In this task, you're given a paragraph and title from the research paper. Your task is to classify whether the given title is suitable or not for the research paper based on the given paragraph. Return "True" if title is proper according to paragraph else "False".
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Question: Paragraph: Secretion of a recombinant protein from the yeast Pichia pastoris requires the presence of a signal peptide at the amino terminus. Maintaining the full amino acid sequence of the signal peptide is thought to be important for proper signal processing and protein secretion. We show that at least for one protein, a synthetic human interferon, the presence of a Gateway recombination site within the signal peptide is fully compatible with high levels of protein secretion. The amino termini of the secreted interferon proteins cloned with Gateway and cloned with restriction enzymes and ligase are identical, and the proteins were highly active in biological assays. Compatibility with Gateway cloning simpliWes construction of plasmids directing secretion of recombinant proteins from P. pastoris.
Title: Gateway cloning is compatible with protein secretion from Pichia pastoris

Answer: False

Question: Paragraph: For the purpose of this work, insect biotechnology, which is also known as yellow biotechnology, is the use of insects as well as insect-derived cells or molecules in medical (red biotechnology), agricultural (green biotechnology), and industrial (white) biotechnology. It is based on the application of biotechnological techniques on insects or their cells to develop products or services for human use. Such products are then applied in agriculture, medicine, and industrial biotechnology. Insect biotechnology has proven to be a useful resource in diverse industries, especially for the production of industrial enzymes including chitinases and cellulases, pharmaceuticals, microbial insecticides, insect genes, and many other substances. Insect cells (ICs), and particularly lepidopteran cells, constitute a competitive strategy to mammalian cells for the manufacturing of biotechnology products. Among the wide range of methods and expression hosts available for the production of biotech products, ICs are ideal for the production of complex proteins requiring extensive posttranslational modifi cation. The progress so far made in insect biotechnology essentially derives from scientifi c breakthroughs in molecular biology, especially with the advances in techniques that allow genetic manipulation of organisms and cells. Insect biotechnology has grown tremendously in the last 30 years.
Title: Insect Biotechnology

Answer: False

Question: Paragraph: Previously described polyclonal or monoclonal antibodies (mAb) to rabbit CD5, raised against expressed recombinant protein or peptides, recognize CD5 on most rabbit B cells. The mAb KEN-5 was originally reported to recognize rabbit CD5. However, KEN-5 binds almost exclusively to T cells and only to a minor population of B cells. We show here that by Enzyme-linked Immunosorbent Assay (ELISA), KEN-5 binds to recombinant rabbit CD5. This interaction is partially inhibited by polyclonal goat anti-CD5 antibody. In addition, immunoprecipitations from lysates of surface biotinylated rabbit lymphocytes with KEN-5 or our anti-CD5 mAb isolate molecules that migrate identically on gels with the same approximate relative molecular mass of 67,000 M r . By flow cytometric analyses of individual cells from spleen, thymus and appendix, KEN-5 recognizes CD5like molecules mainly on T cells and on 3-6% of IgM + B cells. Immunohistochemical staining of splenic and appendix tissues and confocal immunofluorescent imaging confirm and extend results from flow cytometric analyses. Quantitation of fluorescent colocalization indicates that staining by KEN-5 colocalizes with staining by anti-CD5 on small percentages lymphocytes in splenic tissue sections. As CD5 has both N-and O-linked glycosylation, we hypothesised that differential binding of KEN-5 to T cells and B-cells may be explained by different glycan structures on the CD5 present on T compared to B cells. This hypothesis is supported by ELISA data that show that deglycosylation diminishes the binding of KEN-5 to recombinant rabbit CD5. Screening KEN-5 on an array with 406 glycans was inconclusive. Although we did not identify a strongly binding glycan structure, the data are suggestive that the epitope recognized by KEN-5 may be influenced by glycan structures. The epitope this mAb recognizes may either be the glycan itself, or more likely, is influenced by neighboring glycan structure. Our findings suggest that development, selection and function of different B-and T-cell subsets or their preferential survival may be directly or indirectly dependent on different glycan structures associated with CD5 or CD5-like molecules expressed on T cells compared to B cells.
Title: Characterization of Rabbit CD5 Isoforms NIH Public Access Author Manuscript

Answer:
True