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Analytical Chemistry

Call For Antibody Standardization

Reproducibility: All antibody reagents should be sequenced and then produced from the genetic code obtained, scientists say

by Celia Henry Arnaud
February 4, 2015

CORRECTION: This story was updated on Feb. 5, 2015, to correct the timing of when the Global Biological Standards Institute met. It met during the week the story published, not the previous week.

More than 100 scientists have signed a comment in Nature calling for the standardization of antibodies used as research reagents (2015, DOI: 10.1038/518027a). Poorly characterized reagents have contributed to the ongoing challenges with reproducibility in life sciences research (C&EN, Dec. 15, 2014, page 28).

Typically, antibody research reagents are mixtures of proteins with varying genetic sequences. Andrew Bradbury of Los Alamos National Laboratory, Andreas Plückthun of the University of Zurich, in Switzerland, and 110 other life scientists propose that all antibodies used as reagents be sequenced and that the genetic codes obtained be used to produce recombinant versions. To achieve these goals, the scientists call for an international collaboration and funding initiative to underwrite the necessary characterization.

They also call on the scientific leaders of the U.S. National Institutes of Health and the European Union’s funding agencies to convene various stakeholders to establish a realistic timeline for a transition to well-characterized reagents.

The scientists call on NIH to expand its Protein Capture Reagents Program, which was launched in 2010 to develop new methods of producing and validating reagents such as antibodies.

Hundreds of monoclonal and recombinant antibodies and new reagents have been produced as a result of the reagents program, an NIH spokesperson says. “The biggest problem that this program faces is low user interest. We are thus at a point where validation and comparative performance data are critical.”

In a separate effort, the Global Biological Standards Institute has convened a task force on research antibodies. It is meeting this week “to focus on the need for standards and best practices to advance the credibility, reproducibility, and translatability of preclinical research using antibodies,” Leonard P. Freedman, GBSI president, told C&EN.



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Max (February 11, 2015 12:49 PM)
This might be a naive question, but aren't a lot of antibodies glycosylated and isn't that important to their function? By making recombinant antibodies, isn't it possible that without significant work to figure out all the post-translational modifications that they may lose some function?

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