anti-eNOS (a.a. 1172-1181) (lanes 7 & 8).
Western blot analysis of human umbilical vein endothelial cells before (lanes 1, 3, 5) and after (lanes 2, 4, 6) treatment with lambda phosphatase. The blots were probed with anti-endothelial Nitric Oxide Synthase (eNOS) monoclonal antibody (lanes 1 & 2), anti-eNOS (Ser-632) phospho-specific antibody (lanes 3 & 4), and anti-eNOS polyclonal antibody (lanes 5 & 6).Immunocytochemical labeling of endothelial nitric oxide synthase (eNOS) in paraformaldehyde-fixed and NP-40-permeabilized human umbilical vein endothelial cells. The cells were labeled with mouse monoclonal eNOS (NM2211) and rabbit polyclonal eNOS (NP2281) antibodies, then the antibodies were detected using appropriate secondary antibodies conjugated to Cy3.

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