Each antibody contains a paratope that recognizes a specific epitope on an antigen, acting like a lock and key binding mechanism. This binding helps to eliminate antigens from the body, either by ...

An antibody is a Y-shaped protein produced by B cells of the immune system in response to exposure to antigens. The tip of each Y-shaped arm contains antigen binding sites (paratopes) that bind to a ...

In a significant step toward improving targeted cancer therapy, researchers from Japan have developed a novel nanocarrier ...

Each antibody molecule possesses distinct variable and constant regions. The variable region confers an antibody's antigen-binding specificity.

Predicting antibody-antigen interactions is based on predicting the antigen-antibody binding sites, differentiating the binders from non-binders, and deciphering the neutralization vs. non ...

Using secondary antibodies requires more steps and reagents, but increases sensitivity due to the signal amplification from multiple secondary antibodies binding to a single primary antibody.

In a paper published in Structure, Laustsen-Kiel’s team engineered pH-responsive human antibodies, known as acid-switched antibodies, that targeted snake venom toxins. 1 By exploiting pH-dependent ...

The antibody's binding sites, located at the ends of its arms, specifically recognize and attach to the unique regions of the antigens, called epitopes. This specific interaction is crucial for the ...

Monoclonal antibodies have specificity for a particular antigen (target of antibodies), but polyclonal ones are not specific to any antigen.

Antibodies are best known for their ability to latch onto and neutralize bacteria, viruses and other pathogens. But these immune proteins can do more than that: They also activate other components of ...

Determining these structural and functional aspects of antigen and antibody binding can allow researchers to pinpoint more powerful options for disease-fighting therapies.