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Antibody Engineering: Methods and Protocols 2004 Edition
Contributor(s): Lo, Benny K. C. (Editor)
ISBN: 1588290921     ISBN-13: 9781588290922
Publisher: Humana
OUR PRICE:   $161.49  
Product Type: Hardcover - Other Formats
Published: December 2003
Qty:
Annotation: A core collection of diverse cutting-edge techniques for the generation, expression, optimization, and characterization of recombinant antibodies. Readily reproducible protocols for lead generation range from the cloning of human immunoglobulin genes to the selection and generation of human recombinant antibodies by humanization approaches, molecular display technologies and transgenic animals. Procedures are also described on restructuring antibody leads into monovalent, multivalent, and bispecific binding fragments for a wide variety of in vivo applications. State-of-the-art technologies are described for the characterization of antigen-binding affinity and specificity with novel applications in radioimmunotargeting, cancer immunotherapy, drug abuse, and proteomics.
Additional Information
BISAC Categories:
- Medical | Biochemistry
- Medical | Microbiology
- Science | Life Sciences - Molecular Biology
Dewey: 616.079
LCCN: 2003020281
Series: Methods in Molecular Biology
Physical Information: 1.2" H x 6.28" W x 9.22" (1.97 lbs) 562 pages
 
Descriptions, Reviews, Etc.
Publisher Description:
The exquisite binding specificity of antibodies has made them valuable tools from the laboratory to the clinic. Since the description of the murine hybridoma technology by K hler and Milstein in 1975, a phenomenal number of mo- clonal antibodies have been generated against a diverse array of targets. Some of these have become indispensable reagents in biomedical research, while others were developed for novel therapeutic applications. The attractiveness of an- bodies in this regard is obvious--high target specificity, adaptability to a wide range of disease states, and the potential ability to direct the host's immune s- tem for a therapeutic response. The initial excitement in finding Paul Ehrlich's "magic bullet," however, was met with widespread disappointment when it was demonstrated that murine antibodies frequently elicit the human anti-murine an- body (HAMA) response, thus rendering them ineffective and potentially unsafe in humans. Despite this setback, advances in recombinant DNA techniques over the last 15-20 years have empowered the engineering of recombinant antibodies with desired characteristics, including properties to avoid HAMA. The ability to p- duce bulk quantities of recombinant proteins from bacterial fermentation also fueled the design of numerous creative antibody constructs. To date, the United States Food and Drug Administration has approved more than 10 recombinant antibodies for human use, and hundreds more are in the development pipeline. The recent explosion in genomic and proteomic information appears ready to deliver many more disease targets amenable to antibody-based therapy.