Literature DB >> 11861062

Myeloma expression systems.

Esther M Yoo1, Koteswara R Chintalacharuvu, Manuel L Penichet, Sherie L Morrison.   

Abstract

Myeloma expression systems have been utilized successfully for the production of various recombinant proteins. In particular, myeloma cell lines have been exploited to express a variety of different antibodies for diagnostic applications as well as in the treatment of various human diseases. The use of myeloma cells for antibody production is advantageous because they are professional immunoglobulin-secreting cells and are able to make proper post-translational modifications. Proper glycosylation has been shown to be important for antibody function. Advances in genetic engineering and molecular biology techniques have made it possible to isolate murine and human variable regions of almost any desired specificity. Antibodies and antibody variants produced in myeloma cells have been extremely helpful in elucidating the amino acid residues and structural motifs that contribute to antibody function. Because of their domain nature, immunoglobulin genes can be easily manipulated to produce chimeric or humanized antibodies. These antibodies are less immunogenic in humans and also retain their specificity for antigen and biologic properties. In addition, novel proteins in which antibodies are fused to non-immunoglobulin sequences as well as secretory IgA have been produced in myeloma cells.

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Year:  2002        PMID: 11861062     DOI: 10.1016/s0022-1759(01)00559-2

Source DB:  PubMed          Journal:  J Immunol Methods        ISSN: 0022-1759            Impact factor:   2.303


  7 in total

1.  Targeting HER2/neu with a fully human IgE to harness the allergic reaction against cancer cells.

Authors:  Tracy R Daniels; Richard K Leuchter; Rafaela Quintero; Gustavo Helguera; José A Rodríguez; Otoniel Martínez-Maza; Birgit C Schultes; Christopher F Nicodemus; Manuel L Penichet
Journal:  Cancer Immunol Immunother       Date:  2011-11-30       Impact factor: 6.968

Review 2.  Antibody-cytokine fusion proteins: applications in cancer therapy.

Authors:  Elizabeth Ortiz-Sánchez; Gustavo Helguera; Tracy R Daniels; Manuel L Penichet
Journal:  Expert Opin Biol Ther       Date:  2008-05       Impact factor: 4.388

3.  Toward more efficient protein expression: keep the message simple.

Authors:  Stephan Kalwy; James Rance; Robert Young
Journal:  Mol Biotechnol       Date:  2006-10       Impact factor: 2.695

4.  Restricted Proteolysis and LC-MS/MS To Evaluate the Orientation of Surface-Immobilized Antibodies.

Authors:  Min Shen; Di Jiang; P I Thilini De Silva; Boya Song; James F Rusling
Journal:  Anal Chem       Date:  2019-03-14       Impact factor: 6.986

5.  Structural correlates of mouse IgA allotypes.

Authors:  Julia M Phillips-Quagliata
Journal:  Immunogenetics       Date:  2009-12-15       Impact factor: 2.846

6.  Recombinant human heterodimeric IL-15 complex displays extensive and reproducible N- and O-linked glycosylation.

Authors:  M Thaysen-Andersen; E Chertova; C Bergamaschi; E S X Moh; O Chertov; J Roser; R Sowder; J Bear; J Lifson; N H Packer; B K Felber; G N Pavlakis
Journal:  Glycoconj J       Date:  2015-11-12       Impact factor: 2.916

Review 7.  Glycosylated Biotherapeutics: Immunological Effects of N-Glycolylneuraminic Acid.

Authors:  Sharon Yehuda; Vered Padler-Karavani
Journal:  Front Immunol       Date:  2020-01-23       Impact factor: 7.561

  7 in total

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