Tumor-infiltrating B lymphocytes as an efficient source of highly specific immunoglobulins recognizing tumor cells-3

<p><b>Copyright information:</b></p><p>Taken from "Tumor-infiltrating B lymphocytes as an efficient source of highly specific immunoglobulins recognizing tumor cells"</p><p>http://www.biomedcentral.com/1472-6750/7/70</p><p>BMC Biotechnology 2007;7():70-70.</p><p>Published online 18 Oct 2007</p><p>PMCID:PMC2175506.</p><p></p>y genes. Corresponding PEG-purified phage was used as positive control (). The irrelevant anti-SP2 antibody gene of known origin, selected earlier from scFvEC23 library, was also tested

Tumor-infiltrating B lymphocytes as an efficient source of highly specific immunoglobulins recognizing tumor cells-5

<p><b>Copyright information:</b></p><p>Taken from "Tumor-infiltrating B lymphocytes as an efficient source of highly specific immunoglobulins recognizing tumor cells"</p><p>http://www.biomedcentral.com/1472-6750/7/70</p><p>BMC Biotechnology 2007;7():70-70.</p><p>Published online 18 Oct 2007</p><p>PMCID:PMC2175506.</p><p></p>ained with MIX7, MIX17 and MIX39 soluble antibodies and an irrelevant anti-SP2 antibody. Intensive staining tumor tissues were observed for all selected antibodies. MIX39 slightly stains matched normal breast tissue of patient B93

Tumor-infiltrating B lymphocytes as an efficient source of highly specific immunoglobulins recognizing tumor cells-7

<p><b>Copyright information:</b></p><p>Taken from "Tumor-infiltrating B lymphocytes as an efficient source of highly specific immunoglobulins recognizing tumor cells"</p><p>http://www.biomedcentral.com/1472-6750/7/70</p><p>BMC Biotechnology 2007;7():70-70.</p><p>Published online 18 Oct 2007</p><p>PMCID:PMC2175506.</p><p></p>gative control MCF10-2A cells was observed (data not shown)

Tumor-infiltrating B lymphocytes as an efficient source of highly specific immunoglobulins recognizing tumor cells-1

<p><b>Copyright information:</b></p><p>Taken from "Tumor-infiltrating B lymphocytes as an efficient source of highly specific immunoglobulins recognizing tumor cells"</p><p>http://www.biomedcentral.com/1472-6750/7/70</p><p>BMC Biotechnology 2007;7():70-70.</p><p>Published online 18 Oct 2007</p><p>PMCID:PMC2175506.</p><p></p>tive proteins. Data reported are the average values of assays performed in duplicate. Several irrelevant proteins and an anti-SP2 irrelevant phage antibody [35] are included as negative controls

Tumor-infiltrating B lymphocytes as an efficient source of highly specific immunoglobulins recognizing tumor cells-8

<p><b>Copyright information:</b></p><p>Taken from "Tumor-infiltrating B lymphocytes as an efficient source of highly specific immunoglobulins recognizing tumor cells"</p><p>http://www.biomedcentral.com/1472-6750/7/70</p><p>BMC Biotechnology 2007;7():70-70.</p><p>Published online 18 Oct 2007</p><p>PMCID:PMC2175506.</p><p></p>5, B87, B89, B90, B91, B92, B93, B95, B96), normal breast, normal testis and peripheral blood lymphocytes from four healthy donors (L1, L2, L3, L4), was used, as template for amplification of V(D)J antibody regions. Samples of cDNA were normalized by amplification of β-actin housekeeping gene. All V(D)J fragments were well-amplified and gave DNA bands of expected molecular weight in all cases, excluding normal testis cDNA sample. The same PCR products were fractionated by 10% PAGE, giving a higher resolution of DNA bands. Antibody subclass distribution. PCR-amplified normal breast and B84 cDNA samples not showing oligoclonal bands in V(D)J test, have prevalence of IgA bands in comparison to IgG1 and IgG2 (), while three samples, B91, B92 and B93, giving strong oligoclonal bands in previous test, have IgG1 or both IgG1 and IgG2 band prevalence in comparison with IgA (). Clonality of heavy chain antibodies derived from B92 and B93 cDNA samples. Amino acid sequences of variable regions of 30 clones were deduced from randomly sequenced γ-chain antibody genes derived from B92 and B93 cDNA. Peptide sequences are reported in single-letter code. Identical amino acids in similar clones are represented by a dash

