Wikipedia:Good article reassessment/Antibody/1

Antibody

 * • [//en.wikipedia.org/w/index.php?title=Wikipedia:Good_article_reassessment/Antibody/1&action=watch Watch article reassessment page] • GAN review not found
 * Result: No significant improvement, even giving the extra allotted time. Delisted. AirshipJungleman29 (talk) 22:10, 2 March 2023 (UTC)

There's lots of uncited material including And more. These will all need to be cited. Onegreatjoke (talk) 21:08, 9 February 2023 (UTC)
 * "In the framework of the immune network theory, CDRs are also called idiotypes. According to immune network theory, the adaptive immune system is regulated by interactions between idiotypes."
 * The protein structure section
 * Antibodies also form complexes by binding to antigen: this is called an antigen-antibody complex or immune complex. Small antigens can cross-link two antibodies, also leading to the formation of antibody dimers, trimers, tetramers, etc. Multivalent antigens (e.g., cells with multiple epitopes) can form larger complexes with antibodies. An extreme example is the clumping, or agglutination, of red blood cells with antibodies in the Coombs test to determine blood groups: the large clumps become insoluble, leading to visually apparent precipitation.
 * Each antibody contains two identical light chains: both κ or both λ. Proportions of κ and λ types vary by species and can be used to detect abnormal proliferation of B cell clones. Other types of light chains, such as the iota (ι) chain, are found in other vertebrates like sharks (Chondrichthyes) and bony fishes (Teleostei).
 * The entire Antibody–antigen interactions section.
 * Being able to control the combinational design of the sequence and three-dimensional space could transcend the natural design and allow for the attachment of different combinations of drugs to the arms. Heterodimeric antibodies have a greater range in shapes they can take and the drugs that are attached to the arms don't have to be the same on each arm, allowing for different combinations of drugs to be used in cancer treatment. Pharmaceuticals are able to produce highly functional bispecific, and even multispecific, antibodies. The degree to which they can function is impressive given that such a change of shape from the natural form should lead to decreased functionality.