More than 100 researchers from around the world have issued an initiative that could radically alter the way in which antibodies are studied. The article was published in the February 5th issue of the journal Nature (Nature).
Los Alamos National Laboratory (Los Alamos National Laboratory) researcher Andrew Bradbury said: "we put forward, like gene, antibody should also be to define the sequence of them, and they should be in the formation of recombinant cell lines."
To reference the antibodies used for each detection according to the sequence encoding of various subunits, concentration and standard experiment buffer them, can let the researchers around the world have the same affinity antibody can be used under the same conditions.
A sequence of antibodies or binding agents that is the ultimate "bar code" of the reagent, which ensures that everyone can use the same reagents to detect the same target. Deriving this bar code involves the selection of some antibodies from an in vitro library, or cloning and sequencing of antibody genes from hybridomas. This will require a major change in the mode of antibody supply.
Antibodies are a special class of proteins that help the body recognize and neutralize bacteria and other attacks on the immune system, and scientists have been using them as a specific binding agent. Antibody quality control and precise identification are the problems that researchers have been trying to solve with the need for sequencing and recombinant expression. Unlike antibodies to genes, oligonucleotides, plasmids, recombinant proteins, antibodies are the only widely used reagents in biological studies that have not been defined at the sequence level, Bradbury said.
The researchers noted that the quality of all antibodies varies greatly because of manufacturers, and that most antibodies are rarely tested and that differences between batches are very common.
Also, the quality of the documentation attached to the bulk product is also very different, and even the documentation provided often does not correspond to the batch to be supplied.
"In order to stop due to the lack of verification and identification of materials, researchers time and money wasted, we must define antibody according to their sequence, and to re production under standard conditions," the authors pointed out that. "Re production" here refers to the use of some methods that do not involve animal immunization to produce antibodies or other binding agents from scratch, rather than antibody produced by immunization.
For example, polyclonal antibodies are produced by injecting a protein into an animal's body and then extracting antibodies that are produced and carried in the blood of the animal that responds to the immune protein. Various antibodies are not highly accurate, and only 0.5-5% products are desired antibodies that can react to the initial target. The rest were antibodies originally present in the bloodstream of animals, indicating the animal's previous immune stress. By harvesting so many false antibodies aimlessly, some specific antibodies have been created, which has wasted research.
"We suggest using an in vitro method to generate antibodies so that animals are not needed at all and, importantly, molecules that have known sequences are generated directly," Bradbury said.