Enhancement of hybridoma formation, clonability and cell proliferation in a nanoparticle-doped aqueous environment-4

<p><b>Copyright information:</b></p><p>Taken from "Enhancement of hybridoma formation, clonability and cell proliferation in a nanoparticle-doped aqueous environment"</p><p>http://www.biomedcentral.com/1472-6750/8/3</p><p>BMC Biotechnology 2008;8():3-3.</p><p>Published online 14 Jan 2008</p><p>PMCID:PMC2254390.</p><p></p>m powder forms with either NPD or DI water. For each fusion, PBMC from a single batch were divided into two equal fractures and used to prepare two parallel experiments, in NPD or DI based reagents. The figure presents percent of hybridoma-positive wells in each fusion experiment. The percent was calculated as the number of hybridoma-positive wells from 96-well plates where the cells were seeded and grown after the fusion process. The difference between the NPD- and DI-fusion results was found to be statistically significant by Chi-square analysis (

Enhancement of hybridoma formation, clonability and cell proliferation in a nanoparticle-doped aqueous environment-2

<p><b>Copyright information:</b></p><p>Taken from "Enhancement of hybridoma formation, clonability and cell proliferation in a nanoparticle-doped aqueous environment"</p><p>http://www.biomedcentral.com/1472-6750/8/3</p><p>BMC Biotechnology 2008;8():3-3.</p><p>Published online 14 Jan 2008</p><p>PMCID:PMC2254390.</p><p></p>in NPD and the other in DI medium and both were kept in standard culture conditions. After a week of growth the supernatants were collected, and the antibody concentrations were measured by a standard sandwich ELISA. Each column represents the mean antibody concentration that was measured in NPD and DI cultures. The error bars denote the standard error of the means. We have observed increased secretion of monoclonal antibody with a series of stable hybridoma clones and presented a detailed analysis with one of them in this manuscript. Panel A: Total antibody concentration measured in the culture supernatants; Panel B: Antibody concentration normalized per cell

Enhancement of hybridoma formation, clonability and cell proliferation in a nanoparticle-doped aqueous environment-3

<p><b>Copyright information:</b></p><p>Taken from "Enhancement of hybridoma formation, clonability and cell proliferation in a nanoparticle-doped aqueous environment"</p><p>http://www.biomedcentral.com/1472-6750/8/3</p><p>BMC Biotechnology 2008;8():3-3.</p><p>Published online 14 Jan 2008</p><p>PMCID:PMC2254390.</p><p></p>ased medium supplemented with 3% FCS. Before seeding the cells were washed in serum-free media to verify the removal of any residual serum. During a period of two weeks the supernatants were collected as indicated and the cells were counted on the same day. The cultures were fed on the 4and 10day and medium was placed in the cultures on day 6. Although the cells in DI culture proliferated normally under these conditions, they failed to produce measurable quantities of antibody. Panel A: IgM production per hybridoma cell in 3% FCS; Panel B: Number of live cells at each antibody titration

A human monoclonal autoantibody to breast cancer identifies the PDZ domain containing protein GIPC1 as a novel breast cancer-associated antigen-4

S analyzed by confocal microscopy and indicates that the target antigen is present in the membrane and cytoplasm. Staining of human breast cancer tissue was analyzed by standard fluorescent microscopy.<p><b>Copyright information:</b></p><p>Taken from "A human monoclonal autoantibody to breast cancer identifies the PDZ domain containing protein GIPC1 as a novel breast cancer-associated antigen"</p><p>http://www.biomedcentral.com/1471-2407/8/248</p><p>BMC Cancer 2008;8():248-248.</p><p>Published online 24 Aug 2008</p><p>PMCID:PMC2529336.</p><p></p

A human monoclonal autoantibody to breast cancer identifies the PDZ domain containing protein GIPC1 as a novel breast cancer-associated antigen-3

St epithelium cell line HBL100 and breast cancer cell lines MCF-7, T47D, SK-BR-3, MDA231, MDA157 and MDA453. A probe for the GAPDH gene was used to normalize expression. Panel B: Densitometry analysis of the Northern blot was performed to quantitate the mRNA expression. The data indicates that the GIPC1 gene is upregulated in breast cancer cell lines.<p><b>Copyright information:</b></p><p>Taken from "A human monoclonal autoantibody to breast cancer identifies the PDZ domain containing protein GIPC1 as a novel breast cancer-associated antigen"</p><p>http://www.biomedcentral.com/1471-2407/8/248</p><p>BMC Cancer 2008;8():248-248.</p><p>Published online 24 Aug 2008</p><p>PMCID:PMC2529336.</p><p></p

A human monoclonal autoantibody to breast cancer identifies the PDZ domain containing protein GIPC1 as a novel breast cancer-associated antigen-2

This suggests that two populations of GIPC1 molecules exist in these cells and may be related to the protein doublet identified by Western blot analysis in Figure 2.<p><b>Copyright information:</b></p><p>Taken from "A human monoclonal autoantibody to breast cancer identifies the PDZ domain containing protein GIPC1 as a novel breast cancer-associated antigen"</p><p>http://www.biomedcentral.com/1471-2407/8/248</p><p>BMC Cancer 2008;8():248-248.</p><p>Published online 24 Aug 2008</p><p>PMCID:PMC2529336.</p><p></p

A human monoclonal autoantibody to breast cancer identifies the PDZ domain containing protein GIPC1 as a novel breast cancer-associated antigen-0

S analyzed by confocal microscopy and indicates that the target antigen is present in the membrane and cytoplasm. Staining of human breast cancer tissue was analyzed by standard fluorescent microscopy.<p><b>Copyright information:</b></p><p>Taken from "A human monoclonal autoantibody to breast cancer identifies the PDZ domain containing protein GIPC1 as a novel breast cancer-associated antigen"</p><p>http://www.biomedcentral.com/1471-2407/8/248</p><p>BMC Cancer 2008;8():248-248.</p><p>Published online 24 Aug 2008</p><p>PMCID:PMC2529336.</p><p></p

A human monoclonal autoantibody to breast cancer identifies the PDZ domain containing protein GIPC1 as a novel breast cancer-associated antigen-1

displayed. Human Ig H and L chains are present in the tissue and are recognized by the secondary anti-human antiserum. The target antigen is detected as a doublet in both the breast cancer tissue and SK-BR-3 cell line but is not detected in normal breast tissue. Both bands in the doublet are present in all breast cancer cell lines analyzed by Western blot but their intensity is variable. B. Immunoblotting with 27.B1 antibody of total cell lysates prepared from SK-BR-3 cells. 27.B1 antibody was preincubated with recombinant GIPC1 protein prior to blotting (lane 1), and compared to non-preincubated control (lane 2).<p><b>Copyright information:</b></p><p>Taken from "A human monoclonal autoantibody to breast cancer identifies the PDZ domain containing protein GIPC1 as a novel breast cancer-associated antigen"</p><p>http://www.biomedcentral.com/1471-2407/8/248</p><p>BMC Cancer 2008;8():248-248.</p><p>Published online 24 Aug 2008</p><p>PMCID:PMC2529336.</p><p></p