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Results: 6

1.
Figure 5

Figure 5. From: Reevaluation of the 22-1-1 antibody and its putative antigen, EBAG9/RCAS1, as a tumor marker.

Endogenous expression of EBAG9 in cancer cell lines. Cells were lysed in NP-40 buffer and 50 μg of total protein was separated by SDS-PAGE and analysed by immunoblot using our polyclonal anti-EBAG9 antibody. α-actin served as control indicating protein load.

Tatiana A Reimer, et al. BMC Cancer. 2005;5:47-47.
2.
Figure 3

Figure 3. From: Reevaluation of the 22-1-1 antibody and its putative antigen, EBAG9/RCAS1, as a tumor marker.

Subcellular localization of EBAG9 analysed by electron microscopy. Immunogold labeling of HEK293 A cells. EBAG9-GFP is found in Golgi cisternae and small vesicles in stably transfected cells. a) small vesicles surrounding the Golgi apparatus, b) Golgi stacks, c) control-non transfected cells. Bar; 0.5 μm.

Tatiana A Reimer, et al. BMC Cancer. 2005;5:47-47.
3.
Figure 1

Figure 1. From: Reevaluation of the 22-1-1 antibody and its putative antigen, EBAG9/RCAS1, as a tumor marker.

Examples of the different immunostaining patterns obtained using the antibody clones 22-1-1 and Ab-1 in normal glandular tissues. Mucosa of the corpus of stomach (a, b; magnification × 10) and (c, d; magnification × 45). Colonic mucosa (e, f; magnification × 25), (g; magnification × 60) and (h; magnification × 50). Prostatic glands (i; magnification × 60) and (j; magnification × 50).

Tatiana A Reimer, et al. BMC Cancer. 2005;5:47-47.
4.
Figure 2

Figure 2. From: Reevaluation of the 22-1-1 antibody and its putative antigen, EBAG9/RCAS1, as a tumor marker.

Examples of the different immunostaining patterns obtained using the antibody clones 22-1-1 and Ab-1 in various adenocarcinomas. Signet ring cell gastric carcinoma (a, b; magnification × 80). Colorectal adenocarcinoma (c, d; magnification × 60). Lymph node metastasis (e, f; magnification × 50). Prostatic adenocarcinoma (g; magnification × 60) and (h; magnification × 50): Adenocarcinoma of the lung (i, j; magnification × 60).

Tatiana A Reimer, et al. BMC Cancer. 2005;5:47-47.
5.
Figure 4

Figure 4. From: Reevaluation of the 22-1-1 antibody and its putative antigen, EBAG9/RCAS1, as a tumor marker.

EBAG9 is sensitive to treatment with BFA and nocodazole. Displacement of EBAG9 from Golgi structures upon treatment with BFA. Cells stably transfected with EBAG9-GFP were left untreated (w/o) (a, b, c), incubated for 15 min (d, e, f) and 60 min (g, h, i) with BFA (5 μg/ml) or with nocodazole -Noc (10 μg/ml) (m, n, o) for 2 h. Cells were fixed and stained with anti-mannosidase and anti-TGN38 antibodies (red). Merged image, yellow. Bar; 10 μm

Tatiana A Reimer, et al. BMC Cancer. 2005;5:47-47.
6.
Figure 6

Figure 6. From: Reevaluation of the 22-1-1 antibody and its putative antigen, EBAG9/RCAS1, as a tumor marker.

The 22-1-1 antigen does not induce apoptosis in K562 cells. a) Cells were irradiated with UV-light as positive control for apoptosis, or incubated with regular non concentrated medium, or 1:4 dilution of concentrated regular medium, or concentrated MCF-7 cell culture supernatant. Apoptosis was assessed by annexin V-FITC staining. b) K562 cells were incubated with 50 μg, or 100 μg of (1) TF; (2) α-GalNAc-PAA; (3) β-GlcNAc-PAA; (4) β-GalNAc-PAA-biotin and subjected to caspase -3 and -7 activity assay. P-cells irradiated with UV; N-non treated cells.

Tatiana A Reimer, et al. BMC Cancer. 2005;5:47-47.

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