Tumor-infiltrating B lymphocytes as an efficient source of highly specific immunoglobulins recognizing tumor cells-4

<p><b>Copyright information:</b></p><p>Taken from "Tumor-infiltrating B lymphocytes as an efficient source of highly specific immunoglobulins recognizing tumor cells"</p><p>http://www.biomedcentral.com/1472-6750/7/70</p><p>BMC Biotechnology 2007;7():70-70.</p><p>Published online 18 Oct 2007</p><p>PMCID:PMC2175506.</p><p></p>ells. No staining is observed with the negative control (irrelevant anti-SP2 antibody). Staining of breast carcinoma cells in comparison with normal breast epithelial cells MCF10-2A. The selected antibodies stain the non-fixed cells more intensively than the fixed MCF7 cells, but not the MCF10-2A cells. Weak background is observed only for MIX39 scFv when it interacts with MCF10-2A cells. No staining is observed for negative control anti-SP2 antibody. Staining non-fixed MCF7 cells, magnification ×60

Tumor-infiltrating B lymphocytes as an efficient source of highly specific immunoglobulins recognizing tumor cells-0

<p><b>Copyright information:</b></p><p>Taken from "Tumor-infiltrating B lymphocytes as an efficient source of highly specific immunoglobulins recognizing tumor cells"</p><p>http://www.biomedcentral.com/1472-6750/7/70</p><p>BMC Biotechnology 2007;7():70-70.</p><p>Published online 18 Oct 2007</p><p>PMCID:PMC2175506.</p><p></p>5, B87, B89, B90, B91, B92, B93, B95, B96), normal breast, normal testis and peripheral blood lymphocytes from four healthy donors (L1, L2, L3, L4), was used, as template for amplification of V(D)J antibody regions. Samples of cDNA were normalized by amplification of β-actin housekeeping gene. All V(D)J fragments were well-amplified and gave DNA bands of expected molecular weight in all cases, excluding normal testis cDNA sample. The same PCR products were fractionated by 10% PAGE, giving a higher resolution of DNA bands. Antibody subclass distribution. PCR-amplified normal breast and B84 cDNA samples not showing oligoclonal bands in V(D)J test, have prevalence of IgA bands in comparison to IgG1 and IgG2 (), while three samples, B91, B92 and B93, giving strong oligoclonal bands in previous test, have IgG1 or both IgG1 and IgG2 band prevalence in comparison with IgA (). Clonality of heavy chain antibodies derived from B92 and B93 cDNA samples. Amino acid sequences of variable regions of 30 clones were deduced from randomly sequenced γ-chain antibody genes derived from B92 and B93 cDNA. Peptide sequences are reported in single-letter code. Identical amino acids in similar clones are represented by a dash

Selection, affinity maturation, and characterization of a human scFv antibody against CEA protein-0

<p><b>Copyright information:</b></p><p>Taken from "Selection, affinity maturation, and characterization of a human scFv antibody against CEA protein"</p><p>BMC Cancer 2006;6():41-41.</p><p>Published online 24 Feb 2006</p><p>PMCID:PMC1402309.</p><p>Copyright © 2006 Pavoni et al; licensee BioMed Central Ltd.</p>uration library was constructed by error-prone PCR method

Selection, affinity maturation, and characterization of a human scFv antibody against CEA protein-6

<p><b>Copyright information:</b></p><p>Taken from "Selection, affinity maturation, and characterization of a human scFv antibody against CEA protein"</p><p>BMC Cancer 2006;6():41-41.</p><p>Published online 24 Feb 2006</p><p>PMCID:PMC1402309.</p><p>Copyright © 2006 Pavoni et al; licensee BioMed Central Ltd.</p>of the negative control scFv directed to glucose oxidase

Selection, affinity maturation, and characterization of a human scFv antibody against CEA protein-8

<p><b>Copyright information:</b></p><p>Taken from "Selection, affinity maturation, and characterization of a human scFv antibody against CEA protein"</p><p>BMC Cancer 2006;6():41-41.</p><p>Published online 24 Feb 2006</p><p>PMCID:PMC1402309.</p><p>Copyright © 2006 Pavoni et al; licensee BioMed Central Ltd.</p