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ARS Home » Northeast Area » Beltsville, Maryland (BHNRC) » Beltsville Human Nutrition Research Center » Diet, Genomics and Immunology Laboratory » Research » Publications at this Location » Publication #188184

Title: PRODUCTION OF RECOMBINANT ANTIBODIES FOR LOW-ABUNDANCE PROTEINS

Author
item Cao, Heping
item Anderson, Richard
item BLACKSHEAR, PERRY - DHHS-NIH-NIEHS-LN, NC

Submitted to: Protein Engineering
Publication Type: Abstract Only
Publication Acceptance Date: 3/13/2006
Publication Date: 4/26/2006
Citation: Cao, H., Anderson, R.A., Blackshear, P.J. 2006. Current issues in Protein Engineering. [CD-ROM] In: Production of Recombinant Antibodies For Low-abundance proteins. Protein Engineering.

Interpretive Summary:

Technical Abstract: Production of high quality antibodies is extremely important for the detection of low abundance proteins. Tristetraprolin (TTP), an anti-inflammatory protein, is such a very low-abundance protein in normal cells and tissues. Numerous laboratories and a few companies have produced TTP antibodies, but they are largely ineffective in detecting this protein in endogenous sources. We have raised TTP antibodies against recombinant proteins. These antibodies have been used successfully in the study of this protein by immunoblotting, immunoprecipitation, and immunocytochemistry procedures. (References: 1)Cao H, Tuttle JS, Blackshear PJ (2004) Immunological characterization of tristetraprolin as a low abundance, inducible, stable cytosolic protein. Journal of Biological Chemistry, 279: 21489-21499; 2)Cao H (2004) Expression, purification, and biochemical characterization of the antiinflammatory tristetraprolin: a zinc-dependent mRNA binding protein affected by posttranslational modifications, Biochemistry, 43: 13724-13738; 3)Cao H, Deterding LJ, Venable JD, Kennington EA, Yates, JR 3rd, Tomer KB, Blackshear PJ (2005) Identification of the anti-inflammatory protein tristetraprolin as a hyperphosphorylated protein by mass spectrometry and site-directed mutagenesis, Biochemical Journal Immediate Publication 20051316).